VAC14_HUMAN - dbPTM
VAC14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VAC14_HUMAN
UniProt AC Q08AM6
Protein Name Protein VAC14 homolog
Gene Name VAC14
Organism Homo sapiens (Human).
Sequence Length 782
Subcellular Localization Endosome membrane . Microsome membrane. Mainly associated with membranes of the late endocytic pathway.
Protein Description The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Acts as a positive activator of PIKfyve kinase activity. Also required to maintain normal levels of phosphatidylinositol 3-phosphate (PtdIns(3)P) and phosphatidylinositol 5-phosphate (PtdIns(5)P). Plays a role in the biogenesis of endosome carrier vesicles (ECV) / multivesicular bodies (MVB) transport intermediates from early endosomes..
Protein Sequence MNPEKDFAPLTPNIVRALNDKLYEKRKVAALEIEKLVREFVAQNNTVQIKHVIQTLSQEFALSQHPHSRKGGLIGLAACSIALGKDSGLYLKELIEPVLTCFNDADSRLRYYACEALYNIVKVARGAVLPHFNVLFDGLSKLAADPDPNVKSGSELLDRLLKDIVTESNKFDLVSFIPLLRERIYSNNQYARQFIISWILVLESVPDINLLDYLPEILDGLFQILGDNGKEIRKMCEVVLGEFLKEIKKNPSSVKFAEMANILVIHCQTTDDLIQLTAMCWMREFIQLAGRVMLPYSSGILTAVLPCLAYDDRKKSIKEVANVCNQSLMKLVTPEDDELDELRPGQRQAEPTPDDALPKQEGTASGGPDGSCDSSFSSGISVFTAASTERAPVTLHLDGIVQVLNCHLSDTAIGMMTRIAVLKWLYHLYIKTPRKMFRHTDSLFPILLQTLSDESDEVILKDLEVLAEIASSPAGQTDDPGPLDGPDLQASHSELQVPTPGRAGLLNTSGTKGLECSPSTPTMNSYFYKFMINLLKRFSSERKLLEVRGPFIIRQLCLLLNAENIFHSMADILLREEDLKFASTMVHALNTILLTSTELFQLRNQLKDLKTLESQNLFCCLYRSWCHNPVTTVSLCFLTQNYRHAYDLIQKFGDLEVTVDFLAEVDKLVQLIECPIFTYLRLQLLDVKNNPYLIKALYGLLMLLPQSSAFQLLSHRLQCVPNPELLQTEDSLKAAPKSQKADSPSIDYAELLQHFEKVQNKHLEVRHQRSGRGDHLDRRVVL
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
1Acetylation-------MNPEKDFA
-------CCHHHHCC		19.9422814378
5Ubiquitination---MNPEKDFAPLTP
---CCHHHHCCCCCH		60.44-
11PhosphorylationEKDFAPLTPNIVRAL
HHHCCCCCHHHHHHH		17.1522617229
21AcetylationIVRALNDKLYEKRKV
HHHHHHHHHHHHHHH		52.4725953088
21MalonylationIVRALNDKLYEKRKV
HHHHHHHHHHHHHHH		52.4726320211
21UbiquitinationIVRALNDKLYEKRKV
HHHHHHHHHHHHHHH		52.4729967540
27MalonylationDKLYEKRKVAALEIE
HHHHHHHHHHHHHHH		47.4926320211
35UbiquitinationVAALEIEKLVREFVA
HHHHHHHHHHHHHHH		58.9229967540
70UbiquitinationSQHPHSRKGGLIGLA
HCCCCCCCCCHHHHH		61.41-
107PhosphorylationTCFNDADSRLRYYAC
HHCCCCCHHHHHHHH		34.6328634120
151UbiquitinationADPDPNVKSGSELLD
CCCCCCCCCHHHHHH		56.6029967540
152PhosphorylationDPDPNVKSGSELLDR
CCCCCCCCHHHHHHH		43.1823532336
154PhosphorylationDPNVKSGSELLDRLL
CCCCCCHHHHHHHHH		31.9623532336
170UbiquitinationDIVTESNKFDLVSFI
HHHHHCCCCCHHHHH		49.9233845483
185PhosphorylationPLLRERIYSNNQYAR
HHHHHHHHCCCHHHH		16.15-
186PhosphorylationLLRERIYSNNQYARQ
HHHHHHHCCCHHHHH		27.25-
190PhosphorylationRIYSNNQYARQFIIS
HHHCCCHHHHHHHHH		13.08-
296PhosphorylationAGRVMLPYSSGILTA
HCCHHCCCCCCHHHH		16.1125072903
297PhosphorylationGRVMLPYSSGILTAV
CCHHCCCCCCHHHHH		21.8325072903
298PhosphorylationRVMLPYSSGILTAVL
CHHCCCCCCHHHHHH		24.8225072903
302PhosphorylationPYSSGILTAVLPCLA
CCCCCHHHHHHHHHH		16.8825072903
310PhosphorylationAVLPCLAYDDRKKSI
HHHHHHHCHHHHHHH		12.8625072903
318UbiquitinationDDRKKSIKEVANVCN
HHHHHHHHHHHHHHC		53.9129967540
327PhosphorylationVANVCNQSLMKLVTP
HHHHHCHHHHHHCCC		19.2130622161
329SulfoxidationNVCNQSLMKLVTPED
HHHCHHHHHHCCCCC		3.7021406390
352PhosphorylationGQRQAEPTPDDALPK
CCCCCCCCCCCCCCC		30.7521815630
363PhosphorylationALPKQEGTASGGPDG
CCCCCCCCCCCCCCC		19.5222210691
365PhosphorylationPKQEGTASGGPDGSC
CCCCCCCCCCCCCCC		44.0922210691
374PhosphorylationGPDGSCDSSFSSGIS
CCCCCCCCCCCCCEE		37.3027251275
375PhosphorylationPDGSCDSSFSSGISV
CCCCCCCCCCCCEEE		18.8527251275
471PhosphorylationEVLAEIASSPAGQTD
HHHHHHHCCCCCCCC		42.3828102081
472PhosphorylationVLAEIASSPAGQTDD
HHHHHHCCCCCCCCC		15.1128102081
477PhosphorylationASSPAGQTDDPGPLD
HCCCCCCCCCCCCCC		41.2628102081
491PhosphorylationDGPDLQASHSELQVP
CCCCCCCCCCCCCCC		18.0028102081
493PhosphorylationPDLQASHSELQVPTP
CCCCCCCCCCCCCCC		37.1924173317
499PhosphorylationHSELQVPTPGRAGLL
CCCCCCCCCCCCCCC		39.2517192257
508PhosphorylationGRAGLLNTSGTKGLE
CCCCCCCCCCCCCCC		28.6221082442
509PhosphorylationRAGLLNTSGTKGLEC
CCCCCCCCCCCCCCC		43.3125159151
511PhosphorylationGLLNTSGTKGLECSP
CCCCCCCCCCCCCCC		23.0025159151
517PhosphorylationGTKGLECSPSTPTMN
CCCCCCCCCCCCCHH		16.7125159151
519PhosphorylationKGLECSPSTPTMNSY
CCCCCCCCCCCHHHH		30.6321815630
520PhosphorylationGLECSPSTPTMNSYF
CCCCCCCCCCHHHHH		26.6021815630
522PhosphorylationECSPSTPTMNSYFYK
CCCCCCCCHHHHHHH		29.1327732954
525PhosphorylationPSTPTMNSYFYKFMI
CCCCCHHHHHHHHHH		13.0427732954
526PhosphorylationSTPTMNSYFYKFMIN
CCCCHHHHHHHHHHH		13.1127732954
634PhosphorylationHNPVTTVSLCFLTQN
CCCCCHHHHHHHCCC		19.8230631047
646PhosphorylationTQNYRHAYDLIQKFG
CCCHHHHHHHHHHHC		12.7320071362
740UbiquitinationKAAPKSQKADSPSID
HHCCCCCCCCCCCCC		62.3429967540
743PhosphorylationPKSQKADSPSIDYAE
CCCCCCCCCCCCHHH		25.9630266825
745PhosphorylationSQKADSPSIDYAELL
CCCCCCCCCCHHHHH		31.8530266825
748PhosphorylationADSPSIDYAELLQHF
CCCCCCCHHHHHHHH		10.5823186163
757UbiquitinationELLQHFEKVQNKHLE
HHHHHHHHHHHCCHH		48.4529967540
770PhosphorylationLEVRHQRSGRGDHLD
HHHHHCCCCCCCCCC		26.6922817900
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 VAC14_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VAC14_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 VAC14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VAC14_HUMANVAC14physical
19037259
A4_HUMANAPPphysical
21832049
VIP2_HUMANPPIP5K2physical
22939629
VIP1_HUMANPPIP5K1physical
22939629
PELI1_HUMANPELI1physical
25416956
SPRY7_HUMANSPRYD7physical
25416956
NGB_HUMANNGBphysical
25416956
FND3B_HUMANFNDC3Bphysical
25416956
MTMR9_HUMANMTMR9physical
25416956
ASB13_HUMANASB13physical
25416956
ZNF34_HUMANZNF34physical
25416956
PADC1_HUMANPRADC1physical
25416956
RHXF2_HUMANRHOXF2physical
25416956
ACS2L_HUMANACSS1physical
25416956
AT2L2_HUMANPHYKPLphysical
25416956
PR20E_HUMANPRR20Aphysical
25416956
PR20C_HUMANPRR20Aphysical
25416956
PR20D_HUMANPRR20Aphysical
25416956
PR20B_HUMANPRR20Aphysical
25416956
PR20A_HUMANPRR20Aphysical
25416956
CD033_HUMANC4orf33physical
25416956
MGT5B_HUMANMGAT5Bphysical
25416956
TEANC_HUMANTCEANCphysical
25416956
FYV1_HUMANPIKFYVEphysical
25416956
CDRT4_HUMANCDRT4physical
25416956
KR195_HUMANKRTAP19-5physical
25416956
KR197_HUMANKRTAP19-7physical
25416956
CC103_HUMANCCDC103physical
25416956
JMJD7_HUMANJMJD7physical
25416956
FIG4_HUMANFIG4physical
28514442
FYV1_HUMANPIKFYVEphysical
28514442
ERGI2_HUMANERGIC2physical
28514442
MAOX_HUMANME1physical
28514442
LNP_HUMANKIAA1715physical
28514442
FACE1_HUMANZMPSTE24physical
28514442
CLCN7_HUMANCLCN7physical
28514442
MAVS_HUMANMAVSphysical
28514442
RAB21_HUMANRAB21physical
28514442
S26A6_HUMANSLC26A6physical
28514442
MTCH2_HUMANMTCH2physical
28514442
ERGI3_HUMANERGIC3physical
28514442
PRAF2_HUMANPRAF2physical
28514442
MPZL1_HUMANMPZL1physical
28514442
QKI_HUMANQKIphysical
28514442
AT2B2_HUMANATP2B2physical
28514442
AT2B4_HUMANATP2B4physical
28514442
SLMAP_HUMANSLMAPphysical
28514442
PYRD_HUMANDHODHphysical
28514442
VAMP3_HUMANVAMP3physical
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 VAC14_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491; THR-508 ANDSER-770, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11 AND THR-499, AND MASSSPECTROMETRY.

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