SP4_HUMAN - dbPTM
SP4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SP4_HUMAN
UniProt AC Q02446
Protein Name Transcription factor Sp4
Gene Name SP4
Organism Homo sapiens (Human).
Sequence Length 784
Subcellular Localization Nucleus.
Protein Description Binds to GT and GC boxes promoters elements. Probable transcriptional activator..
Protein Sequence MSDQKKEEEEEAAAAAAMATEGGKTSEPENNNKKPKTSGSQDSQPSPLALLAATCSKIGTPGENQATGQQQIIIDPSQGLVQLQNQPQQLELVTTQLAGNAWQLVASTPPASKENNVSQPASSSSSSSSSNNGSASPTKTKSGNSSTPGQFQVIQVQNPSGSVQYQVIPQLQTVEGQQIQINPTSSSSLQDLQGQIQLISAGNNQAILTAANRTASGNILAQNLANQTVPVQIRPGVSIPLQLQTLPGTQAQVVTTLPINIGGVTLALPVINNVAAGGGTGQVGQPAATADSGTSNGNQLVSTPTNTTTSASTMPESPSSSTTCTTTASTSLTSSDTLVSSADTGQYASTSASSSERTIEESQTPAATESEAQSSSQLQPNGMQNAQDQSNSLQQVQIVGQPILQQIQIQQPQQQIIQAIPPQSFQLQSGQTIQTIQQQPLQNVQLQAVNPTQVLIRAPTLTPSGQISWQTVQVQNIQSLSNLQVQNAGLSQQLTITPVSSSGGTTLAQIAPVAVAGAPITLNTAQLASVPNLQTVSVANLGAAGVQVQGVPVTITSVAGQQQGQDGVKVQQATIAPVTVAVGGIANATIGAVSPDQLTQVHLQQGQQTSDQEVQPGKRLRRVACSCPNCREGEGRGSNEPGKKKQHICHIEGCGKVYGKTSHLRAHLRWHTGERPFICNWMFCGKRFTRSDELQRHRRTHTGEKRFECPECSKRFMRSDHLSKHVKTHQNKKGGGTALAIVTSGELDSSVTEVLGSPRIVTVAAISQDSNPATPNVSTNMEEF
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------MSDQKKEEE
------CCHHHHHHH		49.0723401153
20PhosphorylationAAAAAMATEGGKTSE
HHHHHHHHCCCCCCC		23.29-
26PhosphorylationATEGGKTSEPENNNK
HHCCCCCCCCCCCCC		55.4228985074
37PhosphorylationNNNKKPKTSGSQDSQ
CCCCCCCCCCCCCCC		47.0130266825
38PhosphorylationNNKKPKTSGSQDSQP
CCCCCCCCCCCCCCC		42.4430266825
40PhosphorylationKKPKTSGSQDSQPSP
CCCCCCCCCCCCCCH		30.4930266825
43PhosphorylationKTSGSQDSQPSPLAL
CCCCCCCCCCCHHHH		36.0330266825
46PhosphorylationGSQDSQPSPLALLAA
CCCCCCCCHHHHHHH		25.5523401153
54PhosphorylationPLALLAATCSKIGTP
HHHHHHHHHHHCCCC		16.2330266825
56PhosphorylationALLAATCSKIGTPGE
HHHHHHHHHCCCCCC		23.9730266825
107PhosphorylationNAWQLVASTPPASKE
CHHHHHHCCCCCCCC		33.6926074081
108PhosphorylationAWQLVASTPPASKEN
HHHHHHCCCCCCCCC		24.4526074081
118PhosphorylationASKENNVSQPASSSS
CCCCCCCCCCCCCCC		32.3523403867
122PhosphorylationNNVSQPASSSSSSSS
CCCCCCCCCCCCCCC		37.1223403867
123PhosphorylationNVSQPASSSSSSSSS
CCCCCCCCCCCCCCC		36.0223403867
124PhosphorylationVSQPASSSSSSSSSN
CCCCCCCCCCCCCCC		31.5723403867
125PhosphorylationSQPASSSSSSSSSNN
CCCCCCCCCCCCCCC		35.8723403867
126PhosphorylationQPASSSSSSSSSNNG
CCCCCCCCCCCCCCC		35.8727794612
127PhosphorylationPASSSSSSSSSNNGS
CCCCCCCCCCCCCCC		35.8727794612
128PhosphorylationASSSSSSSSSNNGSA
CCCCCCCCCCCCCCC		39.4721712546
129PhosphorylationSSSSSSSSSNNGSAS
CCCCCCCCCCCCCCC		38.7521082442
130O-linked_GlycosylationSSSSSSSSNNGSASP
CCCCCCCCCCCCCCC		35.9426431879
130PhosphorylationSSSSSSSSNNGSASP
CCCCCCCCCCCCCCC		35.9421712546
134PhosphorylationSSSSNNGSASPTKTK
CCCCCCCCCCCCCCC		27.9123401153
136PhosphorylationSSNNGSASPTKTKSG
CCCCCCCCCCCCCCC		34.5025463755
138PhosphorylationNNGSASPTKTKSGNS
CCCCCCCCCCCCCCC		49.1825159151
140PhosphorylationGSASPTKTKSGNSST
CCCCCCCCCCCCCCC		32.6830108239
160O-linked_GlycosylationVIQVQNPSGSVQYQV
EEEEECCCCCEEEEE		51.7726431879
173O-linked_GlycosylationQVIPQLQTVEGQQIQ
EEECCEEEECCEEEE		29.1726431879
184O-linked_GlycosylationQQIQINPTSSSSLQD
EEEEECCCCCCHHHH		36.4326431879
186O-linked_GlycosylationIQINPTSSSSLQDLQ
EEECCCCCCHHHHHH		26.8226431879
187O-linked_GlycosylationQINPTSSSSLQDLQG
EECCCCCCHHHHHHH		34.5326431879
188O-linked_GlycosylationINPTSSSSLQDLQGQ
ECCCCCCHHHHHHHE		31.8126431879
209PhosphorylationGNNQAILTAANRTAS
CCCCEEEEEECCCCC		20.0123403867
457MethylationNPTQVLIRAPTLTPS
CCCEEEEECCEECCC		30.2852719415
457DimethylationNPTQVLIRAPTLTPS
CCCEEEEECCEECCC		30.28-
495O-linked_GlycosylationAGLSQQLTITPVSSS
CCCCCCEEEEECCCC		20.6126431879
497O-linked_GlycosylationLSQQLTITPVSSSGG
CCCCEEEEECCCCCC		16.6526431879
500O-linked_GlycosylationQLTITPVSSSGGTTL
CEEEEECCCCCCCCH		21.7126431879
501O-linked_GlycosylationLTITPVSSSGGTTLA
EEEEECCCCCCCCHH		32.9826431879
502O-linked_GlycosylationTITPVSSSGGTTLAQ
EEEECCCCCCCCHHH		33.4626431879
505O-linked_GlycosylationPVSSSGGTTLAQIAP
ECCCCCCCCHHHHCC		23.3526431879
506O-linked_GlycosylationVSSSGGTTLAQIAPV
CCCCCCCCHHHHCCE		24.3026431879
529O-linked_GlycosylationLNTAQLASVPNLQTV
CCHHHHHCCCCCEEE		46.8526431879
535O-linked_GlycosylationASVPNLQTVSVANLG
HCCCCCEEEEEEECC		20.2226431879
537O-linked_GlycosylationVPNLQTVSVANLGAA
CCCCEEEEEEECCCC		20.9226431879
574O-linked_GlycosylationGVKVQQATIAPVTVA
CCEEEEEEEECEEEE		17.2126431879
579O-linked_GlycosylationQATIAPVTVAVGGIA
EEEEECEEEEECCCC		11.1626431879
589O-linked_GlycosylationVGGIANATIGAVSPD
ECCCCCCEECCCCHH		21.5426431879
589PhosphorylationVGGIANATIGAVSPD
ECCCCCCEECCCCHH		21.5428348404
594PhosphorylationNATIGAVSPDQLTQV
CCEECCCCHHHCHHH		23.4028348404
599O-linked_GlycosylationAVSPDQLTQVHLQQG
CCCHHHCHHHHHHCC		23.9426431879
609PhosphorylationHLQQGQQTSDQEVQP
HHHCCCCCCCCCCCC		26.7826074081
610PhosphorylationLQQGQQTSDQEVQPG
HHCCCCCCCCCCCCC		32.7226074081
610O-linked_GlycosylationLQQGQQTSDQEVQPG
HHCCCCCCCCCCCCC		32.7226431879
643SumoylationRGSNEPGKKKQHICH
CCCCCCCCCCEEEEE		68.46-
643SumoylationRGSNEPGKKKQHICH
CCCCCCCCCCEEEEE		68.46-
661PhosphorylationCGKVYGKTSHLRAHL
CCEEECCCHHHHHHH		19.6016332679
662PhosphorylationGKVYGKTSHLRAHLR
CEEECCCHHHHHHHH		24.8216943418
672PhosphorylationRAHLRWHTGERPFIC
HHHHHCCCCCCCEEE		33.50-
689PhosphorylationMFCGKRFTRSDELQR
EEECCCCCCCHHHHH		33.0430108239
691PhosphorylationCGKRFTRSDELQRHR
ECCCCCCCHHHHHHH		32.1725159151
700PhosphorylationELQRHRRTHTGEKRF
HHHHHHHCCCCCCCC		24.60-
702PhosphorylationQRHRRTHTGEKRFEC
HHHHHCCCCCCCCCC		46.56-
719PhosphorylationCSKRFMRSDHLSKHV
HHHHHHHHHHHHHHC		20.0028555341
743PhosphorylationGTALAIVTSGELDSS
CEEEEEEECCCCCCH		25.5427080861
744PhosphorylationTALAIVTSGELDSSV
EEEEEEECCCCCCHH		21.2627080861
749PhosphorylationVTSGELDSSVTEVLG
EECCCCCCHHHHHHC		39.0630301811
750PhosphorylationTSGELDSSVTEVLGS
ECCCCCCHHHHHHCC		32.5030301811
752PhosphorylationGELDSSVTEVLGSPR
CCCCCHHHHHHCCCE		23.4827080861
757PhosphorylationSVTEVLGSPRIVTVA
HHHHHHCCCEEEEEE		13.5720562096
762PhosphorylationLGSPRIVTVAAISQD
HCCCEEEEEEEECCC		11.3230108239
767PhosphorylationIVTVAAISQDSNPAT
EEEEEEECCCCCCCC		24.1730278072
770PhosphorylationVAAISQDSNPATPNV
EEEECCCCCCCCCCC		36.7630278072
774PhosphorylationSQDSNPATPNVSTNM
CCCCCCCCCCCCCCC		19.3622617229
778PhosphorylationNPATPNVSTNMEEF-
CCCCCCCCCCCCCC-		22.2430108239
779PhosphorylationPATPNVSTNMEEF--
CCCCCCCCCCCCC--		34.0130108239
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 SP4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SP4_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 SP4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SP1_HUMANSP1genetic
7559627
SP3_HUMANSP3genetic
7559627
CRX_HUMANCRXphysical
15781457
ADA15_HUMANADAM15physical
25416956
SERF2_HUMANSERF2physical
25416956
LMO3_HUMANLMO3physical
25416956
FOXP2_HUMANFOXP2physical
25416956
CIB3_HUMANCIB3physical
25416956
PR20E_HUMANPRR20Aphysical
25416956
PR20C_HUMANPRR20Aphysical
25416956
PR20D_HUMANPRR20Aphysical
25416956
PR20B_HUMANPRR20Aphysical
25416956
PR20A_HUMANPRR20Aphysical
25416956
AT7L1_HUMANATXN7L1physical
25416956
VRK3_HUMANVRK3physical
28514442
PTPRA_HUMANPTPRAphysical
28514442
HIRA_HUMANHIRAphysical
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 SP4_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-136 AND THR-138, ANDMASS 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-691, AND MASSSPECTROMETRY.

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