GIT2_HUMAN - dbPTM
GIT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GIT2_HUMAN
UniProt AC Q14161
Protein Name ARF GTPase-activating protein GIT2
Gene Name GIT2
Organism Homo sapiens (Human).
Sequence Length 759
Subcellular Localization
Protein Description GTPase-activating protein for the ADP ribosylation factor family..
Protein Sequence MSKRLRSSEVCADCSGPDPSWASVNRGTFLCDECCSVHRSLGRHISQVRHLKHTPWPPTLLQMVETLYNNGANSIWEHSLLDPASIMSGRRKANPQDKVHPNKAEFIRAKYQMLAFVHRLPCRDDDSVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFFHPEKGNTPLHVASKAGQILQAELLAVYGADPGTQDSSGKTPVDYARQGGHHELAERLVEIQYELTDRLAFYLCGRKPDHKNGQHFIIPQMADSSLDLSELAKAAKKKLQSLSNHLFEELAMDVYDEVDRRETDAVWLATQNHSALVTETTVVPFLPVNPEYSSTRNQGRQKLARFNAHEFATLVIDILSDAKRRQQGSSLSGSKDNVELILKTINNQHSVESQDNDQPDYDSVASDEDTDLETTASKTNRQKSLDSDLSDGPVTVQEFMEVKNALVASEAKIQQLMKVNNNLSDELRIMQKKLQTLQSENSNLRKQATTNVYQVQTGSEYTDTSNHSSLKRRPSARGSRPMSMYETGSGQKPYLPMGEASRPEESRMRLQPFPAHIGRSALVTSSSSLPSFPSTLSWSRDESARRASRLEKQNSTPESDYDNTPNDMEPDGMGSSRKGRQRSMVWPGDGLVPDTAEPHVAPSPTLPSTEDVIRKTEQITKNIQELLRAAQENKHDSYIPCSERIHVAVTEMAALFPKKPKSDMVRTSLRLLTSSAYRLQSECKKTLPGDPGSPTDVQLVTQQVIQCAYDIAKAAKQLVTITTKENNN
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
7Phosphorylation-MSKRLRSSEVCADC
-CCCCCCCCCCCCCC
35.1323663014
8PhosphorylationMSKRLRSSEVCADCS
CCCCCCCCCCCCCCC
27.8423663014
20PhosphorylationDCSGPDPSWASVNRG
CCCCCCCCHHCCCCC
42.5327080861
23PhosphorylationGPDPSWASVNRGTFL
CCCCCHHCCCCCCEE
17.4227080861
28PhosphorylationWASVNRGTFLCDECC
HHCCCCCCEECHHHH
15.3627080861
36PhosphorylationFLCDECCSVHRSLGR
EECHHHHHHHHHHHH
32.3927080861
46PhosphorylationRSLGRHISQVRHLKH
HHHHHHHHHHCCCCC
19.2523532336
98UbiquitinationRKANPQDKVHPNKAE
CCCCCCCCCCCCHHH
36.88-
103UbiquitinationQDKVHPNKAEFIRAK
CCCCCCCHHHHHHHH
54.46-
127PhosphorylationLPCRDDDSVTAKDLS
CCCCCCCCCCHHHHH
28.5028857561
129PhosphorylationCRDDDSVTAKDLSKQ
CCCCCCCCHHHHHHH
31.7628857561
131UbiquitinationDDDSVTAKDLSKQLH
CCCCCCHHHHHHHHH
50.24-
135AcetylationVTAKDLSKQLHSSVR
CCHHHHHHHHHHHHH
65.2625953088
135MalonylationVTAKDLSKQLHSSVR
CCHHHHHHHHHHHHH
65.2626320211
135UbiquitinationVTAKDLSKQLHSSVR
CCHHHHHHHHHHHHH
65.26-
139PhosphorylationDLSKQLHSSVRTGNL
HHHHHHHHHHHHCCH
38.8428857561
154PhosphorylationETCLRLLSLGAQANF
HHHHHHHHHCCCCEE
29.3728857561
166AcetylationANFFHPEKGNTPLHV
CEECCCCCCCCCCHH
63.0125953088
195PhosphorylationVYGADPGTQDSSGKT
HHCCCCCCCCCCCCC
34.29-
224PhosphorylationERLVEIQYELTDRLA
HHHHHHHHHHHHHHH
20.6827642862
227PhosphorylationVEIQYELTDRLAFYL
HHHHHHHHHHHHHHH
13.7224719451
255PhosphorylationIIPQMADSSLDLSEL
EECCCCCCCCCHHHH
24.2224247654
258 (in isoform 10)Phosphorylation-50.5322617229
262 (in isoform 10)Phosphorylation-5.49-
286PhosphorylationEELAMDVYDEVDRRE
HHHHHHHHHHHHHHH
11.3422817900
360PhosphorylationAKRRQQGSSLSGSKD
HHHHHCCCCCCCCHH
24.6223403867
361PhosphorylationKRRQQGSSLSGSKDN
HHHHCCCCCCCCHHH
33.1223403867
363PhosphorylationRQQGSSLSGSKDNVE
HHCCCCCCCCHHHHH
42.8623403867
365PhosphorylationQGSSLSGSKDNVELI
CCCCCCCCHHHHHHH
33.2023401153
366UbiquitinationGSSLSGSKDNVELIL
CCCCCCCHHHHHHHH
57.77-
375PhosphorylationNVELILKTINNQHSV
HHHHHHHHHHCCCCC
26.0323927012
381PhosphorylationKTINNQHSVESQDND
HHHHCCCCCCCCCCC
20.1623927012
381 (in isoform 11)Phosphorylation-20.16-
381 (in isoform 2)Phosphorylation-20.16-
384PhosphorylationNNQHSVESQDNDQPD
HCCCCCCCCCCCCCC
40.4523927012
384 (in isoform 11)Phosphorylation-40.45-
384 (in isoform 2)Phosphorylation-40.45-
392PhosphorylationQDNDQPDYDSVASDE
CCCCCCCCCCCCCCC
19.4623927012
392 (in isoform 11)Phosphorylation-19.46-
392 (in isoform 2)Phosphorylation-19.46-
394PhosphorylationNDQPDYDSVASDEDT
CCCCCCCCCCCCCCC
17.2223927012
394 (in isoform 11)Phosphorylation-17.22-
394 (in isoform 2)Phosphorylation-17.22-
397PhosphorylationPDYDSVASDEDTDLE
CCCCCCCCCCCCCHH
39.1025159151
397 (in isoform 11)Phosphorylation-39.10-
397 (in isoform 2)Phosphorylation-39.10-
401PhosphorylationSVASDEDTDLETTAS
CCCCCCCCCHHHHCC
40.2030278072
405PhosphorylationDEDTDLETTASKTNR
CCCCCHHHHCCHHHH
34.6523927012
406PhosphorylationEDTDLETTASKTNRQ
CCCCHHHHCCHHHHC
21.4023927012
408PhosphorylationTDLETTASKTNRQKS
CCHHHHCCHHHHCHH
37.6123927012
410PhosphorylationLETTASKTNRQKSLD
HHHHCCHHHHCHHCC
32.8926074081
415PhosphorylationSKTNRQKSLDSDLSD
CHHHHCHHCCCCCCC
29.1330266825
415 (in isoform 11)Phosphorylation-29.13-
415 (in isoform 2)Phosphorylation-29.13-
418PhosphorylationNRQKSLDSDLSDGPV
HHCHHCCCCCCCCCE
45.8330266825
418 (in isoform 11)Phosphorylation-45.83-
418 (in isoform 2)Phosphorylation-45.83-
421PhosphorylationKSLDSDLSDGPVTVQ
HHCCCCCCCCCEEHH
45.5830266825
421 (in isoform 11)Phosphorylation-45.58-
421 (in isoform 2)Phosphorylation-45.58-
426PhosphorylationDLSDGPVTVQEFMEV
CCCCCCEEHHHHHHH
21.4330266825
434UbiquitinationVQEFMEVKNALVASE
HHHHHHHHHHHHHCH
24.17-
443UbiquitinationALVASEAKIQQLMKV
HHHHCHHHHHHHHHH
36.68-
449UbiquitinationAKIQQLMKVNNNLSD
HHHHHHHHHCCCHHH
50.86-
455PhosphorylationMKVNNNLSDELRIMQ
HHHCCCHHHHHHHHH
31.0329978859
464UbiquitinationELRIMQKKLQTLQSE
HHHHHHHHHHHHHHC
29.00-
467PhosphorylationIMQKKLQTLQSENSN
HHHHHHHHHHHCCCH
36.8822210691
470PhosphorylationKKLQTLQSENSNLRK
HHHHHHHHCCCHHHH
41.6929978859
473PhosphorylationQTLQSENSNLRKQAT
HHHHHCCCHHHHHCC
32.9423401153
477UbiquitinationSENSNLRKQATTNVY
HCCCHHHHHCCCCEE
47.66-
480PhosphorylationSNLRKQATTNVYQVQ
CHHHHHCCCCEEEEE
19.1921945579
481PhosphorylationNLRKQATTNVYQVQT
HHHHHCCCCEEEEEC
26.2121945579
484PhosphorylationKQATTNVYQVQTGSE
HHCCCCEEEEECCCC
12.6821945579
486 (in isoform 11)Phosphorylation-2.77-
488PhosphorylationTNVYQVQTGSEYTDT
CCEEEEECCCCCCCC
43.7621945579
490PhosphorylationVYQVQTGSEYTDTSN
EEEEECCCCCCCCCC
30.7121945579
492PhosphorylationQVQTGSEYTDTSNHS
EEECCCCCCCCCCCC
16.1821945579
493PhosphorylationVQTGSEYTDTSNHSS
EECCCCCCCCCCCCH
28.8421945579
495PhosphorylationTGSEYTDTSNHSSLK
CCCCCCCCCCCCHHC
24.5123401153
496PhosphorylationGSEYTDTSNHSSLKR
CCCCCCCCCCCHHCC
35.0423401153
499PhosphorylationYTDTSNHSSLKRRPS
CCCCCCCCHHCCCCC
41.4321945579
500PhosphorylationTDTSNHSSLKRRPSA
CCCCCCCHHCCCCCC
30.2921945579
506PhosphorylationSSLKRRPSARGSRPM
CHHCCCCCCCCCCCC
28.8724144214
510PhosphorylationRRPSARGSRPMSMYE
CCCCCCCCCCCCEEE
27.8823927012
514PhosphorylationARGSRPMSMYETGSG
CCCCCCCCEEECCCC
22.3923927012
516PhosphorylationGSRPMSMYETGSGQK
CCCCCCEEECCCCCC
11.7530576142
518PhosphorylationRPMSMYETGSGQKPY
CCCCEEECCCCCCCC
21.1128450419
520PhosphorylationMSMYETGSGQKPYLP
CCEEECCCCCCCCCC
45.5323927012
525PhosphorylationTGSGQKPYLPMGEAS
CCCCCCCCCCCCCCC
30.3923927012
532PhosphorylationYLPMGEASRPEESRM
CCCCCCCCCCHHHHC
44.0323927012
537PhosphorylationEASRPEESRMRLQPF
CCCCCHHHHCCCCCC
29.7023312004
551PhosphorylationFPAHIGRSALVTSSS
CCCHHCCCEEEECCC
22.2728450419
555O-linked_GlycosylationIGRSALVTSSSSLPS
HCCCEEEECCCCCCC
24.6028657654
555PhosphorylationIGRSALVTSSSSLPS
HCCCEEEECCCCCCC
24.6028450419
556O-linked_GlycosylationGRSALVTSSSSLPSF
CCCEEEECCCCCCCC
22.2728657654
556PhosphorylationGRSALVTSSSSLPSF
CCCEEEECCCCCCCC
22.2726657352
557O-linked_GlycosylationRSALVTSSSSLPSFP
CCEEEECCCCCCCCC
18.0028657654
557PhosphorylationRSALVTSSSSLPSFP
CCEEEECCCCCCCCC
18.0027794612
558PhosphorylationSALVTSSSSLPSFPS
CEEEECCCCCCCCCC
35.3422617229
559O-linked_GlycosylationALVTSSSSLPSFPST
EEEECCCCCCCCCCC
46.3728657654
559PhosphorylationALVTSSSSLPSFPST
EEEECCCCCCCCCCC
46.3722617229
562PhosphorylationTSSSSLPSFPSTLSW
ECCCCCCCCCCCCCC
55.9027794612
565PhosphorylationSSLPSFPSTLSWSRD
CCCCCCCCCCCCCCC
39.7129507054
566O-linked_GlycosylationSLPSFPSTLSWSRDE
CCCCCCCCCCCCCCH
25.6728657654
566PhosphorylationSLPSFPSTLSWSRDE
CCCCCCCCCCCCCCH
25.6729507054
568O-linked_GlycosylationPSFPSTLSWSRDESA
CCCCCCCCCCCCHHH
24.0828657654
568PhosphorylationPSFPSTLSWSRDESA
CCCCCCCCCCCCHHH
24.0822617229
570O-linked_GlycosylationFPSTLSWSRDESARR
CCCCCCCCCCHHHHH
26.8628657654
570PhosphorylationFPSTLSWSRDESARR
CCCCCCCCCCHHHHH
26.8628450419
574PhosphorylationLSWSRDESARRASRL
CCCCCCHHHHHHHHH
31.2229978859
579PhosphorylationDESARRASRLEKQNS
CHHHHHHHHHHHHCC
35.2726437602
586PhosphorylationSRLEKQNSTPESDYD
HHHHHHCCCCCHHCC
42.7323401153
587PhosphorylationRLEKQNSTPESDYDN
HHHHHCCCCCHHCCC
38.3323911959
590PhosphorylationKQNSTPESDYDNTPN
HHCCCCCHHCCCCCC
42.5524043423
592PhosphorylationNSTPESDYDNTPNDM
CCCCCHHCCCCCCCC
22.0020007894
595PhosphorylationPESDYDNTPNDMEPD
CCHHCCCCCCCCCCC
22.1423403867
596 (in isoform 11)Phosphorylation-40.87-
606PhosphorylationMEPDGMGSSRKGRQR
CCCCCCCCCCCCCCC
20.3423403867
607PhosphorylationEPDGMGSSRKGRQRS
CCCCCCCCCCCCCCC
32.0823403867
614PhosphorylationSRKGRQRSMVWPGDG
CCCCCCCCCCCCCCC
14.8922617229
626PhosphorylationGDGLVPDTAEPHVAP
CCCCCCCCCCCCCCC
27.1828464451
634PhosphorylationAEPHVAPSPTLPSTE
CCCCCCCCCCCCCHH
22.3025627689
668PhosphorylationAQENKHDSYIPCSER
HHHCCCCCCCCHHHH
25.3623663014
669PhosphorylationQENKHDSYIPCSERI
HHCCCCCCCCHHHHH
18.2323403867
673PhosphorylationHDSYIPCSERIHVAV
CCCCCCHHHHHHHHH
25.26-
693PhosphorylationLFPKKPKSDMVRTSL
HCCCCCCHHHHHHHH
39.19-
698PhosphorylationPKSDMVRTSLRLLTS
CCHHHHHHHHHHHHH
22.24-
699PhosphorylationKSDMVRTSLRLLTSS
CHHHHHHHHHHHHHH
10.8325137130
717PhosphorylationLQSECKKTLPGDPGS
HHHHHHHCCCCCCCC
24.5528450419
724PhosphorylationTLPGDPGSPTDVQLV
CCCCCCCCCCHHHHH
29.9828450419
726PhosphorylationPGDPGSPTDVQLVTQ
CCCCCCCCHHHHHHH
50.9628464451
732PhosphorylationPTDVQLVTQQVIQCA
CCHHHHHHHHHHHHH
23.1322199227
740PhosphorylationQQVIQCAYDIAKAAK
HHHHHHHHHHHHHHH
18.6020068231
747UbiquitinationYDIAKAAKQLVTITT
HHHHHHHHHHHEEEE
49.37-

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
195TPhosphorylationKinaseATMQ13315
PSP
384SPhosphorylationKinaseATMQ13315
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GIT2_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 GIT2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARBK1_HUMANADRBK1physical
10896954
PAXI_HUMANPXNphysical
11251077
PCLO_HUMANPCLOphysical
12473661
GIT1_HUMANGIT1physical
12473661
GIT2_HUMANGIT2physical
12473661
TRAF1_HUMANTRAF1physical
21988832
TSN_HUMANTSNphysical
21988832
NEMO_HUMANIKBKGphysical
21988832
TNIP1_HUMANTNIP1physical
21988832
BGLR_HUMANGUSBphysical
21988832
TNAP3_HUMANTNFAIP3physical
21988832
SHLB2_HUMANSH3GLB2physical
21988832
K1C18_HUMANKRT18physical
21988832
HGD_HUMANHGDphysical
21988832
LMNB1_HUMANLMNB1physical
21988832
SMAD3_HUMANSMAD3physical
21988832
IKBB_HUMANNFKBIBphysical
21988832
NDKB_HUMANNME2physical
21988832
PROX1_HUMANPROX1physical
21988832
RECO_HUMANRCVRNphysical
21988832
SPOP_HUMANSPOPphysical
21988832
SAFB2_HUMANSAFB2physical
21988832
RUSC2_HUMANRUSC2physical
21988832
MVP_HUMANMVPphysical
21988832
HNRL1_HUMANHNRNPUL1physical
21988832
NADC_HUMANQPRTphysical
21988832
UBQL1_HUMANUBQLN1physical
21988832
KCTD5_HUMANKCTD5physical
21988832
RUFY1_HUMANRUFY1physical
21988832
USBP1_HUMANUSHBP1physical
21988832
RPA2_HUMANPOLR1Bphysical
21988832
ARHG6_HUMANARHGEF6physical
28514442
ARHG7_HUMANARHGEF7physical
28514442
GIT1_HUMANGIT1physical
28514442
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435
TFPT_HUMANTFPTphysical
27173435
CCHCR_HUMANCCHCR1physical
27173435
YETS4_HUMANYEATS4physical
27173435
TUFT1_HUMANTUFT1physical
27173435
GOGA5_HUMANGOLGA5physical
27173435
RBG10_HUMANRABGAP1Lphysical
27173435
RBG1L_HUMANRABGAP1Lphysical
27173435
CLOCK_HUMANCLOCKphysical
27173435
PSMD9_HUMANPSMD9physical
27173435
VPS53_HUMANVPS53physical
27173435
DZIP3_HUMANDZIP3physical
27173435
GRAP1_HUMANGRIPAP1physical
27173435
RCOR1_HUMANRCOR1physical
27173435
HM20A_HUMANHMG20Aphysical
27173435
VPS50_HUMANCCDC132physical
27173435
CCD93_HUMANCCDC93physical
27173435
MS18B_HUMANOIP5physical
27173435
PF21A_HUMANPHF21Aphysical
27173435
CAVN1_HUMANPTRFphysical
27173435
PHLB3_HUMANPHLDB3physical
27173435
HAUS6_HUMANHAUS6physical
27173435
RPR1A_HUMANRPRD1Aphysical
27173435
RABX5_HUMANRABGEF1physical
27173435
BMAL1_HUMANARNTLphysical
27173435
NUF2_HUMANNUF2physical
27173435
THA11_HUMANTHAP11physical
27173435
VPS51_HUMANVPS51physical
27173435
EIPR1_HUMANTSSC1physical
27173435
RABE1_HUMANRABEP1physical
27173435

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 GIT2_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-394; SER-397; SER-559AND SER-614, AND MASS SPECTROMETRY.
"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-394 AND SER-397, ANDMASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559 AND SER-614, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-397; SER-415;SER-418 AND SER-421, AND MASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-488 AND SER-496, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-484 AND TYR-492, ANDMASS SPECTROMETRY.

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