VATB2_HUMAN - dbPTM
VATB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VATB2_HUMAN
UniProt AC P21281
Protein Name V-type proton ATPase subunit B, brain isoform
Gene Name ATP6V1B2
Organism Homo sapiens (Human).
Sequence Length 511
Subcellular Localization Endomembrane system
Peripheral membrane protein. Melanosome. Endomembrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells..
Protein Sequence MALRAMRGIVNGAAPELPVPTGGPAVGAREQALAVSRNYLSQPRLTYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFERNFIAQGPYENRTVFETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAKH
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
4Methylation----MALRAMRGIVN
----CHHHHHHCHHC
19.46-
7Methylation-MALRAMRGIVNGAA
-CHHHHHHCHHCCCC
30.60-
39PhosphorylationALAVSRNYLSQPRLT
HHHHCCCCCCCCCCE
13.4528152594
41PhosphorylationAVSRNYLSQPRLTYK
HHCCCCCCCCCCEEE
27.9824719451
44MethylationRNYLSQPRLTYKTVS
CCCCCCCCCEEEEEC
31.83-
48AcetylationSQPRLTYKTVSGVNG
CCCCCEEEEECCCCC
36.9025953088
48MalonylationSQPRLTYKTVSGVNG
CCCCCEEEEECCCCC
36.9026320211
48UbiquitinationSQPRLTYKTVSGVNG
CCCCCEEEEECCCCC
36.90-
49PhosphorylationQPRLTYKTVSGVNGP
CCCCEEEEECCCCCC
14.97-
51PhosphorylationRLTYKTVSGVNGPLV
CCEEEEECCCCCCEE
42.11-
642-HydroxyisobutyrylationLVILDHVKFPRYAEI
EEEEECCCCCCCEEE
46.35-
64UbiquitinationLVILDHVKFPRYAEI
EEEEECCCCCCCEEE
46.3521890473
64UbiquitinationLVILDHVKFPRYAEI
EEEEECCCCCCCEEE
46.3521890473
67MethylationLDHVKFPRYAEIVHL
EECCCCCCCEEEEEE
46.56-
68PhosphorylationDHVKFPRYAEIVHLT
ECCCCCCCEEEEEEE
14.6128152594
812-HydroxyisobutyrylationLTLPDGTKRSGQVLE
EECCCCCCCCCCEEE
50.53-
83PhosphorylationLPDGTKRSGQVLEVS
CCCCCCCCCCEEEEE
34.8221712546
90PhosphorylationSGQVLEVSGSKAVVQ
CCCEEEEECCEEEEE
28.1525693802
92PhosphorylationQVLEVSGSKAVVQVF
CEEEEECCEEEEEEE
15.2225693802
103PhosphorylationVQVFEGTSGIDAKKT
EEEEECCCCCCCCCC
44.6124719451
108MalonylationGTSGIDAKKTSCEFT
CCCCCCCCCCEEEEC
53.4926320211
108UbiquitinationGTSGIDAKKTSCEFT
CCCCCCCCCCEEEEC
53.49-
1082-HydroxyisobutyrylationGTSGIDAKKTSCEFT
CCCCCCCCCCEEEEC
53.49-
108AcetylationGTSGIDAKKTSCEFT
CCCCCCCCCCEEEEC
53.4925953088
109MalonylationTSGIDAKKTSCEFTG
CCCCCCCCCEEEECC
47.6026320211
1092-HydroxyisobutyrylationTSGIDAKKTSCEFTG
CCCCCCCCCEEEECC
47.60-
109UbiquitinationTSGIDAKKTSCEFTG
CCCCCCCCCEEEECC
47.60-
112S-nitrosylationIDAKKTSCEFTGDIL
CCCCCCEEEECCCCC
6.372212679
124PhosphorylationDILRTPVSEDMLGRV
CCCCCCCCHHHCHHH
29.14-
127SulfoxidationRTPVSEDMLGRVFNG
CCCCCHHHCHHHCCC
3.6230846556
137UbiquitinationRVFNGSGKPIDRGPV
HHCCCCCCCCCCCCE
40.26-
154SulfoxidationAEDFLDIMGQPINPQ
EHHHHHHCCCCCCCC
3.9921406390
162GlutathionylationGQPINPQCRIYPEEM
CCCCCCCCCCCHHHH
2.7722555962
169SulfoxidationCRIYPEEMIQTGISA
CCCCHHHHHHHCHHH
2.3430846556
180SulfoxidationGISAIDGMNSIARGQ
CHHHHHCCCHHHCCC
2.9330846556
182PhosphorylationSAIDGMNSIARGQKI
HHHHCCCHHHCCCCC
14.5618452278
185MethylationDGMNSIARGQKIPIF
HCCCHHHCCCCCCEE
46.54-
188UbiquitinationNSIARGQKIPIFSAA
CHHHCCCCCCEEECC
53.96-
222PhosphorylationKSKDVVDYSEENFAI
CCCCCCCCCHHHHHH
13.33-
289GlutathionylationAEFLAYQCEKHVLVI
HHHHHHHHHCCEEEE
4.9822555962
326PhosphorylationGRRGFPGYMYTDLAT
CCCCCCCCHHHHHHH
6.2821406692
327SulfoxidationRRGFPGYMYTDLATI
CCCCCCCHHHHHHHH
3.4430846556
328PhosphorylationRGFPGYMYTDLATIY
CCCCCCHHHHHHHHH
6.6621406692
329PhosphorylationGFPGYMYTDLATIYE
CCCCCHHHHHHHHHH
14.1721406692
333PhosphorylationYMYTDLATIYERAGR
CHHHHHHHHHHHHCC
31.2421406692
335PhosphorylationYTDLATIYERAGRVE
HHHHHHHHHHHCCCC
8.6021406692
389PhosphorylationQLHNRQIYPPINVLP
CCCCCCCCCCHHHHH
8.4620068231
397PhosphorylationPPINVLPSLSRLMKS
CCHHHHHHHHHHHHH
34.5120068231
399PhosphorylationINVLPSLSRLMKSAI
HHHHHHHHHHHHHHH
27.9220068231
403UbiquitinationPSLSRLMKSAIGEGM
HHHHHHHHHHHCCCC
41.13-
404PhosphorylationSLSRLMKSAIGEGMT
HHHHHHHHHHCCCCC
15.9121082442
410SulfoxidationKSAIGEGMTRKDHAD
HHHHCCCCCCCCHHH
2.5930846556
457UbiquitinationLYLEFLQKFERNFIA
HHHHHHHHHHHHCCC
51.87-
460MethylationEFLQKFERNFIAQGP
HHHHHHHHHCCCCCC
46.63-
498PhosphorylationMLKRIPQSTLSEFYP
HHHCCCHHHHHHHCC
26.4328857561
499PhosphorylationLKRIPQSTLSEFYPR
HHCCCHHHHHHHCCC
29.1124076635
501PhosphorylationRIPQSTLSEFYPRDS
CCCHHHHHHHCCCCC
26.2528857561
506MethylationTLSEFYPRDSAKH--
HHHHHCCCCCCCC--
38.85-
508PhosphorylationSEFYPRDSAKH----
HHHCCCCCCCC----
40.2628857561

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 VATB2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VATB2_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 VATB2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VATE1_HUMANATP6V1E1physical
22939629
VATD_HUMANATP6V1Dphysical
22939629
VATH_HUMANATP6V1Hphysical
22939629
VATF_HUMANATP6V1Fphysical
22939629
WDR5_HUMANWDR5physical
22939629
YIF1B_HUMANYIF1Bphysical
22939629
ANCHR_HUMANZFYVE19physical
22939629
VIGLN_HUMANHDLBPphysical
22939629
ZYX_HUMANZYXphysical
22939629
ZPR1_HUMANZPR1physical
22939629
ZBED1_HUMANZBED1physical
22939629
CUL2_HUMANCUL2physical
22863883
CSDE1_HUMANCSDE1physical
22863883
GANAB_HUMANGANABphysical
22863883
GMPPB_HUMANGMPPBphysical
22863883
HYOU1_HUMANHYOU1physical
22863883
PLAK_HUMANJUPphysical
22863883
MSH6_HUMANMSH6physical
22863883
SPT5H_HUMANSUPT5Hphysical
22863883
SWP70_HUMANSWAP70physical
22863883
XRCC6_HUMANXRCC6physical
22863883
ITF2_HUMANTCF4physical
25416956
ABCF3_HUMANABCF3physical
26344197
ATPG_HUMANATP5C1physical
26344197
VA0D1_HUMANATP6V0D1physical
26344197
VATA_HUMANATP6V1Aphysical
26344197
VATF_HUMANATP6V1Fphysical
26344197
VATH_HUMANATP6V1Hphysical
26344197
XPO2_HUMANCSE1Lphysical
26344197
MCA3_HUMANEEF1E1physical
26344197
GCC1_HUMANGCC1physical
26344197
SYIC_HUMANIARSphysical
26344197
CNOT9_HUMANRQCD1physical
26344197
RUVB1_HUMANRUVBL1physical
26344197
TMOD2_HUMANTMOD2physical
26344197
TBA1C_HUMANTUBA1Cphysical
26344197
WDR61_HUMANWDR61physical
26344197

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
DB05260Gallium nitrate
Regulatory Network of VATB2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP