UniProt ID | TMM62_HUMAN | |
---|---|---|
UniProt AC | Q0P6H9 | |
Protein Name | Transmembrane protein 62 | |
Gene Name | TMEM62 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 643 | |
Subcellular Localization |
Membrane Multi-pass membrane protein . |
|
Protein Description | ||
Protein Sequence | MAAVLALRVVAGLAAAALVAMLLEHYGLAGQPSPLPRPAPPRRPHPAPGPGDSNIFWGLQISDIHLSRFRDPGRAVDLEKFCSETIDIIQPALVLATGDLTDAKTKEQLGSRQHEVEWQTYQGILKKTRVMEKTKWLDIKGNHDAFNIPSLDSIKNYYRKYSAVRRDGSFHYVHSTPFGNYSFICVDATVNPGPKRPYNFFGILDKKKMEELLLLAKESSRSNHTIWFGHFTTSTILSPSPGIRSIMSSAIAYLCGHLHTLGGLMPVLHTRHFQGTLELEVGDWKDNRRYRIFAFDHDLFSFADLIFGKWPVVLITNPKSLLYSCGEHEPLERLLHSTHIRVLAFSLSSITSVTVKIDGVHLGQAVHVSGPIFVLKWNPRNYSSGTHNIEVIVQDSAGRSKSVHHIFSVQENNHLSFDPLASFILRTDHYIMARVLFVLIVLSQLTILIIFRYRGYPELKEPSGFINLTSFSLHVLSKINIFYYSVLLLTLYTVLGPWFFGEIIDGKFGCCFSFGIFVNGHFLQGSITFIIGILQLAFFNIPLMAYMCWSLLQRCFGHNFRSHLHQRKYLKIMPVHLLMLLLYIWQVYSCYFLYATYGTLAFLFSPLRTWLTLLTPVLIRYVWTLNSTKFGIFMVQLKSHLSS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
33 | Phosphorylation | YGLAGQPSPLPRPAP HCCCCCCCCCCCCCC | 31.05 | 24719451 | |
153 | Phosphorylation | FNIPSLDSIKNYYRK CCCCCHHHHHHHHHH | 40.53 | 22210691 | |
180 | N-linked_Glycosylation | VHSTPFGNYSFICVD EECCCCCCEEEEEEE | 29.65 | 19159218 | |
354 | Phosphorylation | LSSITSVTVKIDGVH HHHCCEEEEEECCEE | 18.82 | - | |
453 | Phosphorylation | TILIIFRYRGYPELK HHHHHHHHCCCCCCC | 9.53 | 29116813 | |
467 | N-linked_Glycosylation | KEPSGFINLTSFSLH CCCCCCEECCHHHHH | 34.70 | UniProtKB CARBOHYD | |
469 | Phosphorylation | PSGFINLTSFSLHVL CCCCEECCHHHHHHH | 24.20 | 29116813 | |
562 | Phosphorylation | CFGHNFRSHLHQRKY HHCCCHHHHHHHHHH | 26.68 | 26074081 | |
569 | Phosphorylation | SHLHQRKYLKIMPVH HHHHHHHHHHHHHHH | 18.54 | 26074081 | |
626 | N-linked_Glycosylation | IRYVWTLNSTKFGIF HHHHHHCCCCCEEEE | 40.01 | UniProtKB CARBOHYD |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of TMM62_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TMM62_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of TMM62_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
NPL4_HUMAN | NPLOC4 | physical | 26186194 | |
UFD1_HUMAN | UFD1L | physical | 26186194 | |
HERC3_HUMAN | HERC3 | physical | 26186194 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-180, AND MASSSPECTROMETRY. |