GA2L1_HUMAN - dbPTM
GA2L1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GA2L1_HUMAN
UniProt AC Q99501
Protein Name GAS2-like protein 1
Gene Name GAS2L1
Organism Homo sapiens (Human).
Sequence Length 681
Subcellular Localization Cytoplasm, cytoskeleton .
Protein Description Seems to be involved in the cross-linking of microtubules and microfilaments..
Protein Sequence MADPVAGIAGSAAKSVRPFRSSEAYVEAMKEDLAEWLNALYGLGLPGGGDGFLTGLATGTTLCQHANAVTEAARALAAARPARGVAFQAHSVVPGSFMARDNVATFIGWCRVELGVPEVLMFETEDLVLRKNEKSVVLCLLEVARRGARLGLLAPRLVQFEQEIERELRAAPPAPNAPAAGEDTTETAPAPGTPARGPRMTPSDLRNLDELVREILGRCTCPDQFPMIKVSEGKYRVGDSSLLIFVRVLRSHVMVRVGGGWDTLEHYLDKHDPCRCSSTAHRPPQPRVCTFSPQRVSPTTSPRPASPVPGSERRGSRPEMTPVSLRSTKEGPETPPRPRDQLPPHPRSRRYSGDSDSSASSAQSGPLGTRSDDTGTGPRRERPSRRLTTGTPASPRRPPALRSQSRDRLDRGRPRGAPGGRGAQLSVPSPARRARSQSREEQAVLLVRRDRDGQHSWVPRGRGSGGSGRSTPQTPRARSPAAPRLSRVSSPSPELGTTPASIFRTPLQLDPQQEQQLFRRLEEEFLANARALEAVASVTPTGPVPDPARAPDPPAPDSAYCSSSSSSSSLSVLGGKCGQPGDSGRTANGLPGPRSQALSSSSDEGSPCPGMGGPLDAPGSPLACTEPSRTWARGRMDTQPDRKPSRIPTPRGPRRPSGPAELGTWHALHSVTPRAEPDSWM
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------MADPVAGIA
------CCCCCCCCC		29.7922223895
11PhosphorylationPVAGIAGSAAKSVRP
CCCCCCCHHHHCCCC		18.9425159151
14UbiquitinationGIAGSAAKSVRPFRS
CCCCHHHHCCCCCCC		49.56-
14UbiquitinationGIAGSAAKSVRPFRS
CCCCHHHHCCCCCCC		49.56-
22PhosphorylationSVRPFRSSEAYVEAM
CCCCCCCCHHHHHHH		23.2229507054
193PhosphorylationETAPAPGTPARGPRM
CCCCCCCCCCCCCCC		16.8321712546
201PhosphorylationPARGPRMTPSDLRNL
CCCCCCCCHHHHCCH		22.4121815630
220PhosphorylationREILGRCTCPDQFPM
HHHHCCCCCCCCCCE		26.2230266825
231PhosphorylationQFPMIKVSEGKYRVG
CCCEEEEECCEEEEC		35.31-
263PhosphorylationRVGGGWDTLEHYLDK
EECCCHHHHHHHHHH		27.7722210691
267PhosphorylationGWDTLEHYLDKHDPC
CHHHHHHHHHHCCCC		13.7622210691
270AcetylationTLEHYLDKHDPCRCS
HHHHHHHHCCCCCCC		47.5125953088
290PhosphorylationPPQPRVCTFSPQRVS
CCCCCEECCCCCCCC		25.0430266825
292PhosphorylationQPRVCTFSPQRVSPT
CCCEECCCCCCCCCC		11.2830266825
297PhosphorylationTFSPQRVSPTTSPRP
CCCCCCCCCCCCCCC		20.7930266825
299PhosphorylationSPQRVSPTTSPRPAS
CCCCCCCCCCCCCCC		32.1930266825
300PhosphorylationPQRVSPTTSPRPASP
CCCCCCCCCCCCCCC		39.8730266825
301PhosphorylationQRVSPTTSPRPASPV
CCCCCCCCCCCCCCC		22.7630266825
306PhosphorylationTTSPRPASPVPGSER
CCCCCCCCCCCCCCC		29.1623401153
311PhosphorylationPASPVPGSERRGSRP
CCCCCCCCCCCCCCC		23.1230266825
316PhosphorylationPGSERRGSRPEMTPV
CCCCCCCCCCCCCCC		42.7325159151
321PhosphorylationRGSRPEMTPVSLRST
CCCCCCCCCCCCCCC		20.9023927012
324PhosphorylationRPEMTPVSLRSTKEG
CCCCCCCCCCCCCCC		21.1921712546
324 (in isoform 4)Phosphorylation-21.1922210691
334PhosphorylationSTKEGPETPPRPRDQ
CCCCCCCCCCCCHHH		41.5530266825
334 (in isoform 4)Phosphorylation-41.5522210691
337 (in isoform 4)Phosphorylation-39.8422210691
348PhosphorylationQLPPHPRSRRYSGDS
HCCCCCCCCCCCCCC		26.0930576142
351PhosphorylationPHPRSRRYSGDSDSS
CCCCCCCCCCCCCCC		18.8530576142
352PhosphorylationHPRSRRYSGDSDSSA
CCCCCCCCCCCCCCC		34.0230266825
355PhosphorylationSRRYSGDSDSSASSA
CCCCCCCCCCCCCCC		42.8130266825
357PhosphorylationRYSGDSDSSASSAQS
CCCCCCCCCCCCCCC		31.5823927012
358PhosphorylationYSGDSDSSASSAQSG
CCCCCCCCCCCCCCC		36.8430278072
360PhosphorylationGDSDSSASSAQSGPL
CCCCCCCCCCCCCCC		28.3123927012
361PhosphorylationDSDSSASSAQSGPLG
CCCCCCCCCCCCCCC		30.0023927012
364PhosphorylationSSASSAQSGPLGTRS
CCCCCCCCCCCCCCC		41.9423403867
369PhosphorylationAQSGPLGTRSDDTGT
CCCCCCCCCCCCCCC		34.3823403867
374PhosphorylationLGTRSDDTGTGPRRE
CCCCCCCCCCCCCCC		41.4522210691
384PhosphorylationGPRRERPSRRLTTGT
CCCCCCCCCCCCCCC		35.9317081983
388PhosphorylationERPSRRLTTGTPASP
CCCCCCCCCCCCCCC		22.7423403867
389PhosphorylationRPSRRLTTGTPASPR
CCCCCCCCCCCCCCC		43.5823403867
391PhosphorylationSRRLTTGTPASPRRP
CCCCCCCCCCCCCCC		17.3723927012
394PhosphorylationLTTGTPASPRRPPAL
CCCCCCCCCCCCCHH		21.8328731282
403PhosphorylationRRPPALRSQSRDRLD
CCCCHHHCCCCCCHH		33.1026074081
405PhosphorylationPPALRSQSRDRLDRG
CCHHHCCCCCCHHCC		37.0826074081
421MethylationPRGAPGGRGAQLSVP
CCCCCCCCCCCCCCC		43.09-
426PhosphorylationGGRGAQLSVPSPARR
CCCCCCCCCCCHHHH		21.6526425664
429PhosphorylationGAQLSVPSPARRARS
CCCCCCCCHHHHHHH		29.0930576142
430PhosphorylationAQLSVPSPARRARSQ
CCCCCCCHHHHHHHC		24.58-
436PhosphorylationSPARRARSQSREEQA
CHHHHHHHCCHHHHE		31.3630266825
438PhosphorylationARRARSQSREEQAVL
HHHHHHCCHHHHEEE		42.7930266825
456PhosphorylationRDRDGQHSWVPRGRG
ECCCCCCCEECCCCC		23.1427251275
474PhosphorylationSGRSTPQTPRARSPA
CCCCCCCCCCCCCCC		18.8824532841
479PhosphorylationPQTPRARSPAAPRLS
CCCCCCCCCCCCCCC		20.2230266825
486PhosphorylationSPAAPRLSRVSSPSP
CCCCCCCCCCCCCCC		31.7323403867
487MethylationPAAPRLSRVSSPSPE
CCCCCCCCCCCCCCC		36.61-
489PhosphorylationAPRLSRVSSPSPELG
CCCCCCCCCCCCCCC		35.1130266825
490PhosphorylationPRLSRVSSPSPELGT
CCCCCCCCCCCCCCC		26.9229255136
492PhosphorylationLSRVSSPSPELGTTP
CCCCCCCCCCCCCCC		32.7130266825
497PhosphorylationSPSPELGTTPASIFR
CCCCCCCCCCHHHHC		42.0823927012
498PhosphorylationPSPELGTTPASIFRT
CCCCCCCCCHHHHCC		18.3023927012
501PhosphorylationELGTTPASIFRTPLQ
CCCCCCHHHHCCCCC		24.3823403867
504MethylationTTPASIFRTPLQLDP
CCCHHHHCCCCCCCH		33.49-
505PhosphorylationTPASIFRTPLQLDPQ
CCHHHHCCCCCCCHH		20.0121815630
539PhosphorylationLEAVASVTPTGPVPD
HHHHHCCCCCCCCCC		16.7927251275
558PhosphorylationPDPPAPDSAYCSSSS
CCCCCCCCCCCCCCC		21.78-
562PhosphorylationAPDSAYCSSSSSSSS
CCCCCCCCCCCCCCC		22.15-
586PhosphorylationQPGDSGRTANGLPGP
CCCCCCCCCCCCCCC		28.18-
595PhosphorylationNGLPGPRSQALSSSS
CCCCCCHHHHHCCCC		23.9628111955
599PhosphorylationGPRSQALSSSSDEGS
CCHHHHHCCCCCCCC		31.0528111955
600PhosphorylationPRSQALSSSSDEGSP
CHHHHHCCCCCCCCC		34.4128111955
601PhosphorylationRSQALSSSSDEGSPC
HHHHHCCCCCCCCCC		38.1328111955
602PhosphorylationSQALSSSSDEGSPCP
HHHHCCCCCCCCCCC		41.4528111955
606PhosphorylationSSSSDEGSPCPGMGG
CCCCCCCCCCCCCCC		22.6828111955
620PhosphorylationGPLDAPGSPLACTEP
CCCCCCCCCCCCCCC		18.7128985074
625PhosphorylationPGSPLACTEPSRTWA
CCCCCCCCCCCCCCC		45.3728111955
628PhosphorylationPLACTEPSRTWARGR
CCCCCCCCCCCCCCC		35.7928111955
633MethylationEPSRTWARGRMDTQP
CCCCCCCCCCCCCCC		25.47-
645PhosphorylationTQPDRKPSRIPTPRG
CCCCCCCCCCCCCCC		45.9725921289
649PhosphorylationRKPSRIPTPRGPRRP
CCCCCCCCCCCCCCC		24.2028060719
657PhosphorylationPRGPRRPSGPAELGT
CCCCCCCCCCCCCCC		56.4427273156
672PhosphorylationWHALHSVTPRAEPDS
CEECCCCCCCCCCCC		15.2928555341
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
352SPhosphorylationKinaseNEK2P51955
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GA2L1_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 GA2L1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MARE1_HUMANMAPRE1physical
26186194
MARE3_HUMANMAPRE3physical
26186194
NXN_HUMANNXNphysical
26186194
SNX5_HUMANSNX5physical
26186194
EPN1_HUMANEPN1physical
26186194
SH3K1_HUMANSH3KBP1physical
26186194
RRP44_HUMANDIS3physical
26186194
UBP7_HUMANUSP7physical
26186194
CCNB1_HUMANCCNB1physical
26186194
GELS_HUMANGSNphysical
26186194
WIPI3_HUMANWDR45Bphysical
26186194
ZZEF1_HUMANZZEF1physical
26186194
RBM12_HUMANRBM12physical
26186194
NAGK_HUMANNAGKphysical
26186194
PLCG1_HUMANPLCG1physical
26186194
GNB1L_HUMANGNB1Lphysical
26186194
KLH42_HUMANKLHL42physical
26186194
CDN2C_HUMANCDKN2Cphysical
26186194
MARE3_HUMANMAPRE3physical
28514442
EPN1_HUMANEPN1physical
28514442
PLCG1_HUMANPLCG1physical
28514442
MARE1_HUMANMAPRE1physical
28514442
SH3K1_HUMANSH3KBP1physical
28514442
WIPI3_HUMANWDR45Bphysical
28514442
GNB1L_HUMANGNB1Lphysical
28514442
CDN2C_HUMANCDKN2Cphysical
28514442
RRP44_HUMANDIS3physical
28514442
KLH42_HUMANKLHL42physical
28514442
CCNB1_HUMANCCNB1physical
28514442
SNX5_HUMANSNX5physical
28514442
GELS_HUMANGSNphysical
28514442
RBM12_HUMANRBM12physical
28514442
CKS2_HUMANCKS2physical
28514442
LRRF1_HUMANLRRFIP1physical
28514442
HECD3_HUMANHECTD3physical
28514442
UBP7_HUMANUSP7physical
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 GA2L1_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-352; SER-394; SER-436AND SER-438, 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 THR-193; SER-297; SER-306;THR-391; SER-394; SER-436; SER-438; SER-489; SER-490; SER-492 ANDTHR-498, AND MASS 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-352, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-352, 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-384, AND MASSSPECTROMETRY.

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