SHKB1_HUMAN - dbPTM
SHKB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHKB1_HUMAN
UniProt AC Q8TBC3
Protein Name SH3KBP1-binding protein 1
Gene Name SHKBP1
Organism Homo sapiens (Human).
Sequence Length 707
Subcellular Localization Lysosome .
Protein Description Inhibits CBL-SH3KBP1 complex mediated down-regulation of EGFR signaling by sequestration of SH3KBP1. Binds to SH3KBP1 and prevents its interaction with CBL and inhibits translocation of SH3KBP1 to EGFR containing vesicles upon EGF stimulation..
Protein Sequence MAAAATAAEGVPSRGPPGEVIHLNVGGKRFSTSRQTLTWIPDSFFSSLLSGRISTLKDETGAIFIDRDPTVFAPILNFLRTKELDPRGVHGSSLLHEAQFYGLTPLVRRLQLREELDRSSCGNVLFNGYLPPPVFPVKRRNRHSLVGPQQLGGRPAPVRRSNTMPPNLGNAGLLGRMLDEKTPPSPSGQPEEPGMVRLVCGHHNWIAVAYTQFLVCYRLKEASGWQLVFSSPRLDWPIERLALTARVHGGALGEHDKMVAAATGSEILLWALQAEGGGSEIGVFHLGVPVEALFFVGNQLIATSHTGRIGVWNAVTKHWQVQEVQPITSYDAAGSFLLLGCNNGSIYYVDVQKFPLRMKDNDLLVSELYRDPAEDGVTALSVYLTPKTSDSGNWIEIAYGTSSGGVRVIVQHPETVGSGPQLFQTFTVHRSPVTKIMLSEKHLISVCADNNHVRTWSVTRFRGMISTQPGSTPLASFKILALESADGHGGCSAGNDIGPYGERDDQQVFIQKVVPSASQLFVRLSSTGQRVCSVRSVDGSPTTAFTVLECEGSRRLGSRPRRYLLTGQANGSLAMWDLTTAMDGLGQAPAGGLTEQELMEQLEHCELAPPAPSAPSWGCLPSPSPRISLTSLHSASSNTSLSGHRGSPSPPQAEARRRGGGSFVERCQELVRSGPDLRRPPTPAPWPSSGLGTPLTPPKMKLNETSF
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
2Acetylation------MAAAATAAE
------CCCCHHHCC		13.0522814378
28UbiquitinationIHLNVGGKRFSTSRQ
EEEEECCEEEECCCC		44.32-
28 (in isoform 2)Ubiquitination-44.32-
36PhosphorylationRFSTSRQTLTWIPDS
EEECCCCEEEECCHH		25.6625072903
38PhosphorylationSTSRQTLTWIPDSFF
ECCCCEEEECCHHHH		25.4125072903
47PhosphorylationIPDSFFSSLLSGRIS
CCHHHHHHHHHCCCC		28.3328355574
82UbiquitinationILNFLRTKELDPRGV
HHHHHHCCCCCCCCC		50.25-
138UbiquitinationPPPVFPVKRRNRHSL
CCCCCCCCCCCCCCC		45.97-
144PhosphorylationVKRRNRHSLVGPQQL
CCCCCCCCCCCHHHH		22.8523401153
161PhosphorylationRPAPVRRSNTMPPNL
CCCCCCCCCCCCCCC		26.5323403867
163PhosphorylationAPVRRSNTMPPNLGN
CCCCCCCCCCCCCCC		32.0928348404
181 (in isoform 1)Ubiquitination-67.0321890473
181 (in isoform 2)Ubiquitination-67.0321906983
181UbiquitinationLGRMLDEKTPPSPSG
HHHHHCCCCCCCCCC		67.0321906983
182PhosphorylationGRMLDEKTPPSPSGQ
HHHHCCCCCCCCCCC		38.0827251275
185PhosphorylationLDEKTPPSPSGQPEE
HCCCCCCCCCCCCCC		32.6628985074
187PhosphorylationEKTPPSPSGQPEEPG
CCCCCCCCCCCCCCC		55.1627251275
195SulfoxidationGQPEEPGMVRLVCGH
CCCCCCCCEEEEECC		2.0121406390
359UbiquitinationQKFPLRMKDNDLLVS
CCCCCCCCCCCEEEE		47.12-
381PhosphorylationEDGVTALSVYLTPKT
CCCCEEEEEEECCCC		13.2730576142
389PhosphorylationVYLTPKTSDSGNWIE
EEECCCCCCCCCEEE		35.5930576142
402PhosphorylationIEIAYGTSSGGVRVI
EEEEEECCCCCEEEE		23.7130576142
435 (in isoform 1)Ubiquitination-26.7621890473
435UbiquitinationVHRSPVTKIMLSEKH
EECCCCCEEEECCCE		26.7621890473
467PhosphorylationRFRGMISTQPGSTPL
EEECCEECCCCCCCC		28.0527282143
471PhosphorylationMISTQPGSTPLASFK
CEECCCCCCCCEEEE		33.2723186163
472PhosphorylationISTQPGSTPLASFKI
EECCCCCCCCEEEEE		28.3923917254
476PhosphorylationPGSTPLASFKILALE
CCCCCCEEEEEEEEE		34.4524719451
512 (in isoform 1)Ubiquitination-40.1421890473
512UbiquitinationDQQVFIQKVVPSASQ
CCEEEEEECCCCHHH		40.1421890473
624PhosphorylationWGCLPSPSPRISLTS
CCCCCCCCCCEEEEE		31.0220363803
628PhosphorylationPSPSPRISLTSLHSA
CCCCCCEEEEEEEEC		27.2023403867
630PhosphorylationPSPRISLTSLHSASS
CCCCEEEEEEEECCC		23.5823403867
631PhosphorylationSPRISLTSLHSASSN
CCCEEEEEEEECCCC		29.4023403867
634PhosphorylationISLTSLHSASSNTSL
EEEEEEEECCCCCCC		34.8323403867
636PhosphorylationLTSLHSASSNTSLSG
EEEEEECCCCCCCCC		27.4326657352
637PhosphorylationTSLHSASSNTSLSGH
EEEEECCCCCCCCCC		43.7923927012
639PhosphorylationLHSASSNTSLSGHRG
EEECCCCCCCCCCCC		32.7526657352
640PhosphorylationHSASSNTSLSGHRGS
EECCCCCCCCCCCCC		25.4523927012
642PhosphorylationASSNTSLSGHRGSPS
CCCCCCCCCCCCCCC		32.1123403867
647PhosphorylationSLSGHRGSPSPPQAE
CCCCCCCCCCCCHHH		23.3530266825
649PhosphorylationSGHRGSPSPPQAEAR
CCCCCCCCCCHHHHH		51.4130266825
658MethylationPQAEARRRGGGSFVE
CHHHHHHHCCCCHHH		42.42115916925
662PhosphorylationARRRGGGSFVERCQE
HHHHCCCCHHHHHHH		29.4123401153
673PhosphorylationRCQELVRSGPDLRRP
HHHHHHHHCCCCCCC		47.3924719451
679MethylationRSGPDLRRPPTPAPW
HHCCCCCCCCCCCCC		49.17115387777
682PhosphorylationPDLRRPPTPAPWPSS
CCCCCCCCCCCCCCC		34.4628450419
688PhosphorylationPTPAPWPSSGLGTPL
CCCCCCCCCCCCCCC		32.9230108239
689PhosphorylationTPAPWPSSGLGTPLT
CCCCCCCCCCCCCCC		33.6830108239
693PhosphorylationWPSSGLGTPLTPPKM
CCCCCCCCCCCCCCC		21.8423898821
696PhosphorylationSGLGTPLTPPKMKLN
CCCCCCCCCCCCCCC		38.4527273156
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 SHKB1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHKB1_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 SHKB1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SH3K1_HUMANSH3KBP1physical
21830225
ASPC1_HUMANASPSCR1physical
28514442
FEM1B_HUMANFEM1Bphysical
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 SHKB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-647 AND SER-649, ANDMASS SPECTROMETRY.

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