ITA7_HUMAN - dbPTM
ITA7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITA7_HUMAN
UniProt AC Q13683
Protein Name Integrin alpha-7
Gene Name ITGA7
Organism Homo sapiens (Human).
Sequence Length 1181
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Integrin alpha-7/beta-1 is the primary laminin receptor on skeletal myoblasts and adult myofibers. During myogenic differentiation, it may induce changes in the shape and mobility of myoblasts, and facilitate their localization at laminin-rich sites of secondary fiber formation. It is involved in the maintenance of the myofibers cytoarchitecture as well as for their anchorage, viability and functional integrity. Isoform Alpha-7X2B and isoform Alpha-7X1B promote myoblast migration on laminin 1 and laminin 2/4, but isoform Alpha-7X1B is less active on laminin 1 (In vitro). Acts as Schwann cell receptor for laminin-2. Acts as a receptor of COMP and mediates its effect on vascular smooth muscle cells (VSMCs) maturation (By similarity). Required to promote contractile phenotype acquisition in differentiated airway smooth muscle (ASM) cells..
Protein Sequence MAGARSRDPWGASGICYLFGSLLVELLFSRAVAFNLDVMGALRKEGEPGSLFGFSVALHRQLQPRPQSWLLVGAPQALALPGQQANRTGGLFACPLSLEETDCYRVDIDQGADMQKESKENQWLGVSVRSQGPGGKIVTCAHRYEARQRVDQILETRDMIGRCFVLSQDLAIRDELDGGEWKFCEGRPQGHEQFGFCQQGTAAAFSPDSHYLLFGAPGTYNWKGTARVELCAQGSADLAHLDDGPYEAGGEKEQDPRLIPVPANSYFGLLFVTNIDSSDPDQLVYKTLDPADRLPGPAGDLALNSYLGFSIDSGKGLVRAEELSFVAGAPRANHKGAVVILRKDSASRLVPEVMLSGERLTSGFGYSLAVADLNSDGWPDLIVGAPYFFERQEELGGAVYVYLNQGGHWAGISPLRLCGSPDSMFGISLAVLGDLNQDGFPDIAVGAPFDGDGKVFIYHGSSLGVVAKPSQVLEGEAVGIKSFGYSLSGSLDMDGNQYPDLLVGSLADTAVLFRARPILHVSHEVSIAPRSIDLEQPNCAGGHSVCVDLRVCFSYIAVPSSYSPTVALDYVLDADTDRRLRGQVPRVTFLSRNLEEPKHQASGTVWLKHQHDRVCGDAMFQLQENVKDKLRAIVVTLSYSLQTPRLRRQAPGQGLPPVAPILNAHQPSTQRAEIHFLKQGCGEDKICQSNLQLVRARFCTRVSDTEFQPLPMDVDGTTALFALSGQPVIGLELMVTNLPSDPAQPQADGDDAHEAQLLVMLPDSLHYSGVRALDPAEKPLCLSNENASHVECELGNPMKRGAQVTFYLILSTSGISIETTELEVELLLATISEQELHPVSARARVFIELPLSIAGMAIPQQLFFSGVVRGERAMQSERDVGSKVKYEVTVSNQGQSLRTLGSAFLNIMWPHEIANGKWLLYPMQVELEGGQGPGQKGLCSPRPNILHLDVDSRDRRRRELEPPEQQEPGERQEPSMSWWPVSSAEKKKNITLDCARGTANCVVFSCPLYSFDRAAVLHVWGRLWNSTFLEEYSAVKSLEVIVRANITVKSSIKNLMLRDASTVIPVMVYLDPMAVVAEGVPWWVILLAVLAGLLVLALLVLLLWKMGFFKRAKHPEATVPQYHAVKIPREDRQQFKEEKTGTILRNNWGSPRREGPDAHPILAADGHPELGPDGHPGPGTA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
6 (in isoform 13)Phosphorylation-40.2723663014
13 (in isoform 13)Phosphorylation-25.4223663014
14 (in isoform 13)Phosphorylation-17.2923663014
15 (in isoform 13)Phosphorylation-0.9823663014
50PhosphorylationRKEGEPGSLFGFSVA
HCCCCCCCHHEEEEE		31.10-
86N-linked_GlycosylationALPGQQANRTGGLFA
CCCCCCCCCCCCCCC		37.40UniProtKB CARBOHYD
127PhosphorylationENQWLGVSVRSQGPG
CCCEEEEEEEECCCC		15.2623403867
130PhosphorylationWLGVSVRSQGPGGKI
EEEEEEEECCCCCEE		37.0223403867
156PhosphorylationRVDQILETRDMIGRC
HHHHHHHHHHHHHHH		28.6424505115
306PhosphorylationGDLALNSYLGFSIDS
HCHHHHHHCCEEECC		15.1222461510
313PhosphorylationYLGFSIDSGKGLVRA
HCCEEECCCCCEEEH		40.5122461510
345PhosphorylationVVILRKDSASRLVPE
EEEEECCCHHHHCCE		31.0427282143
347PhosphorylationILRKDSASRLVPEVM
EEECCCHHHHCCEEE		30.0524505115
413PhosphorylationGGHWAGISPLRLCGS
CCCCCCCCCHHCCCC		19.5724719451
526PhosphorylationLHVSHEVSIAPRSID
EEEECEEEECCCCCC		15.2824719451
638PhosphorylationRAIVVTLSYSLQTPR
HHHHHEEEHHCCCHH		11.87-
689PhosphorylationGEDKICQSNLQLVRA
CCCCHHHHHHHHHHH		34.7928102081
786N-linked_GlycosylationPLCLSNENASHVECE
CEECCCCCCCCEEEE		51.50UniProtKB CARBOHYD
876PhosphorylationRGERAMQSERDVGSK
CCCHHCCCCCCCCCE		22.8630631047
886PhosphorylationDVGSKVKYEVTVSNQ
CCCCEEEEEEEECCC		20.7224043423
889PhosphorylationSKVKYEVTVSNQGQS
CEEEEEEEECCCCCE		13.2824043423
891PhosphorylationVKYEVTVSNQGQSLR
EEEEEEECCCCCEEE		17.6724043423
896PhosphorylationTVSNQGQSLRTLGSA
EECCCCCEEEEEHHH		27.0024043423
911UbiquitinationFLNIMWPHEIANGKW
HHHHHCCHHHHCCCE		24.4721890473
911 (in isoform 9)Ubiquitination-24.4721890473
937 (in isoform 3)Phosphorylation-24.8324719451
977PhosphorylationERQEPSMSWWPVSSA
CCCCCCCCCCCCCCH		30.2624719451
987UbiquitinationPVSSAEKKKNITLDC
CCCCHHHCCCEEEEE		42.42-
988UbiquitinationVSSAEKKKNITLDCA
CCCHHHCCCEEEEEC		65.73-
989N-linked_GlycosylationSSAEKKKNITLDCAR
CCHHHCCCEEEEECC		41.16UniProtKB CARBOHYD
1025N-linked_GlycosylationHVWGRLWNSTFLEEY
HHHHHHHCCHHHHHH		35.4519159218
1045N-linked_GlycosylationLEVIVRANITVKSSI
EEEEHHCCEEECHHH		21.65UniProtKB CARBOHYD
1047PhosphorylationVIVRANITVKSSIKN
EEHHCCEEECHHHHH		22.9929449344
1050PhosphorylationRANITVKSSIKNLML
HCCEEECHHHHHHCC		32.7229449344
1051PhosphorylationANITVKSSIKNLMLR
CCEEECHHHHHHCCC		31.6829449344
1051 (in isoform 9)Ubiquitination-31.68-
1082 (in isoform 7)Ubiquitination-10.2821890473
1086 (in isoform 3)Ubiquitination-1.4921890473
1086UbiquitinationGVPWWVILLAVLAGL
CCCHHHHHHHHHHHH		1.4921890473
1110 (in isoform 3)Phosphorylation-49.5424719451
1122PhosphorylationPEATVPQYHAVKIPR
CCCCCCCCEEEECCH		5.9127642862
1126 (in isoform 1)Ubiquitination-48.0221890473
1126UbiquitinationVPQYHAVKIPREDRQ
CCCCEEEECCHHHHH		48.022189047
1150PhosphorylationILRNNWGSPRREGPD
CCCCCCCCCCCCCCC		13.5726029660
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 ITA7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITA7_HUMAN !!
Disease-associated PTM Sites based on SAP

* 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 ITA7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FHL2_HUMANFHL2physical
15117962
FHL3_HUMANFHL3physical
15117962
ACHA_HUMANCHRNA1physical
10910772
ITB1_HUMANITGB1physical
11278916
Drug and Disease Associations
Kegg Disease
H00590 Congenital muscular dystrophies (CMD/MDC), including: Merosin-deficient CMD (MDC1A); Ullrich CMD (UC
OMIM Disease
613204Muscular dystrophy congenital due to integrin alpha-7 deficiency (MDCI)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITA7_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-1025, AND MASSSPECTROMETRY.

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