UniProt ID | ITA11_HUMAN | |
---|---|---|
UniProt AC | Q9UKX5 | |
Protein Name | Integrin alpha-11 | |
Gene Name | ITGA11 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 1188 | |
Subcellular Localization |
Membrane Single-pass type I membrane protein. |
|
Protein Description | Integrin alpha-11/beta-1 is a receptor for collagen.. | |
Protein Sequence | MDLPRGLVVAWALSLWPGFTDTFNMDTRKPRVIPGSRTAFFGYTVQQHDISGNKWLVVGAPLETNGYQKTGDVYKCPVIHGNCTKLNLGRVTLSNVSERKDNMRLGLSLATNPKDNSFLACSPLWSHECGSSYYTTGMCSRVNSNFRFSKTVAPALQRCQTYMDIVIVLDGSNSIYPWVEVQHFLINILKKFYIGPGQIQVGVVQYGEDVVHEFHLNDYRSVKDVVEAASHIEQRGGTETRTAFGIEFARSEAFQKGGRKGAKKVMIVITDGESHDSPDLEKVIQQSERDNVTRYAVAVLGYYNRRGINPETFLNEIKYIASDPDDKHFFNVTDEAALKDIVDALGDRIFSLEGTNKNETSFGLEMSQTGFSSHVVEDGVLLGAVGAYDWNGAVLKETSAGKVIPLRESYLKEFPEELKNHGAYLGYTVTSVVSSRQGRVYVAGAPRFNHTGKVILFTMHNNRSLTIHQAMRGQQIGSYFGSEITSVDIDGDGVTDVLLVGAPMYFNEGRERGKVYVYELRQNLFVYNGTLKDSHSYQNARFGSSIASVRDLNQDSYNDVVVGAPLEDNHAGAIYIFHGFRGSILKTPKQRITASELATGLQYFGCSIHGQLDLNEDGLIDLAVGALGNAVILWSRPVVQINASLHFEPSKINIFHRDCKRSGRDATCLAAFLCFTPIFLAPHFQTTTVGIRYNATMDERRYTPRAHLDEGGDRFTNRAVLLSSGQELCERINFHVLDTADYVKPVTFSVEYSLEDPDHGPMLDDGWPTTLRVSVPFWNGCNEDEHCVPDLVLDARSDLPTAMEYCQRVLRKPAQDCSAYTLSFDTTVFIIESTRQRVAVEATLENRGENAYSTVLNISQSANLQFASLIQKEDSDGSIECVNEERRLQKQVCNVSYPFFRAKAKVAFRLDFEFSKSIFLHHLEIELAAGSDSNERDSTKEDNVAPLRFHLKYEADVLFTRSSSLSHYEVKPNSSLERYDGIGPPFSCIFRIQNLGLFPIHGMMMKITIPIATRSGNRLLKLRDFLTDEANTSCNIWGNSTEYRPTPVEEDLRRAPQLNHSNSDVVSINCNIRLVPNQEINFHLLGNLWLRSLKALKYKSMKIMVNAALQRQFHSPFIFREEDPSRQIVFEISKQEDWQVPIWIIVGSTLGGLLLLALLVLALWKLGFFRSARRRREPGLDPTPKVLE | |
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 |
---|---|---|---|---|---|
82 | N-linked_Glycosylation | KCPVIHGNCTKLNLG ECCEEECCCCEEECC | 19.00 | UniProtKB CARBOHYD | |
92 | Phosphorylation | KLNLGRVTLSNVSER EEECCEEEECCHHHC | 24.10 | 22210691 | |
94 | Phosphorylation | NLGRVTLSNVSERKD ECCEEEECCHHHCCC | 26.31 | 29396449 | |
95 | N-linked_Glycosylation | LGRVTLSNVSERKDN CCEEEECCHHHCCCC | 44.43 | UniProtKB CARBOHYD | |
97 | Phosphorylation | RVTLSNVSERKDNMR EEEECCHHHCCCCEE | 35.61 | 29396449 | |
150 | Acetylation | NSNFRFSKTVAPALQ CCCCCCCCCHHHHHH | 44.28 | 7480079 | |
291 | N-linked_Glycosylation | IQQSERDNVTRYAVA HHHHHHHCHHHHHHH | 43.19 | UniProtKB CARBOHYD | |
331 | N-linked_Glycosylation | PDDKHFFNVTDEAAL CCCCCCCCCCCHHHH | 34.53 | 19159218 | |
351 | Phosphorylation | ALGDRIFSLEGTNKN HHHCEEEEEECCCCC | 24.12 | 23403867 | |
358 | N-linked_Glycosylation | SLEGTNKNETSFGLE EEECCCCCCCCEEEE | 60.90 | UniProtKB CARBOHYD | |
409 | Phosphorylation | KVIPLRESYLKEFPE CEEECCHHHHHHCCH | 29.36 | 24719451 | |
430 | Phosphorylation | AYLGYTVTSVVSSRQ CCCCEEEEEEEECCC | 14.17 | 22210691 | |
431 | Phosphorylation | YLGYTVTSVVSSRQG CCCEEEEEEEECCCC | 19.04 | - | |
434 | Phosphorylation | YTVTSVVSSRQGRVY EEEEEEEECCCCCEE | 20.04 | 22210691 | |
449 | N-linked_Glycosylation | VAGAPRFNHTGKVIL EEECCCCCCCCCEEE | 32.84 | UniProtKB CARBOHYD | |
462 | N-linked_Glycosylation | ILFTMHNNRSLTIHQ EEEEEECCCEEEEEH | 21.90 | UniProtKB CARBOHYD | |
479 | Phosphorylation | RGQQIGSYFGSEITS CCCCCHHHCCCEEEE | 13.52 | 22210691 | |
485 | Phosphorylation | SYFGSEITSVDIDGD HHCCCEEEEEECCCC | 20.74 | 23403867 | |
486 | Phosphorylation | YFGSEITSVDIDGDG HCCCEEEEEECCCCC | 24.37 | 23403867 | |
528 | N-linked_Glycosylation | RQNLFVYNGTLKDSH CCCEEEEECCCCCCC | 31.50 | UniProtKB CARBOHYD | |
583 | Phosphorylation | IFHGFRGSILKTPKQ EEECCCCCCCCCHHH | 22.08 | 24719451 | |
642 | N-linked_Glycosylation | SRPVVQINASLHFEP CCCEEEEEEEECCCH | 13.34 | UniProtKB CARBOHYD | |
686 | Phosphorylation | FLAPHFQTTTVGIRY HHCCCCCCCEEEEEE | 24.40 | - | |
693 | Phosphorylation | TTTVGIRYNATMDER CCEEEEEEECCCCCC | 13.76 | 25262027 | |
694 | N-linked_Glycosylation | TTVGIRYNATMDERR CEEEEEEECCCCCCC | 21.06 | UniProtKB CARBOHYD | |
696 | Phosphorylation | VGIRYNATMDERRYT EEEEEECCCCCCCCC | 22.86 | 25262027 | |
703 | Phosphorylation | TMDERRYTPRAHLDE CCCCCCCCCCCCCCC | 12.42 | 30631047 | |
769 | Phosphorylation | MLDDGWPTTLRVSVP CCCCCCCCEEEEEEE | 31.77 | 20363803 | |
770 | Phosphorylation | LDDGWPTTLRVSVPF CCCCCCCEEEEEEEE | 14.42 | 20363803 | |
857 | N-linked_Glycosylation | NAYSTVLNISQSANL CHHHHHEEHHHCCCC | 27.77 | UniProtKB CARBOHYD | |
894 | N-linked_Glycosylation | RLQKQVCNVSYPFFR HHHHHHHCCCCHHHH | 27.24 | UniProtKB CARBOHYD | |
953 | Phosphorylation | PLRFHLKYEADVLFT CCEEEEEEEEEEEEE | 23.78 | 24719451 | |
960 | Phosphorylation | YEADVLFTRSSSLSH EEEEEEEECCCCCCC | 26.02 | 24719451 | |
973 | N-linked_Glycosylation | SHYEVKPNSSLERYD CCCEECCCCCCCCCC | 38.21 | UniProtKB CARBOHYD | |
1031 | N-linked_Glycosylation | DFLTDEANTSCNIWG HHHCCCCCCCCCCCC | 30.40 | UniProtKB CARBOHYD | |
1039 | N-linked_Glycosylation | TSCNIWGNSTEYRPT CCCCCCCCCCCCCCC | 30.66 | UniProtKB CARBOHYD | |
1059 | N-linked_Glycosylation | LRRAPQLNHSNSDVV HHHCCCCCCCCCCCE | 31.15 | UniProtKB CARBOHYD | |
1098 | Phosphorylation | RSLKALKYKSMKIMV HHHHHHHHCHHHHHH | 14.78 | 18083107 | |
1100 | Phosphorylation | LKALKYKSMKIMVNA HHHHHHCHHHHHHHH | 23.40 | - | |
1183 | Phosphorylation | REPGLDPTPKVLE-- CCCCCCCCCCCCC-- | 35.09 | 30266825 |
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 ITA11_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ITA11_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 ITA11_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ITA11_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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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-331, AND MASSSPECTROMETRY. |