UniProt ID | ITA9_HUMAN | |
---|---|---|
UniProt AC | Q13797 | |
Protein Name | Integrin alpha-9 | |
Gene Name | ITGA9 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 1035 | |
Subcellular Localization |
Membrane Single-pass type I membrane protein . |
|
Protein Description | Integrin alpha-9/beta-1 (ITGA9:ITGB1) is a receptor for VCAM1, cytotactin and osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in cytotactin.. | |
Protein Sequence | MGGPAAPRGAGRLRALLLALVVAGIPAGAYNLDPQRPVHFQGPADSFFGYAVLEHFHDNTRWVLVGAPKADSKYSPSVKSPGAVFKCRVHTNPDRRCTELDMARGKNRGTSCGKTCREDRDDEWMGVSLARQPKADGRVLACAHRWKNIYYEADHILPHGFCYIIPSNLQAKGRTLIPCYEEYKKKYGEEHGSCQAGIAGFFTEELVVMGAPGSFYWAGTIKVLNLTDNTYLKLNDEVIMNRRYTYLGYAVTAGHFSHPSTIDVVGGAPQDKGIGKVYIFRADRRSGTLIKIFQASGKKMGSYFGSSLCAVDLNGDGLSDLLVGAPMFSEIRDEGQVTVYINRGNGALEEQLALTGDGAYNAHFGESIASLDDLDNDGFPDVAIGAPKEDDFAGAVYIYHGDAGGIVPQYSMKLSGQKINPVLRMFGQSISGGIDMDGNGYPDVTVGAFMSDSVVLLRARPVITVDVSIFLPGSINITAPQCHDGQQPVNCLNVTTCFSFHGKHVPGEIGLNYVLMADVAKKEKGQMPRVYFVLLGETMGQVTEKLQLTYMEETCRHYVAHVKRRVQDVISPIVFEAAYSLSEHVTGEEERELPPLTPVLRWKKGQKIAQKNQTVFERNCRSEDCAADLQLQGKLLLSSMDEKTLYLALGAVKNISLNISISNLGDDAYDANVSFNVSRELFFINMWQKEEMGISCELLESDFLKCSVGFPFMRSKSKYEFSVIFDTSHLSGEEEVLSFIVTAQSGNTERSESLHDNTLVLMVPLMHEVDTSITGIMSPTSFVYGESVDAANFIQLDDLECHFQPINITLQVYNTGPSTLPGSSVSISFPNRLSSGGAEMFHVQEMVVGQEKGNCSFQKNPTPCIIPQEQENIFHTIFAFFTKSGRKVLDCEKPGISCLTAHCNFSALAKEESRTIDIYMLLNTEILKKDSSSVIQFMSRAKVKVDPALRVVEIAHGNPEEVTVVFEALHNLEPRGYVVGWIIAISLLVGILIFLLLAVLLWKMGFFRRRYKEIIEAEKNRKENEDSWDWVQKNQ | |
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 |
---|---|---|---|---|---|
73 | Ubiquitination | GAPKADSKYSPSVKS ECCCCCCCCCCCCCC | 50.74 | - | |
73 | Acetylation | GAPKADSKYSPSVKS ECCCCCCCCCCCCCC | 50.74 | 20167786 | |
175 | Phosphorylation | NLQAKGRTLIPCYEE CCCCCCCEEEECHHH | 37.39 | 26437602 | |
180 | Phosphorylation | GRTLIPCYEEYKKKY CCEEEECHHHHHHHH | 13.36 | 26437602 | |
183 | Phosphorylation | LIPCYEEYKKKYGEE EEECHHHHHHHHCHH | 19.03 | 26437602 | |
225 | N-linked_Glycosylation | AGTIKVLNLTDNTYL EEEEEEEECCCCCEE | 43.83 | 19159218 | |
319 | Phosphorylation | DLNGDGLSDLLVGAP ECCCCCHHHHCCCCC | 31.57 | 29759185 | |
329 | Phosphorylation | LVGAPMFSEIRDEGQ CCCCCCCEEECCCCE | 26.34 | 29759185 | |
429 | Phosphorylation | VLRMFGQSISGGIDM HHHHHCCCCCCCCCC | 21.07 | 23532336 | |
453 | Phosphorylation | VGAFMSDSVVLLRAR EEEECCCCEEEECCC | 13.55 | 23532336 | |
476 | N-linked_Glycosylation | IFLPGSINITAPQCH EECCCCEEEECCCCC | 27.53 | UniProtKB CARBOHYD | |
493 | N-linked_Glycosylation | QQPVNCLNVTTCFSF CCCCCEEEEEEEEEE | 31.15 | UniProtKB CARBOHYD | |
612 | N-linked_Glycosylation | GQKIAQKNQTVFERN CHHHHHHCCHHHHCC | 30.58 | UniProtKB CARBOHYD | |
622 | Phosphorylation | VFERNCRSEDCAADL HHHCCCCCHHHHHHH | 39.73 | - | |
638 | Phosphorylation | LQGKLLLSSMDEKTL HCCEEHHHCCCHHHH | 24.48 | - | |
639 | Phosphorylation | QGKLLLSSMDEKTLY CCEEHHHCCCHHHHH | 30.17 | - | |
654 | N-linked_Glycosylation | LALGAVKNISLNISI HHHHHHHEEEEEEEE | 23.60 | UniProtKB CARBOHYD | |
658 | N-linked_Glycosylation | AVKNISLNISISNLG HHHEEEEEEEEECCC | 21.12 | UniProtKB CARBOHYD | |
672 | N-linked_Glycosylation | GDDAYDANVSFNVSR CCCCCCCCCEEECCH | 27.37 | UniProtKB CARBOHYD | |
676 | N-linked_Glycosylation | YDANVSFNVSRELFF CCCCCEEECCHHHEE | 24.29 | UniProtKB CARBOHYD | |
707 | Phosphorylation | ESDFLKCSVGFPFMR HCCCCCCCCCCCCCC | 24.56 | - | |
715 | Phosphorylation | VGFPFMRSKSKYEFS CCCCCCCCCCEEEEE | 29.50 | - | |
807 | N-linked_Glycosylation | ECHFQPINITLQVYN EEEEEEEEEEEEEEE | 28.07 | UniProtKB CARBOHYD | |
854 | N-linked_Glycosylation | VVGQEKGNCSFQKNP ECCCCCCCCCCCCCC | 29.36 | UniProtKB CARBOHYD | |
904 | N-linked_Glycosylation | SCLTAHCNFSALAKE EEEEECCCHHHHHCC | 24.84 | UniProtKB CARBOHYD | |
913 | Phosphorylation | SALAKEESRTIDIYM HHHHCCHHCEEEEEE | 35.50 | - | |
915 | Phosphorylation | LAKEESRTIDIYMLL HHCCHHCEEEEEEEE | 32.08 | - | |
938 | Oxidation | SSSVIQFMSRAKVKV CCHHHHHHHHCCCCC | 1.20 | 17322306 | |
939 | Phosphorylation | SSVIQFMSRAKVKVD CHHHHHHHHCCCCCC | 30.30 | 24114839 | |
1027 | Phosphorylation | NRKENEDSWDWVQKN HHCCCCCCCHHHHHC | 22.28 | 26657352 | |
1033 | Ubiquitination | DSWDWVQKNQ----- CCCHHHHHCC----- | 47.93 | - |
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 ITA9_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ITA9_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 ITA9_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
AL1A3_HUMAN | ALDH1A3 | physical | 28514442 | |
NGAL_HUMAN | LCN2 | physical | 28514442 | |
SPB4_HUMAN | SERPINB4 | physical | 28514442 | |
SPR1B_HUMAN | SPRR1B | physical | 28514442 | |
ITB1_HUMAN | ITGB1 | physical | 28514442 | |
PCYXL_HUMAN | PCYOX1L | physical | 28514442 | |
SMOC1_HUMAN | SMOC1 | physical | 28514442 | |
IGLL5_HUMAN | IGLL5 | physical | 28514442 | |
KLK10_HUMAN | KLK10 | physical | 28514442 | |
INVO_HUMAN | IVL | physical | 28514442 | |
GRP78_HUMAN | HSPA5 | physical | 28514442 | |
CALL5_HUMAN | CALML5 | physical | 28514442 | |
EVPL_HUMAN | EVPL | physical | 28514442 | |
TBA4A_HUMAN | TUBA4A | physical | 28514442 |
Kegg Disease | ||||||
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H00590 | Congenital muscular dystrophies (CMD/MDC), including: Merosin-deficient CMD (MDC1A); Ullrich CMD (UC | |||||
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-225, AND MASSSPECTROMETRY. |