Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  GAS2-like protein 1  

UniProtKB / Swiss-Prot ID :  GA2L1_HUMAN

Gene Name (Synonyms) : 
GAS2L1, GAR22  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton (Probable). 

Protein Function :  Seems to be involved in the cross-linking of microtubules and microfilaments. 

Protein Sequence MADPVAGIAGSAAKSVRPFRSSEAYVEAMKEDLAEWLNALYGLGLPGGGDGFLTGLATGTTLCQHANAVT...
Predicted Secondary Structure CCCCCCCCCHHHHHHHHHHHHHHCCHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
490S -> G (in dbSNP:rs34124440). VAR_059974
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
193PhosphothreoninePAPGTPARG
CCCCCCCCC
16.83HPRD
Link-
193PhosphothreoninePAPGTPARG
CCCCCCCCC
16.83PhosphoELM
Link-
193PhosphothreoninePAPGTPARG
CCCCCCCCC
16.83Phosphositeplus
Link-
193PhosphothreoninePAPGTPARG
CCCCCCCCC
16.83SysPTM
Link-
193Phosphothreonine.PAPGTPARG
CCCCCCCCC
16.83UniProtKB
Link-
297PhosphoserinePQRVSPTTS
CCCCCCCCC
20.79HPRD
Link-
297PhosphoserinePQRVSPTTS
CCCCCCCCC
20.79PhosphoELM
Link-
297PhosphoserinePQRVSPTTS
CCCCCCCCC
20.79Phosphositeplus
Link-
297PhosphoserinePQRVSPTTS
CCCCCCCCC
20.79SysPTM
Link-
297Phosphoserine.PQRVSPTTS
CCCCCCCCC
20.79UniProtKB
Link-
306PhosphoserinePRPASPVPG
CCCCCCCCC
29.16HPRD
Link-
306PhosphoserinePRPASPVPG
CCCCCCCCC
29.16PhosphoELM
Link-
306PhosphoserinePRPASPVPG
CCCCCCCCC
29.16Phosphositeplus
Link-
306PhosphoserinePRPASPVPG
CCCCCCCCC
29.16SysPTM
Link-
306Phosphoserine.PRPASPVPG
CCCCCCCCC
29.16UniProtKB
Link-
352PhosphoserineSRRYSGDSD
CCCCCCCCC
34.02HPRD
Link-
352PhosphoserineSRRYSGDSD
CCCCCCCCC
34.02PhosphoELM
Link-
352PhosphoserineSRRYSGDSD
CCCCCCCCC
34.02Phosphositeplus
Link-
352PhosphoserineSRRYSGDSD
CCCCCCCCC
34.02SysPTM
Link-
352Phosphoserine.SRRYSGDSD
CCCCCCCCC
34.02UniProtKB
Link-
384PhosphoserineRERPSRRLT
CCCCCCCCC
35.93HPRD
Link-
384PhosphoserineRERPSRRLT
CCCCCCCCC
35.93SysPTM
Link-
384Phosphoserine.RERPSRRLT
CCCCCCCCC
35.93UniProtKB
Link-
391PhosphothreonineLTTGTPASP
CCCCCCCCC
17.37HPRD
Link-
391PhosphothreonineLTTGTPASP
CCCCCCCCC
17.37PhosphoELM
Link-
391PhosphothreonineLTTGTPASP
CCCCCCCCC
17.37Phosphositeplus
Link-
391PhosphothreonineLTTGTPASP
CCCCCCCCC
17.37SysPTM
Link-
391Phosphothreonine.LTTGTPASP
CCCCCCCCC
17.37UniProtKB
Link-
394PhosphoserineGTPASPRRP
CCCCCCCCC
21.83HPRD
Link-
394PhosphoserineGTPASPRRP
CCCCCCCCC
21.83PhosphoELM
Link-
394PhosphoserineGTPASPRRP
CCCCCCCCC
21.83Phosphositeplus
Link-
394PhosphoserineGTPASPRRP
CCCCCCCCC
21.83SysPTM
Link-
394Phosphoserine.GTPASPRRP
CCCCCCCCC
21.83UniProtKB
Link-
436PhosphoserineRRARSQSRE
CCCCCCCCC
31.36HPRD
Link-
436PhosphoserineRRARSQSRE
CCCCCCCCC
31.36PhosphoELM
Link-
436PhosphoserineRRARSQSRE
CCCCCCCCC
31.36Phosphositeplus
Link-
436PhosphoserineRRARSQSRE
CCCCCCCCC
31.36SysPTM
Link-
436Phosphoserine.RRARSQSRE
CCCCCCCCC
31.36UniProtKB
Link-
438PhosphoserineARSQSREEQ
CCCCCCCCC
42.79HPRD
Link-
438PhosphoserineARSQSREEQ
CCCCCCCCC
42.79PhosphoELM
Link-
438PhosphoserineARSQSREEQ
CCCCCCCCC
42.79Phosphositeplus
Link-
438PhosphoserineARSQSREEQ
CCCCCCCCC
42.79SysPTM
Link-
438Phosphoserine.ARSQSREEQ
CCCCCCCCC
42.79UniProtKB
Link-
489PhosphoserineLSRVSSPSP
CCCCCCCCC
35.11HPRD
Link-
489PhosphoserineLSRVSSPSP
CCCCCCCCC
35.11PhosphoELM
Link-
489PhosphoserineLSRVSSPSP
CCCCCCCCC
35.11Phosphositeplus
Link-
489PhosphoserineLSRVSSPSP
CCCCCCCCC
35.11SysPTM
Link-
489Phosphoserine.LSRVSSPSP
CCCCCCCCC
35.11UniProtKB
Link-
490PhosphoserineSRVSSPSPE
CCCCCCCCC
26.92HPRD
Link-
490PhosphoserineSRVSSPSPE
CCCCCCCCC
26.92PhosphoELM
Link-
490PhosphoserineSRVSSPSPE
CCCCCCCCC
26.92Phosphositeplus
Link-
490PhosphoserineSRVSSPSPE
CCCCCCCCC
26.92SysPTM
Link-
490Phosphoserine.SRVSSPSPE
CCCCCCCCC
26.92UniProtKB
Link-
492PhosphoserineVSSPSPELG
CCCCCCCCC
32.71HPRD
Link-
492PhosphoserineVSSPSPELG
CCCCCCCCC
32.71PhosphoELM
Link-
492PhosphoserineVSSPSPELG
CCCCCCCCC
32.71Phosphositeplus
Link-
492PhosphoserineVSSPSPELG
CCCCCCCCC
32.71SysPTM
Link-
492Phosphoserine.VSSPSPELG
CCCCCCCCC
32.71UniProtKB
Link-
498PhosphothreonineELGTTPASI
CCCCCCCCC
18.30HPRD
Link-
498PhosphothreonineELGTTPASI
CCCCCCCCC
18.30PhosphoELM
Link-
498PhosphothreonineELGTTPASI
CCCCCCCCC
18.30Phosphositeplus
Link-
498PhosphothreonineELGTTPASI
CCCCCCCCC
18.30SysPTM
Link-
498Phosphothreonine.ELGTTPASI
CCCCCCCCC
18.30UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RSLAA_HUMANENSP00000332834STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures