| UniProt ID | HIP1_MOUSE | |
|---|---|---|
| UniProt AC | Q8VD75 | |
| Protein Name | Huntingtin-interacting protein 1 {ECO:0000250|UniProtKB:O00291} | |
| Gene Name | Hip1 {ECO:0000312|MGI:MGI:1099804} | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 1029 | |
| Subcellular Localization | Cytoplasm. Nucleus. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Shuttles between cytoplasm and nucleus. Nuclear translocation can be induced by AR (By similarity).. | |
| Protein Description | Plays a role in clathrin-mediated endocytosis and trafficking. [PubMed: 11577110 Involved in regulating AMPA receptor trafficking in the central nervous system in an NMDA-dependent manner] | |
| Protein Sequence | MDRMASSMKQVSNPLPKVLSRRGVGAGMEAAERESFERTQTVSVNKAINTQEVAVKEKHARTCILGTHHEKGAQTFWSVVNRLPLSSNAMLCWKFCHVFHKLLRDGHPNVLKDSLRYKNELSDMSRMWGHLSEGYGQLCSIYLKLLRTRMEYHTKNPRFPGNLQMSDRQLDEAGESDVNNFFQLTVEMFDYLECELNLFQTVFNSLDMSRSVSVTTAGQCRLAPLIQVILDCSHLYDYTVKLLFKLHSCLPADTLQGHRDRFMEQFTKLKDLFQRSSNLQYFKRLIQIPQLPENPPNFLRASALSEHISPVVVIPAEVSSPDSEPVLEKDDLMDMDASQQTLFDNKFDDVFGSSLSSDPFNFNNQNGVNKDEKDHLIERLYREISGLTGQLDNMKIESQRAMLQLKGRVSELEAELAEQQHLGRQAMDDCEFLRTELDELKRQREDTEKAQRSLTEIERKAQANEQRYSKLKEKYSELVQNHADLLRKNAEVTKQVSVARQAQVDLEREKKELADSFARTQEQQDVLENLKHELATSRQELQVLHSNLETSAQSEAKWLTQIAELEKEQGSLATVAAQREEELSALRDQLESTQIKLAGAQESMCQQVKDQRKTLLAGIRKAAEREIQEALSQLEEPTLISCAGSTDHLLSKVSSVSSCLEQLEKNGSQYLACPEDISELLHSITLLAHLTGDTIIQGSATSLRAPPEPADSLTEACRQYGRETLAYLSSLEEEGTMENADVTALRNCLSRVKTLGEELLPRGLDIKQEELGDLVDKEMAATSAAIEAATTRIEEILSKSRAGDTGVKLEVNERILGSCTSLMQAIKVLVVASKDLQKEIVESGRGTASPKEFYAKNSRWTEGLISASKAVGWGATIMVDAADLVVQGKGKFEELMVCSREIAASTAQLVAASKVKANKGSLNLTQLQQASRGVNQATAAVVASTISGKSQIEETDSMDFSSMTLTQIKRQEMDSQVRVLELENDLQKERQKLGELRKKHYELAGVAEGWEEGTEASPSTVQEAIPDKE | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MDRMASSMKQVSN --CHHHHHHHHHHCC | 22.94 | 24719451 | |
| 9 | Ubiquitination | DRMASSMKQVSNPLP HHHHHHHHHHCCCHH | 49.88 | 27667366 | |
| 12 | Phosphorylation | ASSMKQVSNPLPKVL HHHHHHHCCCHHHHH | 30.18 | 24719451 | |
| 46 | Ubiquitination | TQTVSVNKAINTQEV CCEEEHHHCCCCCCH | 48.79 | 22790023 | |
| 78 | Ubiquitination | KGAQTFWSVVNRLPL HCHHHHHHHHHCCCC | 16.40 | 27667366 | |
| 84 | Ubiquitination | WSVVNRLPLSSNAML HHHHHCCCCCCCHHH | 27.27 | 27667366 | |
| 87 | Ubiquitination | VNRLPLSSNAMLCWK HHCCCCCCCHHHHHH | 35.97 | 27667366 | |
| 93 | Ubiquitination | SSNAMLCWKFCHVFH CCCHHHHHHHHHHHH | 7.87 | 27667366 | |
| 112 | Ubiquitination | DGHPNVLKDSLRYKN CCCCCHHHHHHHHHH | 40.77 | 27667366 | |
| 114 | Phosphorylation | HPNVLKDSLRYKNEL CCCHHHHHHHHHHHH | 17.10 | 22817900 | |
| 118 | Ubiquitination | LKDSLRYKNELSDMS HHHHHHHHHHHHHHH | 37.20 | 22790023 | |
| 121 | Ubiquitination | SLRYKNELSDMSRMW HHHHHHHHHHHHHHH | 8.01 | 27667366 | |
| 130 | Ubiquitination | DMSRMWGHLSEGYGQ HHHHHHHHHHCHHHH | 15.63 | 27667366 | |
| 154 | Phosphorylation | RTRMEYHTKNPRFPG HHHHHHHCCCCCCCC | 31.45 | 19144319 | |
| 155 | Ubiquitination | TRMEYHTKNPRFPGN HHHHHHCCCCCCCCC | 52.20 | 22790023 | |
| 283 | Ubiquitination | SSNLQYFKRLIQIPQ HHCHHHHHHHHCCCC | 41.16 | 22790023 | |
| 319 | Phosphorylation | VVIPAEVSSPDSEPV EEEECCCCCCCCCCC | 27.88 | 29472430 | |
| 320 | Phosphorylation | VIPAEVSSPDSEPVL EEECCCCCCCCCCCC | 37.59 | 26824392 | |
| 323 | Phosphorylation | AEVSSPDSEPVLEKD CCCCCCCCCCCCCCC | 47.38 | 27180971 | |
| 338 | Phosphorylation | DLMDMDASQQTLFDN CCCCCCHHHHHHHCC | 20.68 | - | |
| 372 | Ubiquitination | QNGVNKDEKDHLIER CCCCCHHHHHHHHHH | 63.09 | 27667366 | |
| 381 | Ubiquitination | DHLIERLYREISGLT HHHHHHHHHHHHCCC | 16.66 | 27667366 | |
| 395 | Ubiquitination | TGQLDNMKIESQRAM CCCHHHCHHHHHHHH | 49.96 | 22790023 | |
| 406 | Ubiquitination | QRAMLQLKGRVSELE HHHHHHHHHHHHHHH | 31.54 | 22790023 | |
| 410 | Phosphorylation | LQLKGRVSELEAELA HHHHHHHHHHHHHHH | 34.79 | 26060331 | |
| 571 | Phosphorylation | ELEKEQGSLATVAAQ HHHHHHCCHHHHHHH | 17.96 | 28066266 | |
| 655 | Phosphorylation | HLLSKVSSVSSCLEQ HHHHHHHHHHHHHHH | 29.07 | 29514104 | |
| 798 | Phosphorylation | TRIEEILSKSRAGDT HHHHHHHHHCCCCCC | 33.96 | 23737553 | |
| 950 | Phosphorylation | ASTISGKSQIEETDS HHHHCCCCCCEECCC | 39.66 | 20469934 | |
| 955 | Phosphorylation | GKSQIEETDSMDFSS CCCCCEECCCCCCCC | 22.15 | 20469934 | |
| 957 | Phosphorylation | SQIEETDSMDFSSMT CCCEECCCCCCCCCC | 27.89 | 20469934 | |
| 961 | Phosphorylation | ETDSMDFSSMTLTQI ECCCCCCCCCCHHHH | 18.22 | 20469934 | |
| 962 | Phosphorylation | TDSMDFSSMTLTQIK CCCCCCCCCCHHHHH | 18.77 | 20469934 | |
| 964 | Phosphorylation | SMDFSSMTLTQIKRQ CCCCCCCCHHHHHHH | 28.71 | 20469934 | |
| 966 | Phosphorylation | DFSSMTLTQIKRQEM CCCCCCHHHHHHHHH | 21.05 | 20469934 | |
| 1014 | Phosphorylation | AEGWEEGTEASPSTV HCCCCCCCCCCCCHH | 31.49 | 25338131 |
| 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 HIP1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HIP1_MOUSE !! | ||||||
* 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 HIP1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of HIP1_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, AND MASSSPECTROMETRY. | |