RUSC1_HUMAN - dbPTM
RUSC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RUSC1_HUMAN
UniProt AC Q9BVN2
Protein Name RUN and SH3 domain-containing protein 1
Gene Name RUSC1
Organism Homo sapiens (Human).
Sequence Length 902
Subcellular Localization Cytoplasm. Nucleus. Cytoplasm, cytoskeleton. Cytoplasmic vesicle. Early endosome. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Golgi apparatus. Translocated to the nuclear envelope upon stimulation with NGF. Associated wi
Protein Description Putative signaling adapter which may play a role in neuronal differentiation. May be involved in regulation of NGF-dependent neurite outgrowth. Proposed to play a role in neuronal vesicular trafficking, specifically involving pre-synaptic membrane proteins. Seems to be involved in signaling pathways that are regulated by the prolonged activation of MAPK. Can regulate the polyubiquitination of IKBKG and thus may be involved in regulation of the NF-kappa-B pathway..
Protein Sequence MLSPQRALLCNLNHIHLQHVSLGLHLSRRPELQEGPLSTPPPPGDTGGKESRGPCSGTLVDANSNSPAVPCRCCQEHGPGLENRQDPSQEEEGAASPSDPGCSSSLSSCSDLSPDESPVSVYLRDLPGDEDAHPQPSIIPLEQGSPLASAGPGTCSPDSFCCSPDSCSGASSSPDPGLDSNCNALTTCQDVPSPGLEEEDERAEQDLPTSELLEADDGKIDAGKTEPSWKINPIWKIDTEKTKAEWKTTENNNTGWKNNGNVNSSWKSEPEKFDSGWKTNTRITDSGSKTDAGKIDGGWRSDVSEEPVPHRTITSFHELAQKRKRGPGLPLVPQAKKDRSDWLIVFSPDTELPPSGSPGGSSAPPREVTTFKELRSRSRAPAPPVPPRDPPVGWALVPPRPPPPPVPPRRKKNRPGLQPIAEGQSEEGRAVSPAAGEEAPAAKEPGAQAGLEVRSSWSFAGVPGAQRLWMAEAQSGTGQLQEQKKGLLIAVSVSVDKIISHFGAARNLVQKAQLGDSRLSPDVGHLVLTTLCPALHALVADGLKPFRKDLITGQRRSSPWSVVEASVKPGSSTRSLGTLYSQVSRLAPLSSSRSRFHAFILGLLNTKQLELWFSSLQEDAGLLSLLYLPTGFFSLARGGCPSLSTELLLLLQPLSVLTFHLDLLFEHHHHLPLGPPQAPAPPGPPPALQQTMQAMLHFGGRLAQSLRGTSKEAASDPSDSPNLPTPGSWWEQLTQASRVYASGGTEGFPLSRWAPGRHGTAAEEGAQERPLPTDEMAPGRGLWLGRLFGVPGGPAENENGALKSRRPSSWLPPTVSVLALVKRGAPPEMPSPQELEASAPRMVQTHRAVRALCDHTAARPDQLSFRRGEVLRVITTVDEDWLRCGRDGMEGLVPVGYTSLVL
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
3Phosphorylation-----MLSPQRALLC
-----CCCHHHHHHH		20.0721815630
42 (in isoform 2)Ubiquitination-46.8621906983
74UbiquitinationPAVPCRCCQEHGPGL
CCCCCCCCHHHCCCC		2.48-
101UbiquitinationAASPSDPGCSSSLSS
CCCCCCCCCCCCCCC		29.0021906983
224UbiquitinationDGKIDAGKTEPSWKI
CCCCCCCCCCCCCCC		51.97-
225PhosphorylationGKIDAGKTEPSWKIN
CCCCCCCCCCCCCCC		52.8123403867
228PhosphorylationDAGKTEPSWKINPIW
CCCCCCCCCCCCCEE		34.4723403867
230UbiquitinationGKTEPSWKINPIWKI
CCCCCCCCCCCEEEE		36.62-
242 (in isoform 2)Ubiquitination-29.2921906983
268PhosphorylationNVNSSWKSEPEKFDS
CCCCCCCCCCHHCCC		52.7227251275
288PhosphorylationTRITDSGSKTDAGKI
CEECCCCCCCCCCCC		36.0117081983
301UbiquitinationKIDGGWRSDVSEEPV
CCCCCCCCCCCCCCC		35.54-
334 (in isoform 2)Ubiquitination-59.3321906983
350PhosphorylationLIVFSPDTELPPSGS
EEEECCCCCCCCCCC		42.69-
376PhosphorylationTTFKELRSRSRAPAP
CCHHHHHHCCCCCCC		47.4321130716
378PhosphorylationFKELRSRSRAPAPPV
HHHHHHCCCCCCCCC		33.7621130716
393UbiquitinationPPRDPPVGWALVPPR
CCCCCCCCCEECCCC		15.0921906983
432PhosphorylationSEEGRAVSPAAGEEA
CCCCCCCCCCCCCCC		14.0828857561
475PhosphorylationLWMAEAQSGTGQLQE
EEEHHCCCCCCCCHH		45.4224043423
477PhosphorylationMAEAQSGTGQLQEQK
EHHCCCCCCCCHHHH		27.3124043423
484UbiquitinationTGQLQEQKKGLLIAV
CCCCHHHHCCEEEEE		48.32-
492PhosphorylationKGLLIAVSVSVDKII
CCEEEEEEEEHHHHH		10.31-
494PhosphorylationLLIAVSVSVDKIISH
EEEEEEEEHHHHHHH		19.66-
500PhosphorylationVSVDKIISHFGAARN
EEHHHHHHHHHHHHH		19.0822210691
511 (in isoform 1)Ubiquitination-30.5321906983
511UbiquitinationAARNLVQKAQLGDSR
HHHHHHHHHHHCCCC		30.5321906983
552PhosphorylationPFRKDLITGQRRSSP
HHHHHHCCCCCCCCC		34.2627174698
580PhosphorylationTRSLGTLYSQVSRLA
CCCHHHHHHHHHHHH		9.2629496907
584PhosphorylationGTLYSQVSRLAPLSS
HHHHHHHHHHHCCCC		17.59-
590PhosphorylationVSRLAPLSSSRSRFH
HHHHHCCCCCHHHHH		25.8024260401
591PhosphorylationSRLAPLSSSRSRFHA
HHHHCCCCCHHHHHH		37.1424260401
592PhosphorylationRLAPLSSSRSRFHAF
HHHCCCCCHHHHHHH		30.7928842319
634PhosphorylationYLPTGFFSLARGGCP
HCCCCHHHHHCCCCC		20.8922964224
711 (in isoform 1)Ubiquitination-51.7321906983
711UbiquitinationQSLRGTSKEAASDPS
HHHHCCCHHHCCCCC		51.7321906983
715PhosphorylationGTSKEAASDPSDSPN
CCCHHHCCCCCCCCC		58.0427732954
718PhosphorylationKEAASDPSDSPNLPT
HHHCCCCCCCCCCCC		56.5727732954
720PhosphorylationAASDPSDSPNLPTPG
HCCCCCCCCCCCCCC		21.7417192257
725PhosphorylationSDSPNLPTPGSWWEQ
CCCCCCCCCCHHHHH		43.3727732954
728PhosphorylationPNLPTPGSWWEQLTQ
CCCCCCCHHHHHHHH		30.1627732954
734PhosphorylationGSWWEQLTQASRVYA
CHHHHHHHHHHEEEE		23.0627732954
740PhosphorylationLTQASRVYASGGTEG
HHHHHEEEECCCCCC		8.2429978859
742PhosphorylationQASRVYASGGTEGFP
HHHEEEECCCCCCCC		21.7728555341
803UbiquitinationENENGALKSRRPSSW
CCCCCCCCCCCCHHC		41.192190698
803 (in isoform 1)Ubiquitination-41.1921906983
808PhosphorylationALKSRRPSSWLPPTV
CCCCCCCHHCCCCCH		32.1328857561
809PhosphorylationLKSRRPSSWLPPTVS
CCCCCCHHCCCCCHH		35.0027251275
831PhosphorylationGAPPEMPSPQELEAS
CCCCCCCCHHHHHHC		37.5921815630
838PhosphorylationSPQELEASAPRMVQT
CHHHHHHCCCCHHHH		29.4528555341
856PhosphorylationVRALCDHTAARPDQL
HHHHCHHCCCCCHHH		14.5727251275
864PhosphorylationAARPDQLSFRRGEVL
CCCCHHHHCCCCCEE		15.8628857561
899PhosphorylationLVPVGYTSLVL----
CEECCCCEEEC----		14.1624719451
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
-KUbiquitinationE3 ubiquitin ligaseTRAF6Q9Y4K3
PMID:19365808
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RUSC1_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 RUSC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
FAM9B_HUMANFAM9Bphysical
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 RUSC1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-720, AND MASSSPECTROMETRY.

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