SP2_HUMAN - dbPTM
SP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SP2_HUMAN
UniProt AC Q02086
Protein Name Transcription factor Sp2
Gene Name SP2
Organism Homo sapiens (Human).
Sequence Length 613
Subcellular Localization Nucleus.
Protein Description Binds to GC box promoters elements and selectively activates mRNA synthesis from genes that contain functional recognition sites..
Protein Sequence MSDPQTSMAATAAVSPSDYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPGKNSFGILSSKGNILQIQGSQLSASYPGGQLVFAIQNPTMINKGTRSNANIQYQAVPQIQASNSQTIQVQPNLTNQIQIIPGTNQAIITPSPSSHKPVPIKPAPIQKSSTTTTPVQSGANVVKLTGGGGNVTLTLPVNNLVNASDTGAPTQLLTESPPTPLSKTNKKARKKSLPASQPPVAVAEQVETVLIETTADNIIQAGNNLLIVQSPGGGQPAVVQQVQVVPPKAEQQQVVQIPQQALRVVQAASATLPTVPQKPSQNFQIQAAEPTPTQVYIRTPSGEVQTVLVQDSPPATAAATSNTTCSSPASRAPHLSGTSKKHSAAILRKERPLPKIAPAGSIISLNAAQLAAAAQAMQTININGVQVQGVPVTITNTGGQQQLTVQNVSGNNLTISGLSPTQIQLQMEQALAGETQPGEKRRRMACTCPNCKDGEKRSGEQGKKKHVCHIPDCGKTFRKTSLLRAHVRLHTGERPFVCNWFFCGKRFTRSDELQRHARTHTGDKRFECAQCQKRFMRSDHLTKHYKTHLVTKNL
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
8 (in isoform 2)Phosphorylation-3.1429116813
10 (in isoform 2)Phosphorylation-6.8029116813
11PhosphorylationPQTSMAATAAVSPSD
HHHHHHHCCCCCHHH		12.9527251275
15PhosphorylationMAATAAVSPSDYLQP
HHHCCCCCHHHHCCC		17.6026552605
17PhosphorylationATAAVSPSDYLQPAA
HCCCCCHHHHCCCCC		31.2326552605
19PhosphorylationAAVSPSDYLQPAAST
CCCCHHHHCCCCCCC		16.1526552605
25PhosphorylationDYLQPAASTTQDSQP
HHCCCCCCCCCCCCC		33.8127251275
26PhosphorylationYLQPAASTTQDSQPS
HCCCCCCCCCCCCCC		24.6127251275
27PhosphorylationLQPAASTTQDSQPSP
CCCCCCCCCCCCCCH		28.0826552605
30PhosphorylationAASTTQDSQPSPLAL
CCCCCCCCCCCHHHH		33.8926552605
33PhosphorylationTTQDSQPSPLALLAA
CCCCCCCCHHHHHHH		25.5532142685
41PhosphorylationPLALLAATCSKIGPP
HHHHHHHHHHHHCCC		16.2326552605
43PhosphorylationALLAATCSKIGPPAV
HHHHHHHHHHCCCCE		23.9726552605
55PhosphorylationPAVEAAVTPPAPPQP
CCEEECCCCCCCCCC		20.8729255136
63PhosphorylationPPAPPQPTPRKLVPI
CCCCCCCCCCCCEEC		30.4029255136
78PhosphorylationKPAPLPLSPGKNSFG
CCCCCCCCCCCCCEE		29.6629255136
83PhosphorylationPLSPGKNSFGILSSK
CCCCCCCCEEEECCC		28.4729978859
88PhosphorylationKNSFGILSSKGNILQ
CCCEEEECCCCCEEE		28.2523312004
89PhosphorylationNSFGILSSKGNILQI
CCEEEECCCCCEEEE		40.9323312004
102PhosphorylationQIQGSQLSASYPGGQ
EEECCEEEEECCCCE		13.9227251275
104PhosphorylationQGSQLSASYPGGQLV
ECCEEEEECCCCEEE		28.6027251275
187PhosphorylationKPAPIQKSSTTTTPV
CCCCCCCCCCCCCCC		19.2825159151
187O-linked_GlycosylationKPAPIQKSSTTTTPV
CCCCCCCCCCCCCCC		19.2830059200
188PhosphorylationPAPIQKSSTTTTPVQ
CCCCCCCCCCCCCCC		36.4925159151
188O-linked_GlycosylationPAPIQKSSTTTTPVQ
CCCCCCCCCCCCCCC		36.4930059200
189PhosphorylationAPIQKSSTTTTPVQS
CCCCCCCCCCCCCCC		34.9425159151
190PhosphorylationPIQKSSTTTTPVQSG
CCCCCCCCCCCCCCC		30.5327732954
191PhosphorylationIQKSSTTTTPVQSGA
CCCCCCCCCCCCCCC		29.2325159151
192PhosphorylationQKSSTTTTPVQSGAN
CCCCCCCCCCCCCCE		21.2625159151
196PhosphorylationTTTTPVQSGANVVKL
CCCCCCCCCCEEEEE		39.8629396449
196O-linked_GlycosylationTTTTPVQSGANVVKL
CCCCCCCCCCEEEEE		39.8630059200
223PhosphorylationVNNLVNASDTGAPTQ
CCCEECCCCCCCCCH		30.4228348404
225PhosphorylationNLVNASDTGAPTQLL
CEECCCCCCCCCHHH		32.5228348404
229PhosphorylationASDTGAPTQLLTESP
CCCCCCCCHHHCCCC		31.1728122231
233PhosphorylationGAPTQLLTESPPTPL
CCCCHHHCCCCCCCC		42.9028122231
235PhosphorylationPTQLLTESPPTPLSK
CCHHHCCCCCCCCCC		30.8322199227
238PhosphorylationLLTESPPTPLSKTNK
HHCCCCCCCCCCCCH		40.0022199227
241PhosphorylationESPPTPLSKTNKKAR
CCCCCCCCCCCHHHH		38.3422199227
358PhosphorylationPTQVYIRTPSGEVQT
CCEEEEECCCCCEEE		16.5527251275
360PhosphorylationQVYIRTPSGEVQTVL
EEEEECCCCCEEEEE		47.1527251275
365PhosphorylationTPSGEVQTVLVQDSP
CCCCCEEEEEEECCC		22.4527251275
371PhosphorylationQTVLVQDSPPATAAA
EEEEEECCCCCCEEC		18.7228464451
375PhosphorylationVQDSPPATAAATSNT
EECCCCCCEECCCCC		23.7027251275
379PhosphorylationPPATAAATSNTTCSS
CCCCEECCCCCCCCC		20.1327251275
380PhosphorylationPATAAATSNTTCSSP
CCCEECCCCCCCCCC		27.7027251275
382PhosphorylationTAAATSNTTCSSPAS
CEECCCCCCCCCCCC		29.0127251275
383PhosphorylationAAATSNTTCSSPASR
EECCCCCCCCCCCCC		18.0327251275
385PhosphorylationATSNTTCSSPASRAP
CCCCCCCCCCCCCCC		36.9527251275
386PhosphorylationTSNTTCSSPASRAPH
CCCCCCCCCCCCCCC		26.9930576142
389PhosphorylationTTCSSPASRAPHLSG
CCCCCCCCCCCCCCC		32.1527251275
395PhosphorylationASRAPHLSGTSKKHS
CCCCCCCCCCCCCHH		36.6726657352
397PhosphorylationRAPHLSGTSKKHSAA
CCCCCCCCCCCHHHH		33.7225262027
398PhosphorylationAPHLSGTSKKHSAAI
CCCCCCCCCCHHHHH		43.1425262027
400UbiquitinationHLSGTSKKHSAAILR
CCCCCCCCHHHHHHH		42.4329967540
535PhosphorylationHIPDCGKTFRKTSLL
ECCCCCCCHHHHHHH		17.60-
540PhosphorylationGKTFRKTSLLRAHVR
CCCHHHHHHHHHEEE		28.5724719451
550PhosphorylationRAHVRLHTGERPFVC
HHEEEECCCCCCEEE		45.3818669648
567PhosphorylationFFCGKRFTRSDELQR
EEECCCCCCCHHHHH		33.0430108239
569PhosphorylationCGKRFTRSDELQRHA
ECCCCCCCHHHHHHH		32.1729496963
578PhosphorylationELQRHARTHTGDKRF
HHHHHHHHCCCCCHH		25.2728450419
605UbiquitinationDHLTKHYKTHLVTKN
HHHHHHHHHHEEECC		29.2329967540
610PhosphorylationHYKTHLVTKNL----
HHHHHEEECCC----		22.1524719451
611UbiquitinationYKTHLVTKNL-----
HHHHEEECCC-----		49.09-
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 SP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SP2_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 SP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NR0B2_HUMANNR0B2physical
17071613
NKX31_MOUSENkx3-1physical
16201967
IRF1_HUMANIRF1physical
19482358
A4_HUMANAPPphysical
21832049
BANP_HUMANBANPphysical
25416956
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 SP2_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 THR-192, 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 THR-550, AND MASSSPECTROMETRY.

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