SH319_HUMAN - dbPTM
SH319_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH319_HUMAN
UniProt AC Q5HYK7
Protein Name SH3 domain-containing protein 19
Gene Name SH3D19
Organism Homo sapiens (Human).
Sequence Length 790
Subcellular Localization Cytoplasm . Nucleus . Is recruited to the nucleus by the KMT2A/MLL1-EEN fusion protein.
Protein Description May play a role in regulating A disintegrin and metalloproteases (ADAMs) in the signaling of EGFR-ligand shedding. May be involved in suppression of Ras-induced cellular transformation and Ras-mediated activation of ELK1. Plays a role in the regulation of cell morphology and cytoskeletal organization..
Protein Sequence MNIMNTEQSQNSIVSRIKVFEGQTNIETSGLPKKPEITPRSLPPKPTVSSGKPSVAPKPAANRASGEWDSGTENRLKVTSKEGLTPYPPLQEAGSIPVTKPELPKKPNPGLIRSVNPEIPGRGPLAESSDSGKKVPTPAPRPLLLKKSVSSENPTYPSAPLKPVTVPPRLAGASQAKAYKSLGEGPPANPPVPVLQSKPLVDIDLISFDDDVLPTPSGNLAEESVGSEMVLDPFQLPAKTEPIKERAVQPAPTRKPTVIRIPAKPGKCLHEDPQSPPPLPAEKPIGNTFSTVSGKLSNVERTRNLESNHPGQTGGFVRVPPRLPPRPVNGKTIPTQQPPTKVPPERPPPPKLSATRRSNKKLPFNRSSSDMDLQKKQSNLATGLSKAKSQVFKNQDPVLPPRPKPGHPLYSKYMLSVPHGIANEDIVSQNPGELSCKRGDVLVMLKQTENNYLECQKGEDTGRVHLSQMKIITPLDEHLRSRPNDPSHAQKPVDSGAPHAVVLHDFPAEQVDDLNLTSGEIVYLLEKIDTDWYRGNCRNQIGIFPANYVKVIIDIPEGGNGKRECVSSHCVKGSRCVARFEYIGEQKDELSFSEGEIIILKEYVNEEWARGEVRGRTGIFPLNFVEPVEDYPTSGANVLSTKVPLKTKKEDSGSNSQVNSLPAEWCEALHSFTAETSDDLSFKRGDRIQILERLDSDWCRGRLQDREGIFPAVFVRPCPAEAKSMLAIVPKGRKAKALYDFRGENEDELSFKAGDIITELESVDDDWMSGELMGKSGIFPKNYIQFLQIS
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
6Phosphorylation--MNIMNTEQSQNSI
--CCCCCHHHHHCHH		20.30-
9PhosphorylationNIMNTEQSQNSIVSR
CCCCHHHHHCHHHHE		25.71-
18UbiquitinationNSIVSRIKVFEGQTN
CHHHHEEEEEECCCC		39.50-
34UbiquitinationETSGLPKKPEITPRS
CCCCCCCCCCCCCCC		46.04-
45UbiquitinationTPRSLPPKPTVSSGK
CCCCCCCCCCCCCCC		51.92-
52UbiquitinationKPTVSSGKPSVAPKP
CCCCCCCCCCCCCCC		35.75-
65PhosphorylationKPAANRASGEWDSGT
CCCCCCCCCCCCCCC		33.7325159151
70PhosphorylationRASGEWDSGTENRLK
CCCCCCCCCCCCEEE		49.0028102081
72PhosphorylationSGEWDSGTENRLKVT
CCCCCCCCCCEEEEE		33.7628102081
81UbiquitinationNRLKVTSKEGLTPYP
CEEEEECCCCCCCCC		46.57-
100UbiquitinationAGSIPVTKPELPKKP
CCCCCCCCCCCCCCC		36.41-
106UbiquitinationTKPELPKKPNPGLIR
CCCCCCCCCCCCCCC		48.35-
131PhosphorylationPLAESSDSGKKVPTP
CCCCCCCCCCCCCCC		55.2328555341
137PhosphorylationDSGKKVPTPAPRPLL
CCCCCCCCCCCCCEE		34.7623312004
146MethylationAPRPLLLKKSVSSEN
CCCCEEEECCCCCCC		42.86115981297
147MethylationPRPLLLKKSVSSENP
CCCEEEECCCCCCCC		56.94115981305
148PhosphorylationRPLLLKKSVSSENPT
CCEEEECCCCCCCCC		26.1626657352
150PhosphorylationLLLKKSVSSENPTYP
EEEECCCCCCCCCCC		38.7425159151
151PhosphorylationLLKKSVSSENPTYPS
EEECCCCCCCCCCCC		38.9626657352
155PhosphorylationSVSSENPTYPSAPLK
CCCCCCCCCCCCCCC		60.7028450419
156PhosphorylationVSSENPTYPSAPLKP
CCCCCCCCCCCCCCC		9.1026657352
158PhosphorylationSENPTYPSAPLKPVT
CCCCCCCCCCCCCCC		31.9129978859
162UbiquitinationTYPSAPLKPVTVPPR
CCCCCCCCCCCCCHH		36.06-
165PhosphorylationSAPLKPVTVPPRLAG
CCCCCCCCCCHHHCC		35.5023312004
177UbiquitinationLAGASQAKAYKSLGE
HCCHHHHHHHHHHCC		44.61-
180MethylationASQAKAYKSLGEGPP
HHHHHHHHHHCCCCC		44.03115981313
180UbiquitinationASQAKAYKSLGEGPP
HHHHHHHHHHCCCCC		44.03-
181PhosphorylationSQAKAYKSLGEGPPA
HHHHHHHHHCCCCCC		29.0027251275
197PhosphorylationPPVPVLQSKPLVDID
CCCCCCCCCCCEEEE		31.8924719451
240PhosphorylationPFQLPAKTEPIKERA
CCCCCCCCCCCHHCC		49.45-
253PhosphorylationRAVQPAPTRKPTVIR
CCCCCCCCCCCEEEE		54.13-
257PhosphorylationPAPTRKPTVIRIPAK
CCCCCCCEEEEEECC		31.44-
275PhosphorylationCLHEDPQSPPPLPAE
CCCCCCCCCCCCCCC		44.7725159151
358PhosphorylationKLSATRRSNKKLPFN
CCCCCCCCCCCCCCC		50.1124501219
367PhosphorylationKKLPFNRSSSDMDLQ
CCCCCCCCCCHHHHH		34.9923403867
368PhosphorylationKLPFNRSSSDMDLQK
CCCCCCCCCHHHHHH		27.4127794612
369PhosphorylationLPFNRSSSDMDLQKK
CCCCCCCCHHHHHHH		37.9025159151
378PhosphorylationMDLQKKQSNLATGLS
HHHHHHHHHHHHHHH		42.5727251275
385PhosphorylationSNLATGLSKAKSQVF
HHHHHHHHHHHHHHH		31.7322617229
386UbiquitinationNLATGLSKAKSQVFK
HHHHHHHHHHHHHHC		65.95-
389PhosphorylationTGLSKAKSQVFKNQD
HHHHHHHHHHHCCCC		36.1126657352
410PhosphorylationPKPGHPLYSKYMLSV
CCCCCCCCCHHEECC		13.9427642862
411PhosphorylationKPGHPLYSKYMLSVP
CCCCCCCCHHEECCC		25.6227642862
413PhosphorylationGHPLYSKYMLSVPHG
CCCCCCHHEECCCCC		9.4327642862
416PhosphorylationLYSKYMLSVPHGIAN
CCCHHEECCCCCCCC		19.6427642862
435PhosphorylationSQNPGELSCKRGDVL
CCCCCCCCCCCCCEE		17.1927642862
449PhosphorylationLVMLKQTENNYLECQ
EEEEEECCCCEEEEE		40.7717389395
452PhosphorylationLKQTENNYLECQKGE
EEECCCCEEEEECCC		18.5625159151
457UbiquitinationNNYLECQKGEDTGRV
CCEEEEECCCCCCCE		75.76-
481PhosphorylationPLDEHLRSRPNDPSH
CHHHHHHCCCCCHHH		59.4520068231
548PhosphorylationIGIFPANYVKVIIDI
CCEEECCEEEEEEEC		12.0727642862
619 (in isoform 2)Ubiquitination-2.96-
642UbiquitinationGANVLSTKVPLKTKK
CCCCEEECCCCCCCC		38.18-
681PhosphorylationAETSDDLSFKRGDRI
ECCCCCCCCCCCCEE		35.4024719451
696PhosphorylationQILERLDSDWCRGRL
HHHHHCCCCCCCCCC		37.2927251275
731UbiquitinationSMLAIVPKGRKAKAL
HHEEEEECCCCCEEE		61.53-
750PhosphorylationGENEDELSFKAGDII
CCCCCCCCEECCCEE		23.7424719451
758PhosphorylationFKAGDIITELESVDD
EECCCEEEEEECCCC		34.5520873877
762PhosphorylationDIITELESVDDDWMS
CEEEEEECCCCCHHH		43.3929507054
769PhosphorylationSVDDDWMSGELMGKS
CCCCCHHHCHHCCCC		25.5120873877
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 SH319_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH319_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 SH319_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SH3Y1_HUMANSH3YL1physical
12615363
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 SH319_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-150, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-452, AND MASSSPECTROMETRY.

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