VMA5A_HUMAN - dbPTM
VMA5A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VMA5A_HUMAN
UniProt AC O00534
Protein Name von Willebrand factor A domain-containing protein 5A
Gene Name VWA5A
Organism Homo sapiens (Human).
Sequence Length 786
Subcellular Localization
Protein Description May play a role in tumorigenesis as a tumor suppressor. Altered expression of this protein and disruption of the molecular pathway it is involved in, may contribute directly to or modify tumorigenesis..
Protein Sequence MVHFCGLLTLHREPVPLKSISVSVNIYEFVAGVSATLNYENEEKVPLEAFFVFPMDEDSAVYSFEALVDGKKIVAELQDKMKARTNYEKAISQGHQAFLLEGDSSSRDVFSCNVGNLQPGSKAAVTLKYVQELPLEADGALRFVLPAVLNPRYQFSGSSKDSCLNVKTPIVPVEDLPYTLSMVATIDSQHGIEKVQSNCPLSPTEYLGEDKTSAQVSLAAGHKFDRDVELLIYYNEVHTPSVVLEMGMPNMKPGHLMGDPSAMVSFYPNIPEDQPSNTCGEFIFLMDRSGSMQSPMSSQDTSQLRIQAAKETLILLLKSLPIGCYFNIYGFGSSYEACFPESVKYTQQTMEEALGRVKLMQADLGGTEILAPLQNIYRGPSIPGHPLQLFVFTDGEVTDTFSVIKEVRINRQKHRCFSFGIGEGTSTSLIKGIARASGGTSEFITGKDRMQSKALRTLKRSLQPVVEDVSLSWHLPPGLSAKMLSPEQTVIFRGQRLISYAQLTGRMPAAETTGEVCLKYTLQGKTFEDKVTFPLQPKPDVNLTIHRLAAKSLLQTKDMGLRETPASDKKDALNLSLESGVISSFTAFIAINKELNKPVQGPLAHRDVPRPILLGASAPLKIKCQSGFRKALHSDRPPSASQPRGELMCYKAKTFQMDDYSLCGLISHKDQHSPGFGENHLVQLIYHQNANGSWDLNEDLAKILGMSLEEIMAAQPAELVDSSGWATILAVIWLHSNGKDLKCEWELLERKAVAWMRAHAGSTMPSVVKAAITFLKSSVDPAIFAF
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
9PhosphorylationVHFCGLLTLHREPVP
CCCCCEEEECCCCCC		26.09-
72UbiquitinationEALVDGKKIVAELQD
EEEECCHHHHHHHHH		48.20-
80UbiquitinationIVAELQDKMKARTNY
HHHHHHHHHHHCCCH		29.37-
89UbiquitinationKARTNYEKAISQGHQ
HHCCCHHHHHHHCCC		40.43-
92PhosphorylationTNYEKAISQGHQAFL
CCHHHHHHHCCCEEE		34.6628387310
104PhosphorylationAFLLEGDSSSRDVFS
EEEECCCCCCCCEEE		40.8625159151
105PhosphorylationFLLEGDSSSRDVFSC
EEECCCCCCCCEEEE		33.8526657352
106PhosphorylationLLEGDSSSRDVFSCN
EECCCCCCCCEEEEE		36.1325159151
121PhosphorylationVGNLQPGSKAAVTLK
CCCCCCCCEEEEEEE		26.2928387310
122UbiquitinationGNLQPGSKAAVTLKY
CCCCCCCEEEEEEEE		46.40-
126PhosphorylationPGSKAAVTLKYVQEL
CCCEEEEEEEEEEEC		16.8928387310
128UbiquitinationSKAAVTLKYVQELPL
CEEEEEEEEEEECCC		33.73-
160UbiquitinationYQFSGSSKDSCLNVK
CCCCCCCCCCCCCCC		56.19-
162PhosphorylationFSGSSKDSCLNVKTP
CCCCCCCCCCCCCCC		25.0027251275
178PhosphorylationVPVEDLPYTLSMVAT
EEHHHCCCEEEEEEE		27.8424275569
179PhosphorylationPVEDLPYTLSMVATI
EHHHCCCEEEEEEEE		15.4924275569
181PhosphorylationEDLPYTLSMVATIDS
HHCCCEEEEEEEEEH		11.9224275569
185PhosphorylationYTLSMVATIDSQHGI
CEEEEEEEEEHHCCH		17.5724275569
188PhosphorylationSMVATIDSQHGIEKV
EEEEEEEHHCCHHHH		21.8924275569
202PhosphorylationVQSNCPLSPTEYLGE
HHHCCCCCCCCCCCC		18.2121815630
204PhosphorylationSNCPLSPTEYLGEDK
HCCCCCCCCCCCCCC		33.61-
289PhosphorylationFIFLMDRSGSMQSPM
EEEEEECCCCCCCCC		30.84-
291PhosphorylationFLMDRSGSMQSPMSS
EEEECCCCCCCCCCC		18.20-
310UbiquitinationQLRIQAAKETLILLL
HHHHHHHHHHHHHHH		55.00-
345PhosphorylationCFPESVKYTQQTMEE
HCCHHHHHHHHHHHH		13.9726657352
346PhosphorylationFPESVKYTQQTMEEA
CCHHHHHHHHHHHHH		14.4226657352
349PhosphorylationSVKYTQQTMEEALGR
HHHHHHHHHHHHHHH		19.4126657352
358UbiquitinationEEALGRVKLMQADLG
HHHHHHHEEEECCCC		36.56-
381PhosphorylationQNIYRGPSIPGHPLQ
CHHHCCCCCCCCCEE		44.21-
418PhosphorylationRQKHRCFSFGIGEGT
CCCCEEEEECCCCCC		26.6225867546
425PhosphorylationSFGIGEGTSTSLIKG
EECCCCCCCHHHHHH		25.2425867546
426PhosphorylationFGIGEGTSTSLIKGI
ECCCCCCCHHHHHHH		27.1925867546
427PhosphorylationGIGEGTSTSLIKGIA
CCCCCCCHHHHHHHH		27.6525867546
428PhosphorylationIGEGTSTSLIKGIAR
CCCCCCHHHHHHHHH		28.0624719451
447UbiquitinationTSEFITGKDRMQSKA
CCCCCCCCHHHHHHH		33.25-
485PhosphorylationGLSAKMLSPEQTVIF
CCCCCCCCCCCEEEE		23.9224719451
489PhosphorylationKMLSPEQTVIFRGQR
CCCCCCCEEEECCEE		17.5724719451
525UbiquitinationLKYTLQGKTFEDKVT
EEEEECCCCEECEEE		36.76-
597UbiquitinationAINKELNKPVQGPLA
HHHHHCCCCCCCCCC		60.22-
617PhosphorylationRPILLGASAPLKIKC
CCEEECCCCCCEEEE		28.7223312004
621UbiquitinationLGASAPLKIKCQSGF
ECCCCCCEEEECCCH		38.7720972266
623UbiquitinationASAPLKIKCQSGFRK
CCCCCEEEECCCHHH		25.32-
630UbiquitinationKCQSGFRKALHSDRP
EECCCHHHHHHCCCC		53.70-
634PhosphorylationGFRKALHSDRPPSAS
CHHHHHHCCCCCCCC		35.8428857561
639PhosphorylationLHSDRPPSASQPRGE
HHCCCCCCCCCCCCE		43.1425159151
641PhosphorylationSDRPPSASQPRGELM
CCCCCCCCCCCCEEE		45.0923312004
653UbiquitinationELMCYKAKTFQMDDY
EEEEEEEEEEECCCC		45.80-
654PhosphorylationLMCYKAKTFQMDDYS
EEEEEEEEEECCCCC		24.7823312004
660PhosphorylationKTFQMDDYSLCGLIS
EEEECCCCCEEHHHC		10.1625159151
661PhosphorylationTFQMDDYSLCGLISH
EEECCCCCEEHHHCC		24.95-
673PhosphorylationISHKDQHSPGFGENH
HCCCCCCCCCCCCCC		22.5327251275
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 VMA5A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VMA5A_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 VMA5A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
MCM9_HUMANMCM9physical
28514442
ZHANG_HUMANCREBZFphysical
28514442
MA2C1_HUMANMAN2C1physical
28514442
PKNX2_HUMANPKNOX2physical
28514442
PBX3_HUMANPBX3physical
28514442
ARMX3_HUMANARMCX3physical
28514442
HIC2_HUMANHIC2physical
28514442
PTN23_HUMANPTPN23physical
28514442
PBX1_HUMANPBX1physical
28514442
ADDG_HUMANADD3physical
28514442
MCM8_HUMANMCM8physical
28514442
UBB_HUMANUBBphysical
28514442
PEAK1_HUMANPEAK1physical
28514442
SETX_HUMANSETXphysical
28514442
PKNX1_HUMANPKNOX1physical
28514442
SAMD1_HUMANSAMD1physical
28514442
PBX2_HUMANPBX2physical
28514442
MRRP1_HUMANTRMT10Cphysical
28514442
UBR4_HUMANUBR4physical
28514442
UCKL1_HUMANUCKL1physical
28514442
EHD4_HUMANEHD4physical
28514442
FANCJ_HUMANBRIP1physical
28514442
RTEL1_HUMANRTEL1physical
28514442
KCMF1_HUMANKCMF1physical
28514442
BCAS3_HUMANBCAS3physical
28514442
PAPD1_HUMANMTPAPphysical
28514442
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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VMA5A_HUMAN

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Related Literatures of Post-Translational Modification

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