GIT1_MOUSE - dbPTM
GIT1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GIT1_MOUSE
UniProt AC Q68FF6
Protein Name ARF GTPase-activating protein GIT1
Gene Name Git1
Organism Mus musculus (Mouse).
Sequence Length 770
Subcellular Localization Cytoplasm. Cycles between at least 3 distinct intracellular compartments, including focal adhesions, cytoplasmic complexes and membrane protrusions. During cell migration, when cells detach, moves from the adhesions into the cytoplasmic complexes tow
Protein Description GTPase-activating protein for the ADP ribosylation factor family. May serve as a scaffold to bring together molecules to form signaling modules controlling vesicle trafficking, adhesion and cytoskeletal organization. Increases the speed of cell migration, as well as the size and rate of formation of protrusions, possibly by targeting PAK1 to adhesions and the leading edge of lamellipodia. Sequesters inactive non-tyrosine-phosphorylated paxillin in cytoplasmic complexes (By similarity). Involved in the regulation of cytokinesis; the function may involve SDCCAG3 and PTPN13. [PubMed: 23108400]
Protein Sequence MSRKGPRAEVCADCSAPDPGWASISRGVLVCDECCSVHRSLGRHISIVKHLRHSAWPPTLLQMVHTLASNGANSIWEHSLLDPAQVQSGRRKANPQDKVHPIKSEFIRAKYQMLAFVHKLPCRDDDGVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFFHPEKGTTPLHVAAKAGQTLQAELLVVYGADPGSPDVNGRTPIDYARQAGHHELAERLVECQYELTDRLAFYLCGRKPDHKNGHYIIPQMADRSRQKCMSQSLDLSELAKAAKKKLQALSNRLFEELAMDVYDEVDRRENDAVWLATQNHSTLVTERSAVPFLPVNPEYSATRNQGRQKLARFNAREFATLIIDILSEAKRRQQGKSLSSPTDNLELSARSQSELDDQHDYDSVASDEDTDQEPLPSAGATRNNRARSMDSSDLSDGAVTLQEYLELKKALATSEAKVQQLMKVNSSLSDELRRLQREIHKLQAENLQLRQPPGPVPPPSLPSERAEHTLMGPGGSTHRRDRQAFSMYEPGSALKPFGGTPGDELATRLQPFHSTELEDDAIYSVHVPAGLYRIRKGVSASSVPFTPSSPLLSCSQEGSRHASKLSRHGSGADSDYENTQSGDPLLGLEGKRFLELSKEDELHPELESLDGDLDPGLPSTEDVILKTEQVTKNIQELLRAAQEFKHDSFVPCSEKIHLAVTEMASLFPKRPALEPVRSSLRLLNASAYRLQSECRKTVPPEPGAPVDFQLLTQQVIQCAYDIAKAAKQLVTITTREKKQ
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
104PhosphorylationDKVHPIKSEFIRAKY
CCCCCCHHHHHHHHH		38.1626824392
224PhosphorylationERLVECQYELTDRLA
HHHHHHHHHHHHHHH		25.2718034455
261PhosphorylationRSRQKCMSQSLDLSE
HHHHHHHHHCCCHHH		26.5329899451
263PhosphorylationRQKCMSQSLDLSELA
HHHHHHHCCCHHHHH		19.2829899451
281PhosphorylationKKKLQALSNRLFEEL
HHHHHHHHHHHHHHH		23.9522802335
293PhosphorylationEELAMDVYDEVDRRE
HHHHHHHHHHHHHHH		11.34-
330PhosphorylationFLPVNPEYSATRNQG
CCCCCHHHCCCCCHH		12.59-
368PhosphorylationKRRQQGKSLSSPTDN
HHHHCCCCCCCCCCC		40.0624925903
370PhosphorylationRQQGKSLSSPTDNLE
HHCCCCCCCCCCCHH		41.1725521595
371PhosphorylationQQGKSLSSPTDNLEL
HCCCCCCCCCCCHHH		36.7918388127
373PhosphorylationGKSLSSPTDNLELSA
CCCCCCCCCCHHHHH		39.1925521595
379PhosphorylationPTDNLELSARSQSEL
CCCCHHHHHHCHHHC		16.5628833060
382PhosphorylationNLELSARSQSELDDQ
CHHHHHHCHHHCCCC		37.4624925903
384PhosphorylationELSARSQSELDDQHD
HHHHHCHHHCCCCCC		41.1824925903
392PhosphorylationELDDQHDYDSVASDE
HCCCCCCCCCCCCCC		14.1624925903
394PhosphorylationDDQHDYDSVASDEDT
CCCCCCCCCCCCCCC		17.2225521595
397PhosphorylationHDYDSVASDEDTDQE
CCCCCCCCCCCCCCC		39.1025521595
401PhosphorylationSVASDEDTDQEPLPS
CCCCCCCCCCCCCCC		37.2225521595
408PhosphorylationTDQEPLPSAGATRNN
CCCCCCCCCCCCCCC		47.2025619855
412PhosphorylationPLPSAGATRNNRARS
CCCCCCCCCCCCCCC		32.7725619855
419PhosphorylationTRNNRARSMDSSDLS
CCCCCCCCCCHHHCC		26.4226824392
422PhosphorylationNRARSMDSSDLSDGA
CCCCCCCHHHCCCCC		19.6721082442
423PhosphorylationRARSMDSSDLSDGAV
CCCCCCHHHCCCCCE		38.0021082442
426PhosphorylationSMDSSDLSDGAVTLQ
CCCHHHCCCCCEEHH		38.7027087446
431PhosphorylationDLSDGAVTLQEYLEL
HCCCCCEEHHHHHHH		23.3825619855
457PhosphorylationQQLMKVNSSLSDELR
HHHHHHCCHHHHHHH		35.3320415495
458PhosphorylationQLMKVNSSLSDELRR
HHHHHCCHHHHHHHH		27.0429176673
507PhosphorylationTLMGPGGSTHRRDRQ
CCCCCCCCCCCCCCC		27.2725521595
508PhosphorylationLMGPGGSTHRRDRQA
CCCCCCCCCCCCCCC		23.7624719451
517PhosphorylationRRDRQAFSMYEPGSA
CCCCCCCCCCCCCCC		24.3826824392
519PhosphorylationDRQAFSMYEPGSALK
CCCCCCCCCCCCCCC		20.1319060867
523PhosphorylationFSMYEPGSALKPFGG
CCCCCCCCCCCCCCC		40.9429472430
545PhosphorylationTRLQPFHSTELEDDA
HHCCCCCCCCCCCCC		24.7726824392
546PhosphorylationRLQPFHSTELEDDAI
HCCCCCCCCCCCCCE		35.7018515860
554PhosphorylationELEDDAIYSVHVPAG
CCCCCCEEEEEECCC		13.3218515860
555PhosphorylationLEDDAIYSVHVPAGL
CCCCCEEEEEECCCH		10.3022499769
563PhosphorylationVHVPAGLYRIRKGVS
EEECCCHHHCCCCCC		11.7722499769
570O-linked_GlycosylationYRIRKGVSASSVPFT
HHCCCCCCCCCCCCC		30.9722645316
570PhosphorylationYRIRKGVSASSVPFT
HHCCCCCCCCCCCCC		30.9725521595
572PhosphorylationIRKGVSASSVPFTPS
CCCCCCCCCCCCCCC		25.1025619855
573PhosphorylationRKGVSASSVPFTPSS
CCCCCCCCCCCCCCC		33.2625619855
577PhosphorylationSASSVPFTPSSPLLS
CCCCCCCCCCCCCCC		19.0525619855
579PhosphorylationSSVPFTPSSPLLSCS
CCCCCCCCCCCCCCC		41.3425619855
580PhosphorylationSVPFTPSSPLLSCSQ
CCCCCCCCCCCCCCC		22.2923527152
584PhosphorylationTPSSPLLSCSQEGSR
CCCCCCCCCCCCCHH		21.2925619855
585GlutathionylationPSSPLLSCSQEGSRH
CCCCCCCCCCCCHHH		4.9924333276
586PhosphorylationSSPLLSCSQEGSRHA
CCCCCCCCCCCHHHH		28.0825619855
590PhosphorylationLSCSQEGSRHASKLS
CCCCCCCHHHHHHHH		21.8225619855
594PhosphorylationQEGSRHASKLSRHGS
CCCHHHHHHHHHCCC		28.1826643407
597PhosphorylationSRHASKLSRHGSGAD
HHHHHHHHHCCCCCC		26.4326745281
601PhosphorylationSKLSRHGSGADSDYE
HHHHHCCCCCCCCCC		25.3618388127
605PhosphorylationRHGSGADSDYENTQS
HCCCCCCCCCCCCCC		41.3718388127
607PhosphorylationGSGADSDYENTQSGD
CCCCCCCCCCCCCCC		18.2824925903
610PhosphorylationADSDYENTQSGDPLL
CCCCCCCCCCCCCCC		16.5118388127
612PhosphorylationSDYENTQSGDPLLGL
CCCCCCCCCCCCCCC		43.0325619855
628PhosphorylationGKRFLELSKEDELHP
CHHHHHHCCCCCCCH		25.3222324799
639PhosphorylationELHPELESLDGDLDP
CCCHHHHHCCCCCCC		44.3727180971
679PhosphorylationAQEFKHDSFVPCSEK
HHHHCCCCCCCCHHH		28.0626824392
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 GIT1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GIT1_MOUSE !!
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 GIT1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNX6_MOUSESnx6physical
18523162
1433Z_MOUSEYwhazphysical
16959763
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GIT1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-517 ANDSER-601, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-371 ANDSER-394, AND MASS SPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-554, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-224, AND MASSSPECTROMETRY.

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