VP37A_HUMAN - dbPTM
VP37A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VP37A_HUMAN
UniProt AC Q8NEZ2
Protein Name Vacuolar protein sorting-associated protein 37A
Gene Name VPS37A
Organism Homo sapiens (Human).
Sequence Length 397
Subcellular Localization Late endosome membrane
Peripheral membrane protein. Nucleus.
Protein Description Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation..
Protein Sequence MSWLFPLTKSASSSAAGSPGGLTSLQQQKQRLIESLRNSHSSIAEIQKDVEYRLPFTINNLTININILLPPQFPQEKPVISVYPPIRHHLMDKQGVYVTSPLVNNFTMHSDLGKIIQSLLDEFWKNPPVLAPTSTAFPYLYSNPSGMSPYASQGFPFLPPYPPQEANRSITSLSVADTVSSSTTSHTTAKPAAPSFGVLSNLPLPIPTVDASIPTSQNGFGYKMPDVPDAFPELSELSVSQLTDMNEQEEVLLEQFLTLPQLKQIITDKDDLVKSIEELARKNLLLEPSLEAKRQTVLDKYELLTQMKSTFEKKMQRQHELSESCSASALQARLKVAAHEAEEESDNIAEDFLEGKMEIDDFLSSFMEKRTICHCRRAKEEKLQQAIAMHSQFHAPL
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
2Phosphorylation------MSWLFPLTK
------CCCCEECCC		32.2727251275
8PhosphorylationMSWLFPLTKSASSSA
CCCCEECCCCCCCCC		24.1625690035
10PhosphorylationWLFPLTKSASSSAAG
CCEECCCCCCCCCCC		28.3125159151
12PhosphorylationFPLTKSASSSAAGSP
EECCCCCCCCCCCCC		31.7326657352
13PhosphorylationPLTKSASSSAAGSPG
ECCCCCCCCCCCCCC		24.5825159151
14PhosphorylationLTKSASSSAAGSPGG
CCCCCCCCCCCCCCC		21.4625159151
18PhosphorylationASSSAAGSPGGLTSL
CCCCCCCCCCCHHHH		18.6925159151
29 (in isoform 3)Ubiquitination-32.8021906983
29 (in isoform 2)Ubiquitination-32.8021906983
29 (in isoform 1)Ubiquitination-32.8021906983
29UbiquitinationLTSLQQQKQRLIESL
HHHHHHHHHHHHHHH		32.8022817900
70UbiquitinationININILLPPQFPQEK
EEEEEECCCCCCCCC		19.7324816145
100PhosphorylationKQGVYVTSPLVNNFT
CCCEEECCCCCCCEE		13.2425627689
169O-linked_GlycosylationPPQEANRSITSLSVA
CCHHHCCCCEEEEHH		29.9930059200
172O-linked_GlycosylationEANRSITSLSVADTV
HHCCCCEEEEHHHCC		19.5830059200
172PhosphorylationEANRSITSLSVADTV
HHCCCCEEEEHHHCC		19.5830576142
174O-linked_GlycosylationNRSITSLSVADTVSS
CCCCEEEEHHHCCCC		18.2830059200
178O-linked_GlycosylationTSLSVADTVSSSTTS
EEEEHHHCCCCCCCC		16.7330059200
178PhosphorylationTSLSVADTVSSSTTS
EEEEHHHCCCCCCCC		16.7330576142
180O-linked_GlycosylationLSVADTVSSSTTSHT
EEHHHCCCCCCCCCC		22.2130059200
181PhosphorylationSVADTVSSSTTSHTT
EHHHCCCCCCCCCCC		27.6330576142
182PhosphorylationVADTVSSSTTSHTTA
HHHCCCCCCCCCCCC		28.3530576142
182O-linked_GlycosylationVADTVSSSTTSHTTA
HHHCCCCCCCCCCCC		28.3530059200
183O-linked_GlycosylationADTVSSSTTSHTTAK
HHCCCCCCCCCCCCC		33.9830059200
183PhosphorylationADTVSSSTTSHTTAK
HHCCCCCCCCCCCCC		33.9830576142
184O-linked_GlycosylationDTVSSSTTSHTTAKP
HCCCCCCCCCCCCCC		22.0630059200
188O-linked_GlycosylationSSTTSHTTAKPAAPS
CCCCCCCCCCCCCCC		27.5330059200
203UbiquitinationFGVLSNLPLPIPTVD
CCCCCCCCCCCCCCC		40.1024816145
215O-linked_GlycosylationTVDASIPTSQNGFGY
CCCCCCCCCCCCCCC		41.0730059200
239UbiquitinationPELSELSVSQLTDMN
HHHHHCCHHHHCCCC		7.0829901268
244UbiquitinationLSVSQLTDMNEQEEV
CCHHHHCCCCHHHHH		46.6429967540
245UbiquitinationSVSQLTDMNEQEEVL
CHHHHCCCCHHHHHH		5.1129901268
257UbiquitinationEVLLEQFLTLPQLKQ
HHHHHHHHCHHHHHH		4.8629967540
268UbiquitinationQLKQIITDKDDLVKS
HHHHHHCCHHHHHHH		41.8124816145
269UbiquitinationLKQIITDKDDLVKSI
HHHHHCCHHHHHHHH		44.4829967540
282UbiquitinationSIEELARKNLLLEPS
HHHHHHHCCCCCCCC		46.4729967540
289PhosphorylationKNLLLEPSLEAKRQT
CCCCCCCCHHHHHHH		29.48-
293AcetylationLEPSLEAKRQTVLDK
CCCCHHHHHHHHHHH		35.3525953088
293UbiquitinationLEPSLEAKRQTVLDK
CCCCHHHHHHHHHHH		35.3524816145
296PhosphorylationSLEAKRQTVLDKYEL
CHHHHHHHHHHHHHH		27.3729449344
301PhosphorylationRQTVLDKYELLTQMK
HHHHHHHHHHHHHHH		16.1022461510
310UbiquitinationLLTQMKSTFEKKMQR
HHHHHHHHHHHHHHH		30.2329901268
310PhosphorylationLLTQMKSTFEKKMQR
HHHHHHHHHHHHHHH		30.2322461510
329UbiquitinationSESCSASALQARLKV
CHHHCHHHHHHHHHH		11.9229901268
335UbiquitinationSALQARLKVAAHEAE
HHHHHHHHHHHHHHH		25.0329901268
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 VP37A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VP37A_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 VP37A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TS101_HUMANTSG101physical
15240819
VPS28_HUMANVPS28physical
15240819
A4_HUMANAPPphysical
21832049
KDM1A_HUMANKDM1Aphysical
23455924
UBAP1_HUMANUBAP1physical
24284069
TRI42_HUMANTRIM42physical
25416956
UBAP1_HUMANUBAP1physical
21757351
TS101_HUMANTSG101physical
21757351
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614898Spastic paraplegia 53, autosomal recessive (SPG53)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VP37A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.

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