UniProt ID | YIPF3_HUMAN | |
---|---|---|
UniProt AC | Q9GZM5 | |
Protein Name | Protein YIPF3 | |
Gene Name | YIPF3 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 350 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein. Cytoplasm. Golgi apparatus, cis-Golgi network membrane Multi-pass membrane protein. Localization to the cytoplasm or to the cell membrane is developmentally and ontogenetically regulated. |
|
Protein Description | Involved in the maintenance of the Golgi structure. May play a role in hematopoiesis.. | |
Protein Sequence | MATTAAPAGGARNGAGPEWGGFEENIQGGGSAVIDMENMDDTSGSSFEDMGELHQRLREEEVDADAADAAAAEEEDGEFLGMKGFKGQLSRQVADQMWQAGKRQASRAFSLYANIDILRPYFDVEPAQVRSRLLESMIPIKMVNFPQKIAGELYGPLMLVFTLVAILLHGMKTSDTIIREGTLMGTAIGTCFGYWLGVSSFIYFLAYLCNAQITMLQMLALLGYGLFGHCIVLFITYNIHLHALFYLFWLLVGGLSTLRMVAVLVSRTVGPTQRLLLCGTLAALHMLFLLYLHFAYHKVVEGILDTLEGPNIPPIQRVPRDIPAMLPAARLPTTVLNATAKAVAVTLQSH | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MATTAAPAG ------CCCCCCCCC | 17.41 | 22814378 | |
48 | Ubiquitination | DTSGSSFEDMGELHQ CCCCCCHHHHHHHHH | 49.38 | 21963094 | |
51 | Ubiquitination | GSSFEDMGELHQRLR CCCHHHHHHHHHHHH | 46.78 | 27667366 | |
67 | Ubiquitination | EEVDADAADAAAAEE HHCCHHHHHHHHHHH | 13.92 | 27667366 | |
83 | Ubiquitination | DGEFLGMKGFKGQLS CCCCCCCCCCCHHHH | 60.44 | 21906983 | |
86 | Ubiquitination | FLGMKGFKGQLSRQV CCCCCCCCHHHHHHH | 55.18 | 27667366 | |
102 | Ubiquitination | DQMWQAGKRQASRAF HHHHHHHHHHHHHHH | 44.33 | 27667366 | |
106 | Ubiquitination | QAGKRQASRAFSLYA HHHHHHHHHHHHHHH | 18.79 | 22817900 | |
136 | Phosphorylation | VRSRLLESMIPIKMV HHHHHHHHCCCEEEC | 23.21 | - | |
137 | Sulfoxidation | RSRLLESMIPIKMVN HHHHHHHCCCEEECC | 2.85 | 21406390 | |
141 | Ubiquitination | LESMIPIKMVNFPQK HHHCCCEEECCCCHH | 31.29 | 21906983 | |
148 | Ubiquitination | KMVNFPQKIAGELYG EECCCCHHHHHHHHH | 34.46 | - | |
272 | Phosphorylation | VSRTVGPTQRLLLCG HHCCCCHHHHHHHHH | 22.01 | - | |
333 | O-linked_Glycosylation | LPAARLPTTVLNATA CCHHCCCHHHHHHHH | 33.84 | 21757827 | |
334 | O-linked_Glycosylation | PAARLPTTVLNATAK CHHCCCHHHHHHHHH | 22.51 | 21757827 | |
337 | N-linked_Glycosylation | RLPTTVLNATAKAVA CCCHHHHHHHHHHHH | 30.80 | 21757827 | |
339 | O-linked_Glycosylation | PTTVLNATAKAVAVT CHHHHHHHHHHHHHH | 27.84 | 55823995 | |
346 | O-linked_Glycosylation | TAKAVAVTLQSH--- HHHHHHHHCCCC--- | 14.89 | 22171320 | |
349 | O-linked_Glycosylation | AVAVTLQSH------ HHHHHCCCC------ | 33.99 | 55834431 |
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 YIPF3_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YIPF3_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 YIPF3_HUMAN !! |
Kegg Disease | ||||||
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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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O-linked Glycosylation | |
Reference | PubMed |
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD."; Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; Mol. Cell. Proteomics 0:0-0(2011). Cited for: GLYCOSYLATION AT THR-346, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY. | |
"Characterization of YIPF3 and YIPF4, cis-Golgi localizing Yip domainfamily proteins."; Tanimoto K., Suzuki K., Jokitalo E., Sakai N., Sakaguchi T.,Tamura D., Fujii G., Aoki K., Takada S., Ishida R., Tanabe M.,Itoh H., Yoneda Y., Sohda M., Misumi Y., Nakamura N.; Cell Struct. Funct. 36:171-185(2011). Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH YIPF4, ANDGLYCOSYLATION AT THR-333; THR-334; ASN-337 AND THR-346. |