Jump to content

TMEM202

From Wikipedia, the free encyclopedia
TMEM202
Identifiers
AliasesTMEM202, transmembrane protein 202
External IDsMGI: 1921143; HomoloGene: 52264; GeneCards: TMEM202; OMA:TMEM202 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

338949

73893

Ensembl

ENSG00000187806

ENSMUSG00000049526

UniProt

A6NGA9

Q80W35

RefSeq (mRNA)

NM_001080462

NM_178388

RefSeq (protein)

NP_001073931

NP_848475

Location (UCSC)Chr 15: 72.4 – 72.41 MbChr 9: 59.43 – 59.45 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
Transmembrane Protein 202
Identifiers
SymbolTMEM202
Alt. namesFLJ27523
RefSeqNP_001073931
UniProtA6NGA9
Search for
StructuresSwiss-model
DomainsInterPro

Transmembrane 202 protein (Homo sapiens, TMEM202) is encoded by the gene TMEM202 and is a member of the Claudin2 superfamily.[5][6] Human paralogs include LIMP2, GSG1, CLDND2, NKG7.[7] The specific function of TMEM202 has largely yet to be elucidated, but other Claudin2 superfamily proteins plays important roles in paracellular transport by contributing to the structure of gap junctions.[8] In S. scrofa (wild boar), TMEM202 has been found to aid in sperm motility, fertilization, and spermatogenesis.[9]

Gene

[edit]

Location

[edit]

The TMEM202 gene spans 10,063 nucleotides on chromosome 15 located at 15q23-q24.1 and on the forward strand. The most complete isoform of TMEM202 (transcript variant 1) contains five exons.[6] The genetic neighborhood is rather scarce, as HEXA is the gene nearest to TMEM202 and is found ~23,000 nucleotides upstream.[6]

Expression

[edit]

TMEM202 demonstrates restricted and low expression in H. sapiens testis.[10]

RNA and Transcriptional variants

[edit]

There exist four transcriptional variants of TMEM202 mRNA.

Properties of TMEM202 mRNA Transcript Variants.[11][12][13][14]
TMEM202 Transcript Variant Accession Number mRNA length (nucleotides) 5'UTR length (nucleotides) Exon 1 Exon 2 Exon 3 Exon 4 Exon 5
Transcript variant 1 NM_001080462 1318 22 Y Y Y Y Y
Isoform X1 XM_011521497 1326 147 X * Y Y Y
Isoform X2 XM_024449910 1186 22 Y Y Y X Y
Isoform X3 XM_011521499 1132 169 X X Y Y Y

'Y' indicates the presence of the exon in the specific transcript variant, whereas 'X' denotes absence of the exon. '*' represents partial loss of exon two in isoform X1 (first thirty-six nucleotides).

TMEM202 Predicted 3D Structure.[15][16] The three-dimensional structure shows off the predicted four transmembrane domains, three alpha helices, and one disulfide bond (all highlighted in yellow, except for the transmembrane domains) predicted in TMEM202 tertiary structure.

TMEM202 protein

[edit]

TMEM202 is classified as a multi-pass protein as it consists of four transmembrane domains with helical structure (residue: 53-75, 121-141, 155-175, and 189-209) and one disordered region (242-273).[6][17] TMEM202 protein is a member of the Claudin2 superfamily. Claudin proteins often form protein-protein interactions in epithelial and endothelial tissue, contributing to the scaffolding of the tight junction.[18]

Properties of TMEM202 Protein Variants.[19][20][21][22][23][24]
TMEM202 Protein Variant Accession Number Protein Length (A.A) Approx. Molecular Weight Prior to PTMs (kDa) Exons present Similarity (%) Internal Composition
TMEM202 Variant 1 NP_001073931.1 273 ~31.2 1-5 100 L: (+)

W: (+)

TMEM202 Isoform X1 XP_011519799.1 234 ~26.8 Part of 2; 3-5 85.7 L: (+)

W: (++)

TMEM202 Isoform X2 XP_024305678.1 229 ~26.1 1-3, 5 83.9 W: (+)

A: (-) D: (-)

TMEM202 Isoform X3 XP_011519801.1 162 ~18.5 3-5 58.6 N/A

Similarity was calculated using Pairwise Sequence Alignments (PSAs) where all transcripts were aligned to transcript variant 1. The approximate molecular weight was calculated prior to post-translational modifications (PTMs), such as cleavages in the sequence or binding of additional molecules (e.g., phosphorylation, n-glycosylation). Emboss SAPS was used to determine relative composition of residues as compared to their database of H. sapiens samples. One (+/-) denotes one standard deviation away from the average, whereas two (++/--) indicate two standard deviations away from the average. Proteins with a (+/-) can be classified as rich or poor for that amino acid (e.g., TMEM202 Variant 1 is leucine- and tryptophan-rich).

TMEM202 Secondary Domains.[25] A two-dimensional look at important regions of the TMEM202 protein. TM1-4 indicate regions of transmembrane domains, exon X-X indicates the transition between exons of the TMEM202 transcript, and the end of TMEM202 has been classified as disordered. A two-dimensional look at important regions of the TMEM202 protein. TM1-4 indicate regions of transmembrane domains, exon X-X indicates the transition between exons of the TMEM202 transcript, and the end of TMEM202 has been classified as disordered.

TMEM202 Secondary Structure

[edit]

The figure to the right, TMEM202 Secondary Domains shows the predicted secondary structure of TMEM202, along with exon boundaries.

Gene Level Regulation

[edit]

Expression pattern

[edit]

The expression of TMEM202 was found to be restricted to the testis during a RNA-sequence study of normal adult human tissue (27 different tissues were analyzed from 95 individual human samples; RPKM = ~5).[26] An additional RNA-seq study of human fetal tissue (six tissue types were sequenced from 35 human fetal samples between 10 and 20 weeks gestational time) found that TMEM202 is present in intestinal, lung, and stomach tissues at week 10 of gestation and in adrenal tissue at week 20.

Promoter region and transcription factor binding

[edit]

The figure Annotated Promoter Sequence of Human TMEM202 shows potential binding locations for the most compatible transcription factors. The promoter region was defined as the 500 nucleotides directly upstream of transcription (denoted by a right pointing arrow).

Annotated Promoter Sequence of Human TMEM202.[27] Transcription Factors are labeled in bold text with their abbreviated code name. The start of transcription occurs where the right-pointing arrow sticks out above the green 'ATG'.

TMEM202 Transcription Factors Potentially Binding in Promoter Region.[27][28][29]

Transcription Factors Name Binding Site Location (Bases upstream - Strand) Binding Score Function of Transcription Factor Reason for Identification
NFIC 1 - Minus 421 Individually capable of activating transcription Function; proximity to start codon; high conservation
ZSCAN4

(Twice)

49 - Minus

134 - Plus

461

609

Regulates embryonic stem cell pluripotency Function relates to microarray studies; high binding score; appears twice in the promoter region
ZBTB24 75 - Minus 554 Involved in BMP2-induced transcription* High binding score
TBP 106 - Plus 421 Aids in the initiation of RNA polymerase II-dependent transcription Function; high conservation
DUXA

(Twice)

109 - Plus

109 - Minus

476

476

Acts as a repressor Function; binding sites on both the plus and minus strand at the same location; overlapping binding sequence with Tfcp2l1; appears twice in the promoter region
Tfcp2l1 115 - Plus 446 Facilitates establishment and maintenance of pluripotency in embryonic stem cells Function relates to microarray studies; overlapping binding sequence with DUXA, ELF3
ELF3 122 - Plus 400 Acts as an activator Function; overlapping binding sequence with Tfcp2l1
TBX20 124 - Minus 449 Acts as a transcriptional activator and repressor Function; overlapping binding sequence with EOMES
EOMES 125 - Minus 418 Acts as transcriptional activator playing a crucial role during development Function; overlapping binding sequence with TBX20
Prdm5 148 - Minus 427 Acts a transcriptional repressor Function
MEIS2 178 - Plus 405 Transcriptional regulation - stabilization of the homeoprotein-DNA complex Function; overlapping binding sequence with FOXH1; moderate coservation
FOXH1 182 - Minus 481 Acts as an activator Function; overlapping binding sequence with MEIS2; moderate conservation
KLF9 205 - Plus 403 Selectively activates transcription when bound to GC box promoter elements Function; overlapping binding sequence with NR1D1
NR1D1 205 - Minus 405 Acts a transcriptional repressor Function; overlapping binding sequence with KLF9
Sox11 221 - Plus 421 Acts as an activator Function; high coservation
ONECUT3 245 - Minus 508 Acts as an activator Function; high binding score; overlapping binding sequence with ONECUT1
ONECUT1 247 - Minus 346 Acts as an activator Function; overlapping binding sequence with ONECUT3; moderate conservation
FOXD3

(Twice)

270 - Minus

364 - Minus

446

467

Acts as a transcriptional activator and repressor Function; appears twice in the promoter region; overlapping binding sequence with HOXB13; high conservation
HOXB13 355 - Plus 450 Invovled in the developmental regulatory system provides cells with positional identities along the anterior-posterior axis Function; overlapping binding sequence with FOXD3
Neurod2 395 - Minus 403 Involved in neuronal determination Function

(*) Indicates hypothesized function. A higher binding score suggests a higher likelihood that the transcription factor will bind to the sequence when present--binding scores were calculated by the Jaspar Database. This is a non-exhaustive list of potential transcription factors that may bind to TMEM202, but presents transcription factors with the highest binding score or potentially illuminating qualities within the 500 base promoter region.

Protein level regulation

[edit]

Post-translational modifications

[edit]

Predicted Post-Translational Modifications of TMEM202.[30][31][32][33][34]

Type of PTM Number of Sites Location Source Notes
Generic phosphorylation 29 S13, S39, S254 NetPhos Locations denoted were three highest scored
Phosphorylation 2 Y25, S245 PhosphoPlus
GlcNAc O-glycosylation 2 T107, S245 DictyOGlyc
N-myristoylation 2 G61, G145 MyHit
Acetylation 1 K264 PhosphoPlus
N-linked glycosylation 1 N225 NetNGlyc
N-linked glycosylation 1 N225 ELM
Arginine and lysine propeptide cleavage sites None None ProP
C-mannosylation sites None None NetCGlyc
GPI Anchors None None NetGPI Likelihood not anchored by GPI - 0.993
O-GalNAc (mucin type) glycosylation sites None None NetOGlyc

Different types of PTM’s were predicted using a variety of computational systems. Locations bolded were predicted by two or more unique systems.

2D Structure of TMEM202 with PTMs.[25] The figure shows where various post-translational modifications are predicted to occur within the context of the primary structure of TMEM202. All regions are intracellular unless labeled TM (transmembrane) or extracellular.

TMEM202 homology and evolution

[edit]

Paralogs of TMEM202

[edit]

Four paralogs, LIMP2, GSG1, CLDND2, NKG7, have been discovered for TMEM202 and are outlined in the table below.

Paralogs of H. sapiens TMEM202.[35][36][37]

TMEM202 Paralogs Genus and Species Name Common Name Accession Number Sequence Length (amino acids) Sequence Identity to Human Protein (%) Sequence Similarity to Human Protein (%) Sequence Divergence (n) Corrected Sequence Divergence (m)
Protein of Interest Homo sapiens Transmembrane Protein 202 TMEM202 NP_001073931.1 273 100 100 0 0
Paralogs Homo sapiens Lens fiber membrane intrinsic protein isoform 2 LIMP2 NP_085915.2 215 14.5 28.6 85.5 193.1021537
Homo sapiens Protein NKG7 isoform 1 NKG7 NP_005592.1 165 14.3 27.9 85.7 194.4910649
Homo sapiens Claudin domain-containing protein 2 CLDND2 NP_689566.1 167 14.2 25.4 85.8 195.1928221
Homo sapiens Germ cell-specific gene 1 protein isoform 1 GSG1 NP_112579.2 285 8.5 15.3 91.5 246.5104022

Sequences characterized as paralogs were aligned to TMEM202 via pairwise analysis (PSA).[19] The results of the PSA gave percent identity and similarity values, which were also used to calculate the sequence divergence value (n) and corrected sequence divergence value (m). Estimated median date of divergence is based on predicted values found on TimeTree.[37]

Orthologs of TMEM202

[edit]

Orthologs were found using the NCBI Blast database[35] by searching for proteins with similar sequences to the H. sapiens TMEM202 protein. All taxia with sequenced proteins, including bacteria, fungi and plants were searched; however, bony fish were found to be the most diverged species to have orthologous proteins. Orthologs were also found in amphibians, birds, reptiles, and mammals. Orthologs are characterized in the table below:

Orthologs of H. sapiens TMEM202.[35][36][37]

TMEM202 Taxonomic Group Genus and Species Common Name Accession Number Median Date of Divergence (MYA) Sequence Length (amino acids) Sequence Identity to Human Protein (%) Sequence Similarity to Human Protein (%) Sequence Divergence (n) Corrected Sequence Divergence (m)
Mammals Primates Homo sapiens Human NP_001073931.1 0 273 100.0 100.0 0.0 0.0
Lagomorphs Ochotona princeps American pika XP_004594772 87 263 58.3 71.4 41.7 54.0
Perissodactyla Diceros bicornis minor South-central black rhinoceros XP_058396452.1 94 271 76.6 82.4 23.4 26.7
Artiodactyls Sus scrofa Wild boar XP_005666231.1 94 271 68.9 79.1 31.1 37.3
Chiroptera Rousettus aegyptiacus Egyptian fruit bat XP_015982472.2 94 289 63.7 75.8 36.3 45.1
Eulipotyphla Condylura cristata Star-nosed mole XP_004687557.1 94 267 61.7 73.7 38.3 48.3
Proboscideans Elephas maximus indicus Indian elephant XP_049761646.1 99 266 73.6 82.1 26.4 30.7
Diprotodontia Vombatus ursinus Common wombat XP_027713789.1 160 288 42.6 55.1 57.4 85.3
Carnivorous marsupials Sarcophilus harrisii Tasmanian devil XP_031812217.1 160 324 38.4 50.8 61.6 95.7
Reptilia Testudines Chelydra serpentina Common snapping turtle KAG6921653.1 319 190 18.3 33.1 81.7 169.8
Squamata Podarcis lilfordi Lilford's wall lizard CAI5781213.1 319 193 18.0 32.5 82.0 171.5
Squamata Naja naja Indian cobra KAG8143384.1 319 150 17.0 27.8 83.0 177.2
Testudines Chrysemys picta bellii Painted turtle XP_065430698.1 319 484 12.5 20.5 87.5 207.9
Aves Psittaciformes Strigops habroptila Kākāpō XP_030329880.1 319 320 14.2 20.3 85.8 195.2
Gruiformes Grus japonensis Red-crowned crane GAB0205531.1 319 238 11.3 19.8 88.7 218.0
Passeriformes Pseudopodoces humilis Ground tit XP_005533382 319 641 7.7 11.2 92.3 256.4
Amphibia Anura Eleutherodactylus coqui Common coquí XP_066461729.1 352 192 20.1 31.9 79.9 160.4
Anura Ascaphus truei Coastal tailed frog MEE6481875.1 352 168 15.7 27.2 84.3 185.2
Urodela Pleurodeles waltl Iberian ribbed newt KAJ1132505.1 352 179 14.9 28.4 85.1 190.4
Vertebrata Cypriniformes Cyprinus carpio Common carp KTG06534.1 429 224 15.8 30.6 84.2 184.5
Notacanthiformes Aldrovandia affinis Gilbert's halosaurid fish KAJ8399001.1 429 173 14.2 28.4 85.8 195.2

Sequences characterized as orthologs were aligned to TMEM202 via pairwise analysis (PSA).[19] The results of the PSA gave percent identity and similarity values, which were also used to calculate the sequence divergence value (n) and corrected sequence divergence value (m). Estimated median date of divergence is based on predicted values found on TimeTree.[37]

Evolution of TMEM202

[edit]

The evolutionary history of TMEM202 appears to have begun approximately 429 years ago as orthologs of the protein were found in species of bony fish. Since then, TMEM202 has evolved in species of amphibians, reptiles, birds, and mammals. This evolution is quantified in Evolutionary History of TMEM202 compared to Fibrinogen a, cyctochrome C, where corrected sequence divergence of TMEM202 orthologs was graphed over time in comparison to fibrinogen a and cytochrome c.

Evolutionary History of TMEM202 compared to fibrinogen a, cytochrome C.

[edit]

[38][39]

Evolutionary History of TMEM202 compared to Fibrinogen a, cyctochrome C in Humans.

Fibrinogen alpha (a) is a fast-evolving protein as compared to cytochrome c, a slow-evolving protein. Across its evolution, TMEM202 has undergone numerous amino acid mutations, as it has ascertained mutations at a similar rate to fibrinogen alpha. For this reason, TMEM202 can be considered a fast-evolving protein.

Unrooted Phylogenetic Tree of H. sapiens TMEM202 and its Orthologous Species.

To the left, Unrooted Phylogenetic Tree of Homo sapiens TMEM202 and its Orthologous Species, helps visualize divergence of some orthologs from humans. Species were further classified into mammals, aves, amphibians, and reptiles.

TMEM202 interacting proteins

[edit]

STRING Network revealed proteins found to interact with TMEM202 and are detailed in the table below. Along with those proteins, are kinases predicted to phosphorylate TMEM202.

Proteins predicted to interact with TMEM202

[edit]

[40][41][42][43][44]

Protein Abbreviation Protein Name Basis of Identification Function Notes
SPATA31D1 Spermatogenesis-associated protein 31D1 STRING Network Might be involved in cell differentiation and spermatogenesis Predicted to be apart of the cell membrane
CFAP45 Cilia and flagella associated protein 45 STRING Network Enables AMP binding and is involved in establishing left/right asymmetry of the flagella
SPACA1 Sperm acrosome membrane-associated protein 1 STRING Network Aids in the acrosome expansion and establishment of normal sperm morphology during spermatogenesis SPACA1 is recognized by anti-sperm antibodies in infertile males
PKC Protein Kinase C Predicted site of phosphorylation Regulates numerous cellular responses including gene expression, protein secretion, cell proliferation, and the inflammatory response
Cdk5 Cyclin-dependent kinase 5 Predicted site of phosphorylation Plays a pivotal role in brain development (embryogenesis) and maintenance (adolescence and adulthood)
Cdc2 Cell Division Cycle 2 Predicted site of phosphorylation Regulates cell cycle progression Also known as CDK1, or Cyclin Dependent Kinase 1

Clinical significance and pathology

[edit]

Mutations - Single Nucleotide Polymorphisms (SNPs)

[edit]

There exist many identified SNPs in the TMEM202 gene. Found in the table below include six of the most common to occur within the promoter region and coding sequence of TMEM202.

SNPs in Human TMEM202

[edit]

[45][46]

SNP Name SNP Location (Relative to TMEM202) Mutation Amino Acid Change Frequency in human population (%) Significance Clinical Significance
rs74622826 164 bases upstream G → A Glycine → Glutamate 0.25 In promoter region None reported in ClinVar
rs74343303 193 bases upstream A→ C/G Leucine → Leucine

(Does not change)

0.01 In promoter region None reported in ClinVar
rs114543781 284 bases upstream C → T Proline → Leucine 0.42 In promoter region None reported in ClinVar
rs112986603 Base 117 C → T 32A → 32V 0.09 In coding sequence None reported in ClinVar
rs16956904 Base 631 A → T 204M → 204L 3.71 In coding sequence within transmembrane region 4 None reported in ClinVar
rs35916586 Base 679 G → A/T/C 219S → 219T / 219S / 219P 0.01 In coding sequence None reported in ClinVar

A small subset of the SNPs may have functional influences on TMEM202 based on where they occur. The SNP, rs16956904 at base 631, is within the fourth transmembrane region. While this is an area of importance, both the normal and SNP variation result in a hydrophobic amino acid. This could explain why no clinical / phenotypic discrepancies have been observed. SNP rs114543781, 284 bases upstream is present where transcription factor HOXB13 is predicted to bind. This transcription factor is invovled in the developmental regulatory system that provides cells with positional identities along the anterior-posterior axis. SNP rs74343303, 193 bases upstream also interferes with FOXD3 binding. FOXD3 has the ability to act as a transcriptional activator and repressor.

Conceptual translation of TMEM202

[edit]
Conceptual Translation of H. sapiens TMEM202.[47][48]

Key found on page 2.

References

[edit]
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000187806 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000049526 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ "Gene: TMEM202 (ENSG00000187806) - Summary - Homo_sapiens - Ensembl genome browser 113". useast.ensembl.org. Retrieved 2024-10-21.
  6. ^ a b c d "TMEM202 transmembrane protein 202 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-10-21.
  7. ^ "TCDB » SEARCH". www.tcdb.org. Retrieved 2024-10-21.
  8. ^ Heiskala, M.; Peterson, P. A.; Yang, Y. (February 2001). "The roles of claudin superfamily proteins in paracellular transport". Traffic (Copenhagen, Denmark). 2 (2): 93–98. doi:10.1034/j.1600-0854.2001.020203.x. ISSN 1398-9219. PMID 11247307.
  9. ^ Lei Shi, Yan Zhang, Xiaoyu Huang, Mingyue Shi, Di Sun, Yanwei Zhang, Wenxin Li, Tianyu Jin, Jingjuan Feng, Jiandong Xing, Bugao Li, Guoqing Cao. Effects of mitoquinone (MitoQ) supplementation during boar semen cryopreservation on sperm quality, antioxidant status and mitochondrial proteomics, Animal Reproduction Science, Volume 247, 2022, 107099, ISSN 0378-4320, https://doi.org/10.1016/j.anireprosci.2022.107099
  10. ^ "AceView: Gene:TMEM202, a comprehensive annotation of human, mouse and worm genes with mRNAs or ESTsAceView". www.ncbi.nlm.nih.gov. Retrieved 2024-12-10.
  11. ^ "Homo sapiens transmembrane protein 202 (TMEM202), transcript variant 1, mRNA". 2024-08-03. {{cite journal}}: Cite journal requires |journal= (help)
  12. ^ "PREDICTED: Homo sapiens transmembrane protein 202 (TMEM202), transcript variant X1, mRNA". 2024-08-25. {{cite journal}}: Cite journal requires |journal= (help)
  13. ^ "PREDICTED: Homo sapiens transmembrane protein 202 (TMEM202), transcript variant X2, mRNA". 2024-08-25. {{cite journal}}: Cite journal requires |journal= (help)
  14. ^ "PREDICTED: Homo sapiens transmembrane protein 202 (TMEM202), transcript variant X3, mRNA". 2024-08-25. {{cite journal}}: Cite journal requires |journal= (help)
  15. ^ Wang J, Youkharibache P, Zhang D, Lanczycki CJ, Geer RC, Madej T, Phan L, Ward M, Lu S, Marchler GH, Wang Y, Bryant SH, Geer LY, Marchler-Bauer A. iCn3D, a Web-based 3D Viewer for Sharing 1D/2D/3D Representations of Biomolecular Structures. Bioinformatics. 2020 Jan 1;36(1):131-135. (Epub 2019 June 20.) doi: 10.1093/bioinformatics/btz502. Wang J, Youkharibache P, Marchler-Bauer A, Lanczycki C, Zhang D, Lu S, Madej T, Marchler GH, Cheng T, Chong LC, Zhao S, Yang K, Lin J, Cheng Z, Dunn R, Malkaram SA, Tai C-H, Enoma D, Busby B, Johnson NL, Tabaro F, Song G, Ge Y. iCn3D: From Web-Based 3D Viewer to Structural Analysis Tool in Batch Mode. Front. Mol. Biosci. 2022 9:831740. (Epub 2022 Feb 17.) doi: 10.3389/fmolb.2022.831740.
  16. ^ "AlphaFold Protein Structure Database". alphafold.ebi.ac.uk. Retrieved 2024-12-10.
  17. ^ "UniProt". www.uniprot.org. Retrieved 2024-10-21.
  18. ^ Heiskala, M.; Peterson, P. A.; Yang, Y. (February 2001). "The roles of claudin superfamily proteins in paracellular transport". Traffic (Copenhagen, Denmark). 2 (2): 93–98. doi:10.1034/j.1600-0854.2001.020203.x. ISSN 1398-9219. PMID 11247307.
  19. ^ a b c www.ebi.ac.uk https://www.ebi.ac.uk/jdispatcher/psa/emboss_needle. Retrieved 2024-12-10. {{cite web}}: Missing or empty |title= (help)
  20. ^ "transmembrane protein 202 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-12-10.
  21. ^ "transmembrane protein 202 isoform X1 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-12-10.
  22. ^ "transmembrane protein 202 isoform X2 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-12-10.
  23. ^ "transmembrane protein 202 isoform X3 [Homo sapiens] - Protein - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-12-10.
  24. ^ www.ebi.ac.uk https://www.ebi.ac.uk/jdispatcher/seqstats/saps. Retrieved 2024-12-11. {{cite web}}: Missing or empty |title= (help)
  25. ^ a b IBS 2.0: an upgraded illustrator for the visualization of biological sequences. Nucleic Acids Research, 2022. DOI: 10.1093/nar/gkac373.
  26. ^ "TMEM202 transmembrane protein 202 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-12-12.
  27. ^ a b "Human hg38 chr15:72,397,805-72,398,407 UCSC Genome Browser v474". genome.ucsc.edu. Retrieved 2024-12-12.
  28. ^ "JASPAR: An open-access database of transcription factor binding profiles". jaspar.elixir.no. Retrieved 2024-12-12.
  29. ^ "UniProt". www.uniprot.org. Retrieved 2024-12-12.
  30. ^ "NetPhos 3.1 - DTU Health Tech - Bioinformatic Services". services.healthtech.dtu.dk. Retrieved 2024-12-12.
  31. ^ "DictyOGlyc 1.1 - DTU Health Tech - Bioinformatic Services". services.healthtech.dtu.dk. Retrieved 2024-12-12.
  32. ^ "NetNGlyc 1.0 - DTU Health Tech - Bioinformatic Services". services.healthtech.dtu.dk. Retrieved 2024-12-12.
  33. ^ "ELM - unknown". elm.eu.org. Retrieved 2024-12-12.
  34. ^ "TMEM202 (human)". www.phosphosite.org. Retrieved 2024-12-12.
  35. ^ a b c "BLAST: Basic Local Alignment Search Tool". blast.ncbi.nlm.nih.gov. Retrieved 2024-12-12.
  36. ^ a b "National Center for Biotechnology Information". www.ncbi.nlm.nih.gov. Retrieved 2024-12-12.
  37. ^ a b c d "TimeTree :: The Timescale of Life". timetree.org. Retrieved 2024-12-12.
  38. ^ "National Center for Biotechnology Information". www.ncbi.nlm.nih.gov. Retrieved 2024-12-13.
  39. ^ "TimeTree :: The Timescale of Life". timetree.org. Retrieved 2024-12-13.
  40. ^ Genecards (Genecards: The Human Gene Database) Entry on SPATA31D1 [https://www.genecards.org/cgi-bin/carddisp.pl?gene=SPATA31D1]
  41. ^ Genecards (Genecards: The Human Gene Database) Entry on CFAP45 [https://www.genecards.org/cgi-bin/carddisp.pl?gene=CFAP45]
  42. ^ Genecards (Genecards: The Human Gene Database) Entry on SPACA1 [https://www.genecards.org/cgi-bin/carddisp.pl?gene=SPACA1]
  43. ^ Kavita Shah, Debomoy K. Lahiri; Cdk5 activity in the brain – multiple paths of regulation. J Cell Sci 1 June 2014; 127 (11): 2391–2400. doi: https://doi.org/10.1242/jcs.147553
  44. ^ "CDK1 cyclin dependent kinase 1 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-12-12.
  45. ^ "Home - SNP - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-12-12.
  46. ^ "Human hg38 chr15:72,398,305-72,408,367 UCSC Genome Browser v474". genome.ucsc.edu. Retrieved 2024-12-12.
  47. ^ "Six-Frame Translation". www.bioline.com. Retrieved 2024-12-13.
  48. ^ "TMEM202 transmembrane protein 202 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-12-13.
Retrieved from "https://en.wikipedia.org/w/index.php?title=TMEM202&oldid=1264085385"