UniProt ID | NECP1_HUMAN | |
---|---|---|
UniProt AC | Q8NC96 | |
Protein Name | Adaptin ear-binding coat-associated protein 1 | |
Gene Name | NECAP1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 275 | |
Subcellular Localization | Cytoplasmic vesicle, clathrin-coated vesicle membrane. Cell membrane. Colocalizes with AP-2 at the plasma membrane.. | |
Protein Description | Involved in endocytosis.. | |
Protein Sequence | MATELEYESVLCVKPDVSVYRIPPRASNRGYRASDWKLDQPDWTGRLRITSKGKTAYIKLEDKVSGELFAQAPVEQYPGIAVETVTDSSRYFVIRIQDGTGRSAFIGIGFTDRGDAFDFNVSLQDHFKWVKQESEISKESQEMDARPKLDLGFKEGQTIKLCIGNITNKKGGASKPRTARGGGLSLLPPPPGGKVTIPPPSSSVAISNHVTPPPIPKSNHGGSDADILLDLDSPAPVTTPAPTPVSVSNDLWGDFSTASSSVPNQAPQPSNWVQF | |
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 |
---|---|---|---|---|---|
3 | Phosphorylation | -----MATELEYESV -----CCCCCEEEEE | 39.54 | 23663014 | |
7 | Phosphorylation | -MATELEYESVLCVK -CCCCCEEEEEEEEC | 26.57 | 23663014 | |
9 | Phosphorylation | ATELEYESVLCVKPD CCCCEEEEEEEECCC | 21.35 | 23663014 | |
18 | Phosphorylation | LCVKPDVSVYRIPPR EEECCCCEEEECCCC | 22.32 | 23663014 | |
20 | Phosphorylation | VKPDVSVYRIPPRAS ECCCCEEEECCCCCC | 8.70 | 23663014 | |
46 | Methylation | DQPDWTGRLRITSKG CCCCCCCCEEEECCC | 17.26 | 115484785 | |
59 | Ubiquitination | KGKTAYIKLEDKVSG CCCEEEEEEECCCCC | 32.90 | 29967540 | |
103 | Phosphorylation | IQDGTGRSAFIGIGF EECCCCCEEEEEEEE | 28.95 | 24719451 | |
131 | Ubiquitination | QDHFKWVKQESEISK HHHHHHHHHHHHHCH | 47.43 | 29967540 | |
140 | Phosphorylation | ESEISKESQEMDARP HHHHCHHHHHHCCCC | 34.87 | 25159151 | |
154 | Ubiquitination | PKLDLGFKEGQTIKL CCCCCCCCCCCEEEE | 60.17 | - | |
154 | Methylation | PKLDLGFKEGQTIKL CCCCCCCCCCCEEEE | 60.17 | - | |
154 | Acetylation | PKLDLGFKEGQTIKL CCCCCCCCCCCEEEE | 60.17 | 25953088 | |
160 | Ubiquitination | FKEGQTIKLCIGNIT CCCCCEEEEEEECCC | 40.47 | 29967540 | |
169 | Malonylation | CIGNITNKKGGASKP EEECCCCCCCCCCCC | 44.11 | 26320211 | |
180 | Methylation | ASKPRTARGGGLSLL CCCCCCCCCCCCCCC | 43.61 | 24129315 | |
196 | Phosphorylation | PPPGGKVTIPPPSSS CCCCCCEECCCCCCC | 31.11 | 23403867 | |
201 | Phosphorylation | KVTIPPPSSSVAISN CEECCCCCCCEEEEC | 40.81 | 23403867 | |
202 | Phosphorylation | VTIPPPSSSVAISNH EECCCCCCCEEEECC | 34.31 | 23403867 | |
203 | Phosphorylation | TIPPPSSSVAISNHV ECCCCCCCEEEECCC | 21.65 | 23403867 | |
207 | Phosphorylation | PSSSVAISNHVTPPP CCCCEEEECCCCCCC | 15.90 | 22617229 | |
211 | Phosphorylation | VAISNHVTPPPIPKS EEEECCCCCCCCCCC | 23.64 | 25159151 |
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 NECP1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NECP1_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 NECP1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
AP1G1_HUMAN | AP1G1 | physical | 14665628 | |
A4_HUMAN | APP | physical | 21832049 | |
CHSP1_HUMAN | CARHSP1 | physical | 26344197 | |
BLOM7_HUMAN | KIAA0907 | physical | 26344197 | |
SERA_HUMAN | PHGDH | physical | 26344197 | |
PIPNA_HUMAN | PITPNA | physical | 26344197 | |
UFC1_HUMAN | UFC1 | physical | 26344197 | |
AP1G1_HUMAN | AP1G1 | physical | 14973137 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
615833 | Epileptic encephalopathy, early infantile, 21 (EIEE21) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASSSPECTROMETRY. |