S35B2_HUMAN - dbPTM
S35B2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S35B2_HUMAN
UniProt AC Q8TB61
Protein Name Adenosine 3'-phospho 5'-phosphosulfate transporter 1
Gene Name SLC35B2
Organism Homo sapiens (Human).
Sequence Length 432
Subcellular Localization Golgi apparatus membrane
Multi-pass membrane protein .
Protein Description Mediates the transport of adenosine 3'-phospho 5'-phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. May indirectly participate in activation of the NF-kappa-B and MAPK pathways..
Protein Sequence MDARWWAVVVLAAFPSLGAGGETPEAPPESWTQLWFFRFVVNAAGYASFMVPGYLLVQYFRRKNYLETGRGLCFPLVKACVFGNEPKASDEVPLAPRTEAAETTPMWQALKLLFCATGLQVSYLTWGVLQERVMTRSYGATATSPGERFTDSQFLVLMNRVLALIVAGLSCVLCKQPRHGAPMYRYSFASLSNVLSSWCQYEALKFVSFPTQVLAKASKVIPVMLMGKLVSRRSYEHWEYLTATLISIGVSMFLLSSGPEPRSSPATTLSGLILLAGYIAFDSFTSNWQDALFAYKMSSVQMMFGVNFFSCLFTVGSLLEQGALLEGTRFMGRHSEFAAHALLLSICSACGQLFIFYTIGQFGAAVFTIIMTLRQAFAILLSCLLYGHTVTVVGGLGVAVVFAALLLRVYARGRLKQRGKKAVPVESPVQKV
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
14UbiquitinationAVVVLAAFPSLGAGG
HHHHHHHCCCCCCCC		3.3424816145
29UbiquitinationETPEAPPESWTQLWF
CCCCCCCCCHHHHHH		58.8233845483
38UbiquitinationWTQLWFFRFVVNAAG
HHHHHHHHHHHHHHH		17.6133845483
54PhosphorylationASFMVPGYLLVQYFR
HHHHCCHHHHHHHHH		7.2718083107
63UbiquitinationLVQYFRRKNYLETGR
HHHHHHHHCCCCCCC		45.7633845483
73UbiquitinationLETGRGLCFPLVKAC
CCCCCCCHHHHHHHH		3.5332015554
73S-palmitoylationLETGRGLCFPLVKAC
CCCCCCCHHHHHHHH		3.5329575903
78UbiquitinationGLCFPLVKACVFGNE
CCHHHHHHHHHHCCC		43.6933845483
80S-palmitoylationCFPLVKACVFGNEPK
HHHHHHHHHHCCCCC		1.8429575903
82UbiquitinationPLVKACVFGNEPKAS
HHHHHHHHCCCCCCC		9.7633845483
83UbiquitinationLVKACVFGNEPKASD
HHHHHHHCCCCCCCC		19.7329967540
86UbiquitinationACVFGNEPKASDEVP
HHHHCCCCCCCCCCC		41.3229967540
87UbiquitinationCVFGNEPKASDEVPL
HHHCCCCCCCCCCCC		55.1133845483
111UbiquitinationTPMWQALKLLFCATG
CHHHHHHHHHHHHHC		46.2729967540
114UbiquitinationWQALKLLFCATGLQV
HHHHHHHHHHHCCHH		3.7429967540
123UbiquitinationATGLQVSYLTWGVLQ
HHCCHHHHHHHHHHH		14.8629967540
126UbiquitinationLQVSYLTWGVLQERV
CHHHHHHHHHHHHHH		7.7229967540
135PhosphorylationVLQERVMTRSYGATA
HHHHHHHHHCCCCCC		17.38-
137PhosphorylationQERVMTRSYGATATS
HHHHHHHCCCCCCCC		20.8228152594
138PhosphorylationERVMTRSYGATATSP
HHHHHHCCCCCCCCC		13.9028152594
167UbiquitinationRVLALIVAGLSCVLC
HHHHHHHHHHHHHHC		13.2529967540
170UbiquitinationALIVAGLSCVLCKQP
HHHHHHHHHHHCCCC		10.9729967540
208PhosphorylationYEALKFVSFPTQVLA
HHHHHHCCCCHHHHH		28.74-
211UbiquitinationLKFVSFPTQVLAKAS
HHHCCCCHHHHHHHH		29.3329967540
214UbiquitinationVSFPTQVLAKASKVI
CCCCHHHHHHHHCHH		2.6629967540
216AcetylationFPTQVLAKASKVIPV
CCHHHHHHHHCHHHH		49.3726051181
216UbiquitinationFPTQVLAKASKVIPV
CCHHHHHHHHCHHHH		49.3729967540
218PhosphorylationTQVLAKASKVIPVML
HHHHHHHHCHHHHHH		27.0920068231
219MalonylationQVLAKASKVIPVMLM
HHHHHHHCHHHHHHC		49.3926320211
219UbiquitinationQVLAKASKVIPVMLM
HHHHHHHCHHHHHHC		49.3929967540
283UbiquitinationAGYIAFDSFTSNWQD
HHHHHHHHCCCCHHH		24.7823503661
287UbiquitinationAFDSFTSNWQDALFA
HHHHCCCCHHHHHHH		37.0533845483
288UbiquitinationFDSFTSNWQDALFAY
HHHCCCCHHHHHHHH		9.3733845483
288UbiquitinationFDSFTSNWQDALFAY
HHHCCCCHHHHHHHH		9.37-
294PhosphorylationNWQDALFAYKMSSVQ
CHHHHHHHHHHHHHH		12.1432142685
298UbiquitinationALFAYKMSSVQMMFG
HHHHHHHHHHHHHHC		24.1733845483
298UbiquitinationALFAYKMSSVQMMFG
HHHHHHHHHHHHHHC		24.17-
311UbiquitinationFGVNFFSCLFTVGSL
HCCCHHHHHHHHHHH		2.8323503661
315UbiquitinationFFSCLFTVGSLLEQG
HHHHHHHHHHHHHHC		3.7233845483
316UbiquitinationFSCLFTVGSLLEQGA
HHHHHHHHHHHHHCC		14.9833845483
322PhosphorylationVGSLLEQGALLEGTR
HHHHHHHCCCHHCCC		14.6032142685
323UbiquitinationGSLLEQGALLEGTRF
HHHHHHCCCHHCCCC		14.5223503661
326UbiquitinationLEQGALLEGTRFMGR
HHHCCCHHCCCCCCC		60.4133845483
327UbiquitinationEQGALLEGTRFMGRH
HHCCCHHCCCCCCCC		23.3533845483
328UbiquitinationQGALLEGTRFMGRHS
HCCCHHCCCCCCCCH		16.0333845483
334PhosphorylationGTRFMGRHSEFAAHA
CCCCCCCCHHHHHHH		26.4232142685
338UbiquitinationMGRHSEFAAHALLLS
CCCCHHHHHHHHHHH		8.3533845483
367UbiquitinationGQFGAAVFTIIMTLR
HHHHHHHHHHHHHHH		3.3023503661
371UbiquitinationAAVFTIIMTLRQAFA
HHHHHHHHHHHHHHH		2.2633845483
372UbiquitinationAVFTIIMTLRQAFAI
HHHHHHHHHHHHHHH		14.3733845483
378PhosphorylationMTLRQAFAILLSCLL
HHHHHHHHHHHHHHH		8.4432142685
381 (in isoform 2)Ubiquitination-2.51-
382UbiquitinationQAFAILLSCLLYGHT
HHHHHHHHHHHHCCC		10.1633845483
389PhosphorylationSCLLYGHTVTVVGGL
HHHHHCCCCEEECCH		17.3219369195
391 (in isoform 2)Ubiquitination-15.61-
411UbiquitinationALLLRVYARGRLKQR
HHHHHHHHHHHHHHC		12.4723503661
415UbiquitinationRVYARGRLKQRGKKA
HHHHHHHHHHCCCCC		6.5433845483
416UbiquitinationVYARGRLKQRGKKAV
HHHHHHHHHCCCCCC		36.2733845483
420UbiquitinationGRLKQRGKKAVPVES
HHHHHCCCCCCCCCC		39.4833845483
421UbiquitinationRLKQRGKKAVPVESP
HHHHCCCCCCCCCCC		58.3933845483
422PhosphorylationLKQRGKKAVPVESPV
HHHCCCCCCCCCCCC		17.8432142685
426UbiquitinationGKKAVPVESPVQKV-
CCCCCCCCCCCCCC-		43.1633845483
427PhosphorylationKKAVPVESPVQKV--
CCCCCCCCCCCCC--		30.5229255136
431UbiquitinationPVESPVQKV------
CCCCCCCCC------		50.5833845483
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 S35B2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S35B2_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 S35B2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of S35B2_HUMAN !!
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 S35B2_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-427, AND MASSSPECTROMETRY.
"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-427, 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-427, AND MASSSPECTROMETRY.
"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 SER-427, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND MASSSPECTROMETRY.

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