ITB5_HUMAN - dbPTM
ITB5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ITB5_HUMAN
UniProt AC P18084
Protein Name Integrin beta-5
Gene Name ITGB5
Organism Homo sapiens (Human).
Sequence Length 799
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand.; (Microbial infection) Integrin ITGAV:ITGB5 acts as a receptor for adenovirus type C..
Protein Sequence MPRAPAPLYACLLGLCALLPRLAGLNICTSGSATSCEECLLIHPKCAWCSKEDFGSPRSITSRCDLRANLVKNGCGGEIESPASSFHVLRSLPLSSKGSGSAGWDVIQMTPQEIAVNLRPGDKTTFQLQVRQVEDYPVDLYYLMDLSLSMKDDLDNIRSLGTKLAEEMRKLTSNFRLGFGSFVDKDISPFSYTAPRYQTNPCIGYKLFPNCVPSFGFRHLLPLTDRVDSFNEEVRKQRVSRNRDAPEGGFDAVLQAAVCKEKIGWRKDALHLLVFTTDDVPHIALDGKLGGLVQPHDGQCHLNEANEYTASNQMDYPSLALLGEKLAENNINLIFAVTKNHYMLYKNFTALIPGTTVEILDGDSKNIIQLIINAYNSIRSKVELSVWDQPEDLNLFFTATCQDGVSYPGQRKCEGLKIGDTASFEVSLEARSCPSRHTEHVFALRPVGFRDSLEVGVTYNCTCGCSVGLEPNSARCNGSGTYVCGLCECSPGYLGTRCECQDGENQSVYQNLCREAEGKPLCSGRGDCSCNQCSCFESEFGKIYGPFCECDNFSCARNKGVLCSGHGECHCGECKCHAGYIGDNCNCSTDISTCRGRDGQICSERGHCLCGQCQCTEPGAFGEMCEKCPTCPDACSTKRDCVECLLLHSGKPDNQTCHSLCRDEVITWVDTIVKDDQEAVLCFYKTAKDCVMMFTYVELPSGKSNLTVLREPECGNTPNAMTILLAVVGSILLVGLALLAIWKLLVTIHDRREFAKFQSERSRARYEMASNPLYRKPISTHTVDFTFNKFNKSYNGTVD
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
59PhosphorylationEDFGSPRSITSRCDL
CCCCCCCCCHHHCHH		33.3328509920
61PhosphorylationFGSPRSITSRCDLRA
CCCCCCCHHHCHHHH		16.0322817900
62PhosphorylationGSPRSITSRCDLRAN
CCCCCCHHHCHHHHH		29.2828509920
141PhosphorylationEDYPVDLYYLMDLSL
CCCCEEEEEEEECCC		7.0628122231
142PhosphorylationDYPVDLYYLMDLSLS
CCCEEEEEEEECCCC		11.6628122231
147PhosphorylationLYYLMDLSLSMKDDL
EEEEEECCCCCCCCH		17.7128122231
149PhosphorylationYLMDLSLSMKDDLDN
EEEECCCCCCCCHHH		22.0224719451
181PhosphorylationNFRLGFGSFVDKDIS
CCCEECCCCCCCCCC		21.6027794612
188PhosphorylationSFVDKDISPFSYTAP
CCCCCCCCCCCCCCC		29.9920068231
192PhosphorylationKDISPFSYTAPRYQT
CCCCCCCCCCCCCCC		13.8020068231
193PhosphorylationDISPFSYTAPRYQTN
CCCCCCCCCCCCCCC		29.0520068231
199O-linked_GlycosylationYTAPRYQTNPCIGYK
CCCCCCCCCCCCCCC		31.9955833853
206AcetylationTNPCIGYKLFPNCVP
CCCCCCCCCCCCCCC		38.14132981
260UbiquitinationVLQAAVCKEKIGWRK
HHHHHHHHHHHCCCH		56.28-
347N-linked_GlycosylationNHYMLYKNFTALIPG
CCEEEECCEEEECCC		26.41UniProtKB CARBOHYD
460N-linked_GlycosylationLEVGVTYNCTCGCSV
EEECCEEECCCCCEE		12.78UniProtKB CARBOHYD
477N-linked_GlycosylationEPNSARCNGSGTYVC
CCCCCCCCCCCEEEE		41.95UniProtKB CARBOHYD
505N-linked_GlycosylationCECQDGENQSVYQNL
EEECCCCCHHHHHHH		44.98UniProtKB CARBOHYD
552N-linked_GlycosylationGPFCECDNFSCARNK
CCCCCCCCCCCCCCC		42.25UniProtKB CARBOHYD
586N-linked_GlycosylationGYIGDNCNCSTDIST
CCCCCCCCCCCCHHH		29.09UniProtKB CARBOHYD
654N-linked_GlycosylationLHSGKPDNQTCHSLC
HCCCCCCCHHHHHHH		47.81UniProtKB CARBOHYD
656PhosphorylationSGKPDNQTCHSLCRD
CCCCCCHHHHHHHHH		20.59-
659PhosphorylationPDNQTCHSLCRDEVI
CCCHHHHHHHHHHHE		31.17-
667PhosphorylationLCRDEVITWVDTIVK
HHHHHHEEEEEEEEC		25.3122144111
671PhosphorylationEVITWVDTIVKDDQE
HHEEEEEEEECCCHH		20.3222144111
685UbiquitinationEAVLCFYKTAKDCVM
HHHHHEEECHHHEEE		23.04-
701PhosphorylationFTYVELPSGKSNLTV
EEEEECCCCCCCEEE		72.0524719451
705N-linked_GlycosylationELPSGKSNLTVLREP
ECCCCCCCEEEEECC		43.12UniProtKB CARBOHYD
756UbiquitinationHDRREFAKFQSERSR
HHHHHHHHHHHHHHH		49.62-
759PhosphorylationREFAKFQSERSRARY
HHHHHHHHHHHHHHH		37.8022817900
762PhosphorylationAKFQSERSRARYEMA
HHHHHHHHHHHHHHC		26.6622817900
766PhosphorylationSERSRARYEMASNPL
HHHHHHHHHHCCCCC		14.7421945579
770PhosphorylationRARYEMASNPLYRKP
HHHHHHCCCCCCCCC		37.3621945579
774PhosphorylationEMASNPLYRKPISTH
HHCCCCCCCCCCCEE		20.1821945579
776UbiquitinationASNPLYRKPISTHTV
CCCCCCCCCCCEEEE		32.90-
779PhosphorylationPLYRKPISTHTVDFT
CCCCCCCCEEEEEEE		23.7430266825
780PhosphorylationLYRKPISTHTVDFTF
CCCCCCCEEEEEEEE		23.4530266825
782PhosphorylationRKPISTHTVDFTFNK
CCCCCEEEEEEEEEC		23.1230266825
786PhosphorylationSTHTVDFTFNKFNKS
CEEEEEEEEECCCHH		23.1030206219
792UbiquitinationFTFNKFNKSYNGTVD
EEEECCCHHCCCCCC		58.4021906983
793PhosphorylationTFNKFNKSYNGTVD-
EEECCCHHCCCCCC-		25.5729214152
794PhosphorylationFNKFNKSYNGTVD--
EECCCHHCCCCCC--		21.1521712546
797PhosphorylationFNKSYNGTVD-----
CCHHCCCCCC-----		20.1929214152
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
759SPhosphorylationKinasePAK4O96013
PSP
762SPhosphorylationKinasePAK4O96013
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ITB5_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 ITB5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANXA5_HUMANANXA5physical
12769841
FAK1_HUMANPTK2physical
11927607
CYR61_HUMANCYR61physical
11287419
PAK4_HUMANPAK4physical
12356872
ITA3_HUMANITGA3physical
16878156
FAK1_HUMANPTK2physical
15673687
SRSF9_HUMANSRSF9physical
21988832
EPHA2_HUMANEPHA2physical
23874206
EHMT2_HUMANEHMT2physical
25416956
MTUS2_HUMANMTUS2physical
25416956
K1C40_HUMANKRT40physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
ITA5_HUMANITGA5physical
22470492
ZBT17_HUMANZBTB17physical
12356872
ADAM9_HUMANADAM9physical
16373656
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D03497 Cilengitide (USAN/INN)
D09903 Fluciclatide F 18 (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ITB5_HUMAN

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Related Literatures of Post-Translational Modification

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