SUGP1_HUMAN - dbPTM
SUGP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUGP1_HUMAN
UniProt AC Q8IWZ8
Protein Name SURP and G-patch domain-containing protein 1
Gene Name SUGP1
Organism Homo sapiens (Human).
Sequence Length 645
Subcellular Localization Nucleus .
Protein Description Plays a role in pre-mRNA splicing..
Protein Sequence MSLKMDNRDVAGKANRWFGVAPPKSGKMNMNILHQEELIAQKKREIEAKMEQKAKQNQVASPQPPHPGEITNAHNSSCISNKFANDGSFLQQFLKLQKAQTSTDAPTSAPSAPPSTPTPSAGKRSLLISRRTGLGLASLPGPVKSYSHAKQLPVAHRPSVFQSPDEDEEEDYEQWLEIKVSPPEGAETRKVIEKLARFVAEGGPELEKVAMEDYKDNPAFAFLHDKNSREFLYYRKKVAEIRKEAQKSQAASQKVSPPEDEEVKNLAEKLARFIADGGPEVETIALQNNRENQAFSFLYEPNSQGYKYYRQKLEEFRKAKASSTGSFTAPDPGLKRKSPPEALSGSLPPATTCPASSTPAPTIIPAPAAPGKPASAATVKRKRKSRWGPEEDKVELPPAELVQRDVDASPSPLSVQDLKGLGYEKGKPVGLVGVTELSDAQKKQLKEQQEMQQMYDMIMQHKRAMQDMQLLWEKAVQQHQHGYDSDEEVDSELGTWEHQLRRMEMDKTREWAEQLTKMGRGKHFIGDFLPPDELEKFMETFKALKEGREPDYSEYKEFKLTVENIGYQMLMKMGWKEGEGLGSEGQGIKNPVNKGTTTVDGAGFGIDRPAELSKEDDEYEAFRKRMMLAYRFRPNPLNNPRRPYY
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
27AcetylationVAPPKSGKMNMNILH
CCCCCCCCCCCCCCC		33.9025953088
61PhosphorylationAKQNQVASPQPPHPG
HHHCCCCCCCCCCCC		25.8029978859
71PhosphorylationPPHPGEITNAHNSSC
CCCCCCCCCCCCCCC		23.2729978859
76PhosphorylationEITNAHNSSCISNKF
CCCCCCCCCCCCCCC		19.4026074081
77PhosphorylationITNAHNSSCISNKFA
CCCCCCCCCCCCCCC		22.3126074081
80PhosphorylationAHNSSCISNKFANDG
CCCCCCCCCCCCCCC		37.9926074081
88PhosphorylationNKFANDGSFLQQFLK
CCCCCCCHHHHHHHH		26.1621712546
95AcetylationSFLQQFLKLQKAQTS
HHHHHHHHHHHCCCC		50.6026051181
103PhosphorylationLQKAQTSTDAPTSAP
HHHCCCCCCCCCCCC		39.3025332170
107O-linked_GlycosylationQTSTDAPTSAPSAPP
CCCCCCCCCCCCCCC		38.9623301498
108O-linked_GlycosylationTSTDAPTSAPSAPPS
CCCCCCCCCCCCCCC		36.8023301498
111O-linked_GlycosylationDAPTSAPSAPPSTPT
CCCCCCCCCCCCCCC		53.8023301498
111PhosphorylationDAPTSAPSAPPSTPT
CCCCCCCCCCCCCCC		53.8026074081
115PhosphorylationSAPSAPPSTPTPSAG
CCCCCCCCCCCCCCC		46.0622199227
116O-linked_GlycosylationAPSAPPSTPTPSAGK
CCCCCCCCCCCCCCC		36.6323301498
116PhosphorylationAPSAPPSTPTPSAGK
CCCCCCCCCCCCCCC		36.6321815630
118 (in isoform 2)Phosphorylation-29.93-
118PhosphorylationSAPPSTPTPSAGKRS
CCCCCCCCCCCCCCE		29.9322199227
120PhosphorylationPPSTPTPSAGKRSLL
CCCCCCCCCCCCEEE		52.7326074081
123AcetylationTPTPSAGKRSLLISR
CCCCCCCCCEEEEEC		38.2325953088
123MethylationTPTPSAGKRSLLISR
CCCCCCCCCEEEEEC		38.2312431643
125O-linked_GlycosylationTPSAGKRSLLISRRT
CCCCCCCEEEEECCC		30.8923301498
132PhosphorylationSLLISRRTGLGLASL
EEEEECCCCCCCCCC		35.3326074081
138PhosphorylationRTGLGLASLPGPVKS
CCCCCCCCCCCCCCC		39.8922210691
144AcetylationASLPGPVKSYSHAKQ
CCCCCCCCCCCCCCC		46.9725953088
145PhosphorylationSLPGPVKSYSHAKQL
CCCCCCCCCCCCCCC		31.91-
146PhosphorylationLPGPVKSYSHAKQLP
CCCCCCCCCCCCCCC		9.9622817900
159PhosphorylationLPVAHRPSVFQSPDE
CCCCCCCCCCCCCCC		35.2029523821
163PhosphorylationHRPSVFQSPDEDEEE
CCCCCCCCCCCCCCC		23.8929523821
172PhosphorylationDEDEEEDYEQWLEIK
CCCCCCCHHHHHEEE		17.1928796482
181PhosphorylationQWLEIKVSPPEGAET
HHHEEEECCCCCHHH		29.7221815630
228PhosphorylationAFLHDKNSREFLYYR
EEECCCCHHHHHHHH		38.64-
256PhosphorylationQAASQKVSPPEDEEV
HHHHCCCCCCCHHHH		41.6021815630
264AcetylationPPEDEEVKNLAEKLA
CCCHHHHHHHHHHHH		49.9126051181
323PhosphorylationFRKAKASSTGSFTAP
HHHHHHCCCCCCCCC		41.4630624053
324PhosphorylationRKAKASSTGSFTAPD
HHHHHCCCCCCCCCC		34.0630624053
326PhosphorylationAKASSTGSFTAPDPG
HHHCCCCCCCCCCCC		21.3625159151
328PhosphorylationASSTGSFTAPDPGLK
HCCCCCCCCCCCCCC		38.6923186163
335MethylationTAPDPGLKRKSPPEA
CCCCCCCCCCCCHHH		64.79115981385
338PhosphorylationDPGLKRKSPPEALSG
CCCCCCCCCHHHHCC		50.1230576142
344PhosphorylationKSPPEALSGSLPPAT
CCCHHHHCCCCCCCC		33.1225159151
346PhosphorylationPPEALSGSLPPATTC
CHHHHCCCCCCCCCC		34.0425159151
351PhosphorylationSGSLPPATTCPASST
CCCCCCCCCCCCCCC		34.4030576142
352PhosphorylationGSLPPATTCPASSTP
CCCCCCCCCCCCCCC		20.7130576142
356PhosphorylationPATTCPASSTPAPTI
CCCCCCCCCCCCCEE		21.6423312004
357PhosphorylationATTCPASSTPAPTII
CCCCCCCCCCCCEEE		40.2823312004
358PhosphorylationTTCPASSTPAPTIIP
CCCCCCCCCCCEEEE		22.4523312004
362PhosphorylationASSTPAPTIIPAPAA
CCCCCCCEEEECCCC		33.3823312004
375PhosphorylationAAPGKPASAATVKRK
CCCCCCCCCHHHHCH		27.2823312004
378PhosphorylationGKPASAATVKRKRKS
CCCCCCHHHHCHHHH		26.6923312004
409PhosphorylationVQRDVDASPSPLSVQ
HCCCCCCCCCCCCHH		22.8029255136
411PhosphorylationRDVDASPSPLSVQDL
CCCCCCCCCCCHHHH		35.6629255136
414PhosphorylationDASPSPLSVQDLKGL
CCCCCCCCHHHHCCC		22.5530266825
419UbiquitinationPLSVQDLKGLGYEKG
CCCHHHHCCCCCCCC		61.45-
427SumoylationGLGYEKGKPVGLVGV
CCCCCCCCEEEEEEC		47.82-
427UbiquitinationGLGYEKGKPVGLVGV
CCCCCCCCEEEEEEC		47.82-
427SumoylationGLGYEKGKPVGLVGV
CCCCCCCCEEEEEEC		47.82-
455PhosphorylationQQEMQQMYDMIMQHK
HHHHHHHHHHHHHHH		9.6826552605
483PhosphorylationVQQHQHGYDSDEEVD
HHHHHCCCCCHHHHH		15.3422167270
485PhosphorylationQHQHGYDSDEEVDSE
HHHCCCCCHHHHHHH		38.1422167270
491PhosphorylationDSDEEVDSELGTWEH
CCHHHHHHHHCHHHH		39.6423927012
495PhosphorylationEVDSELGTWEHQLRR
HHHHHHCHHHHHHHH		40.0623927012
508PhosphorylationRRMEMDKTREWAEQL
HHHHHHHHHHHHHHH		29.5623403867
516PhosphorylationREWAEQLTKMGRGKH
HHHHHHHHHCCCCCC		20.76-
522UbiquitinationLTKMGRGKHFIGDFL
HHHCCCCCCCCCCCC		33.70-
542MethylationEKFMETFKALKEGRE
HHHHHHHHHHHCCCC		61.30-
542UbiquitinationEKFMETFKALKEGRE
HHHHHHHHHHHCCCC		61.30-
561PhosphorylationEYKEFKLTVENIGYQ
HHHHHEEEHHHHHHH		26.77-
589UbiquitinationGSEGQGIKNPVNKGT
CCCCCCCCCCCCCCC		63.12-
594UbiquitinationGIKNPVNKGTTTVDG
CCCCCCCCCCCCCCC		58.84-
614UbiquitinationDRPAELSKEDDEYEA
CCCHHHCCCCHHHHH		77.21-
619PhosphorylationLSKEDDEYEAFRKRM
HCCCCHHHHHHHHHH		21.3927642862
641MethylationPNPLNNPRRPYY---
CCCCCCCCCCCC---		55.0954559195
642MethylationNPLNNPRRPYY----
CCCCCCCCCCC----		25.4854559203
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 SUGP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SUGP1_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 SUGP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THIK_HUMANACAA1physical
22939629
VDAC3_HUMANVDAC3physical
22939629
RIDA_HUMANHRSP12physical
22939629
SOSB1_HUMANNABP2physical
22939629
STX7_HUMANSTX7physical
22939629
TBL2_HUMANTBL2physical
22939629
SPRE_HUMANSPRphysical
22939629
THY1_HUMANTHY1physical
22939629
SRPRB_HUMANSRPRBphysical
22939629
TIM44_HUMANTIMM44physical
22939629
SLIRP_HUMANSLIRPphysical
22939629
UBL4A_HUMANUBL4Aphysical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
STOM_HUMANSTOMphysical
22939629
VDAC2_HUMANVDAC2physical
22939629
TAGL_HUMANTAGLNphysical
22939629
SNX3_HUMANSNX3physical
22939629
UBC9_HUMANUBE2Iphysical
22939629
VDAC1_HUMANVDAC1physical
22939629
MPLKI_HUMANMPLKIPphysical
22939629
UB2L3_HUMANUBE2L3physical
22939629
VATE1_HUMANATP6V1E1physical
22939629
ZO1_HUMANTJP1physical
22939629
RU2B_HUMANSNRPB2physical
22365833
DHX15_HUMANDHX15physical
22365833
SPF45_HUMANRBM17physical
22365833
U2AF2_HUMANU2AF2physical
22365833
RBM10_HUMANRBM10physical
22365833
U2AF2_HUMANU2AF2physical
21988832
DHX15_HUMANDHX15physical
26344197
PYRG2_HUMANCTPS2physical
28514442
CTR9_HUMANCTR9physical
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 SUGP1_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-409; SER-411 ANDSER-414, AND MASS SPECTROMETRY.
"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-485, 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-409 AND SER-485, ANDMASS SPECTROMETRY.

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