SPE39_HUMAN - dbPTM
SPE39_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPE39_HUMAN
UniProt AC Q9H9C1
Protein Name Spermatogenesis-defective protein 39 homolog
Gene Name VIPAS39
Organism Homo sapiens (Human).
Sequence Length 493
Subcellular Localization Cytoplasm. Cytoplasmic vesicle. Early endosome . Recycling endosome . Late endosome . Colocalizes in clusters with VPS33B at cytoplasmic organelles (PubMed:19109425).
Protein Description Proposed to be involved in endosomal maturation implicating in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical RAB11A-dependent recycling pathway and in the maintenance of the apical-basolateral polarity. [PubMed: 20190753 May play a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes; the functions seems to be indepenedent of VPS33B]
Protein Sequence MNRTKGDEEEYWNSSKFKAFTFDDEDDELSQLKESKRAVNSLRDFVDDDDDDDLERVSWSGEPVGSISWSIRETAGNSGSTHEGREQLKSRNSFSSYAQLPKPTSTYSLSSFFRGRTRPGSFQSLSDALSDTPAKSYAPELGRPKGEYRDYSNDWSPSDTVRRLRKGKVCSLERFRSLQDKLQLLEEAVSMHDGNVITAVLIFLKRTLSKEILFRELEVRQVALRHLIHFLKEIGDQKLLLDLFRFLDRTEELALSHYREHLNIQDPDKRKEFLKTCVGLPFSAEDSAHIQDHYTLLERQIIIEANDRHLESAGQTEIFRKHPRKASILNMPLVTTLFYSCFYHYTEAEGTFSSPVNLKKTFKIPDKQYVLTALAARAKLRAWNDVDALFTTKNWLGYTKKRAPIGFHRVVEILHKNNAPVQILQEYVNLVEDVDTKLNLATKFKCHDVVIDTYRDLKDRQQLLAYRSKVDKGSAEEEKIDALLSSSQIRWKN
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
5Ubiquitination---MNRTKGDEEEYW
---CCCCCCCHHHHH		62.21-
11PhosphorylationTKGDEEEYWNSSKFK
CCCCHHHHHCCCCCE		17.1125159151
14PhosphorylationDEEEYWNSSKFKAFT
CHHHHHCCCCCEEEE		22.2828102081
15PhosphorylationEEEYWNSSKFKAFTF
HHHHHCCCCCEEEEC		38.6126552605
16AcetylationEEYWNSSKFKAFTFD
HHHHCCCCCEEEECC		51.1825953088
16UbiquitinationEEYWNSSKFKAFTFD
HHHHCCCCCEEEECC		51.18-
18UbiquitinationYWNSSKFKAFTFDDE
HHCCCCCEEEECCCC		46.45-
21PhosphorylationSSKFKAFTFDDEDDE
CCCCEEEECCCCCCH		30.8922617229
30PhosphorylationDDEDDELSQLKESKR
CCCCCHHHHHHHHHH		31.2723403867
33UbiquitinationDDELSQLKESKRAVN
CCHHHHHHHHHHHHH		52.91-
66PhosphorylationWSGEPVGSISWSIRE
CCCCCCCEEEEEEEE		17.4328348404
68 (in isoform 2)Phosphorylation-19.2324275569
68PhosphorylationGEPVGSISWSIRETA
CCCCCEEEEEEEECC		19.2328348404
72 (in isoform 2)Phosphorylation-29.6929743597
75 (in isoform 2)Phosphorylation-15.4929116813
78PhosphorylationIRETAGNSGSTHEGR
EEECCCCCCCCHHHH		32.9525627689
90PhosphorylationEGREQLKSRNSFSSY
HHHHHHHHCCCCCCC		45.3323401153
93PhosphorylationEQLKSRNSFSSYAQL
HHHHHCCCCCCCCCC		25.9519664994
95PhosphorylationLKSRNSFSSYAQLPK
HHHCCCCCCCCCCCC		23.4322115753
96PhosphorylationKSRNSFSSYAQLPKP
HHCCCCCCCCCCCCC		23.6022115753
97PhosphorylationSRNSFSSYAQLPKPT
HCCCCCCCCCCCCCC		9.3628464451
104PhosphorylationYAQLPKPTSTYSLSS
CCCCCCCCCCCCCHH		39.5726657352
105PhosphorylationAQLPKPTSTYSLSSF
CCCCCCCCCCCCHHH		33.6027499020
106PhosphorylationQLPKPTSTYSLSSFF
CCCCCCCCCCCHHHH		21.4328464451
107PhosphorylationLPKPTSTYSLSSFFR
CCCCCCCCCCHHHHC		13.8428450419
108PhosphorylationPKPTSTYSLSSFFRG
CCCCCCCCCHHHHCC		23.1225849741
110PhosphorylationPTSTYSLSSFFRGRT
CCCCCCCHHHHCCCC		21.1128450419
111PhosphorylationTSTYSLSSFFRGRTR
CCCCCCHHHHCCCCC		33.4328450419
114MethylationYSLSSFFRGRTRPGS
CCCHHHHCCCCCCCC		31.5054556007
117PhosphorylationSSFFRGRTRPGSFQS
HHHHCCCCCCCCCHH		44.0023927012
118MethylationSFFRGRTRPGSFQSL
HHHCCCCCCCCCHHH		32.02115919845
121PhosphorylationRGRTRPGSFQSLSDA
CCCCCCCCCHHHHHH		23.8523927012
124PhosphorylationTRPGSFQSLSDALSD
CCCCCCHHHHHHHCC		28.0323927012
126PhosphorylationPGSFQSLSDALSDTP
CCCCHHHHHHHCCCC		26.5323927012
130PhosphorylationQSLSDALSDTPAKSY
HHHHHHHCCCCCHHC		40.9523927012
132PhosphorylationLSDALSDTPAKSYAP
HHHHHCCCCCHHCCH		23.0523927012
136PhosphorylationLSDTPAKSYAPELGR
HCCCCCHHCCHHHCC		28.7424719451
137PhosphorylationSDTPAKSYAPELGRP
CCCCCHHCCHHHCCC		26.0128555341
145UbiquitinationAPELGRPKGEYRDYS
CHHHCCCCCCCCCCC		64.11-
151PhosphorylationPKGEYRDYSNDWSPS
CCCCCCCCCCCCCCH		10.6128796482
156PhosphorylationRDYSNDWSPSDTVRR
CCCCCCCCCHHHHHH		19.8620873877
158PhosphorylationYSNDWSPSDTVRRLR
CCCCCCCHHHHHHHH		40.1620873877
168UbiquitinationVRRLRKGKVCSLERF
HHHHHCCCCCCHHHH		43.00-
275UbiquitinationDKRKEFLKTCVGLPF
HHHHHHHHHHHCCCC		45.24-
343PhosphorylationTLFYSCFYHYTEAEG
HHHHHHHHHHHHCCC		9.76-
363UbiquitinationVNLKKTFKIPDKQYV
CCCCCEECCCCHHHH		59.57-
369PhosphorylationFKIPDKQYVLTALAA
ECCCCHHHHHHHHHH		11.8129496907
391PhosphorylationNDVDALFTTKNWLGY
CCCCHHHHCCCCCCC		37.4025219547
392PhosphorylationDVDALFTTKNWLGYT
CCCHHHHCCCCCCCC		18.2925219547
393UbiquitinationVDALFTTKNWLGYTK
CCHHHHCCCCCCCCC		42.97-
398PhosphorylationTTKNWLGYTKKRAPI
HCCCCCCCCCCCCCC		17.1425219547
399PhosphorylationTKNWLGYTKKRAPIG
CCCCCCCCCCCCCCC		28.4325219547
443AcetylationTKLNLATKFKCHDVV
HHHHHHHHCCCCEEE		36.9025953088
479UbiquitinationKGSAEEEKIDALLSS
CCCCHHHHHHHHHHH		49.52-
485PhosphorylationEKIDALLSSSQIRWK
HHHHHHHHHCCCCCC		28.8829514088
486PhosphorylationKIDALLSSSQIRWKN
HHHHHHHHCCCCCCC		26.6529514088
487PhosphorylationIDALLSSSQIRWKN-
HHHHHHHCCCCCCC-		26.6725159151
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 SPE39_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPE39_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 SPE39_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VP33A_HUMANVPS33Aphysical
19109425
VP33B_HUMANVPS33Bphysical
19109425
VPS41_HUMANVPS41physical
19109425
VPS18_MOUSEVps18physical
19109425
VPS11_MOUSEVps11physical
19109425
VPS39_MOUSEVps39physical
19109425
VP33B_HUMANVPS33Bphysical
22939629
VPS39_HUMANVPS39physical
22939629
VP33B_HUMANVPS33Bphysical
25783203
VP33B_HUMANVPS33Bphysical
26463206
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613404Arthrogryposis, renal dysfunction and cholestasis syndrome 2 (ARCS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPE39_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-124 ANDTHR-132, AND MASS SPECTROMETRY.
"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-121 AND THR-132, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11, AND MASSSPECTROMETRY.

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