SPS2L_HUMAN - dbPTM
SPS2L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPS2L_HUMAN
UniProt AC Q9NUQ6
Protein Name SPATS2-like protein
Gene Name SPATS2L
Organism Homo sapiens (Human).
Sequence Length 558
Subcellular Localization Cytoplasm . Nucleus, nucleolus . During oxidative stress as well as UV irradiation, energy deprivation or heat shock, relocalizes to cytoplasmic stress granules. In the nucleus, found in structures lacking NPM1.
Protein Description
Protein Sequence MAELNTHVNVKEKIYAVRSVVPNKSNNEIVLVLQQFDFNVDKAVQAFVDGSAIQVLKEWNMTGKKKNNKRKRSKSKQHQGNKDAKDKVERPEAGPLQPQPPQIQNGPMNGCEKDSSSTDSANEKPALIPREKKISILEEPSKALRGVTEGNRLLQQKLSLDGNPKPIHGTTERSDGLQWSAEQPCNPSKPKAKTSPVKSNTPAAHLEIKPDELAKKRGPNIEKSVKDLQRCTVSLTRYRVMIKEEVDSSVKKIKAAFAELHNCIIDKEVSLMAEMDKVKEEAMEILTARQKKAEELKRLTDLASQMAEMQLAELRAEIKHFVSERKYDEELGKAARFSCDIEQLKAQIMLCGEITHPKNNYSSRTPCSSLLPLLNAHAATSGKQSNFSRKSSTHNKPSEGKAANPKMVSSLPSTADPSHQTMPANKQNGSSNQRRRFNPQYHNNRLNGPAKSQGSGNEAEPLGKGNSRHEHRRQPHNGFRPKNKGGAKNQEASLGMKTPEAPAHSEKPRRRQHAADTSEARPFRGSVGRVSQCNLCPTRIEVSTDAAVLSVPAVTLVA
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------MAELNTHVN
------CCCCCCCCC		29.9519413330
7 (in isoform 3)Phosphorylation-14.2122210691
8 (in isoform 3)Phosphorylation-9.1922210691
9 (in isoform 3)Phosphorylation-31.3822210691
15PhosphorylationVNVKEKIYAVRSVVP
CCHHHHEEEEEEECC		15.3128152594
51PhosphorylationVQAFVDGSAIQVLKE
HHHHHCCHHHHHHHH		20.1027251275
115PhosphorylationMNGCEKDSSSTDSAN
CCCCCCCCCCCCCCC		36.9423927012
116PhosphorylationNGCEKDSSSTDSANE
CCCCCCCCCCCCCCC		47.6030266825
117PhosphorylationGCEKDSSSTDSANEK
CCCCCCCCCCCCCCC		39.9430266825
118PhosphorylationCEKDSSSTDSANEKP
CCCCCCCCCCCCCCC		35.6030266825
120PhosphorylationKDSSSTDSANEKPAL
CCCCCCCCCCCCCCC		32.8430266825
135PhosphorylationIPREKKISILEEPSK
CCHHHHEECCCCHHH		29.9623911959
141PhosphorylationISILEEPSKALRGVT
EECCCCHHHHHCCCH		33.5620068231
148 (in isoform 2)Phosphorylation-40.7929978859
148PhosphorylationSKALRGVTEGNRLLQ
HHHHCCCHHHHHHHH		40.7920068231
155 (in isoform 2)Phosphorylation-42.8429978859
159PhosphorylationRLLQQKLSLDGNPKP
HHHHHHCCCCCCCCC		31.3022617229
170PhosphorylationNPKPIHGTTERSDGL
CCCCCCCCCCCCCCC		16.0127080861
171PhosphorylationPKPIHGTTERSDGLQ
CCCCCCCCCCCCCCC		33.7127080861
189MalonylationEQPCNPSKPKAKTSP
CCCCCCCCCCCCCCC		52.3626320211
194PhosphorylationPSKPKAKTSPVKSNT
CCCCCCCCCCCCCCC		43.0226657352
195PhosphorylationSKPKAKTSPVKSNTP
CCCCCCCCCCCCCCC		27.3025849741
199PhosphorylationAKTSPVKSNTPAAHL
CCCCCCCCCCCCCEE		46.2823927012
201PhosphorylationTSPVKSNTPAAHLEI
CCCCCCCCCCCEEEE		22.7723927012
234PhosphorylationDLQRCTVSLTRYRVM
HHHHHHEEEEEEEEE		13.0824719451
279UbiquitinationMAEMDKVKEEAMEIL
HHHHHHHHHHHHHHH		56.42-
2792-HydroxyisobutyrylationMAEMDKVKEEAMEIL
HHHHHHHHHHHHHHH		56.42-
300PhosphorylationAEELKRLTDLASQMA
HHHHHHHHHHHHHHH		32.7622210691
304PhosphorylationKRLTDLASQMAEMQL
HHHHHHHHHHHHHHH		27.9922210691
319AcetylationAELRAEIKHFVSERK
HHHHHHHHHHHHHHH		23.6126051181
319UbiquitinationAELRAEIKHFVSERK
HHHHHHHHHHHHHHH		23.61-
333AcetylationKYDEELGKAARFSCD
HCHHHHHHHHHHCCC		52.0426051181
333UbiquitinationKYDEELGKAARFSCD
HCHHHHHHHHHHCCC		52.04-
338PhosphorylationLGKAARFSCDIEQLK
HHHHHHHCCCHHHHH		12.8230266825
345MethylationSCDIEQLKAQIMLCG
CCCHHHHHHHHHHHH		37.6323644510
353MethylationAQIMLCGEITHPKNN
HHHHHHHCCCCCCCC		43.66-
361PhosphorylationITHPKNNYSSRTPCS
CCCCCCCCCCCCCHH		19.8821712546
362PhosphorylationTHPKNNYSSRTPCSS
CCCCCCCCCCCCHHH		18.5725159151
363PhosphorylationHPKNNYSSRTPCSSL
CCCCCCCCCCCHHHH		29.7925627689
365PhosphorylationKNNYSSRTPCSSLLP
CCCCCCCCCHHHHHH		30.5126657352
368PhosphorylationYSSRTPCSSLLPLLN
CCCCCCHHHHHHHHH		25.8127251275
369PhosphorylationSSRTPCSSLLPLLNA
CCCCCHHHHHHHHHH		40.4125394399
380PhosphorylationLLNAHAATSGKQSNF
HHHHHHHCCCCCCCC		38.5020860994
381PhosphorylationLNAHAATSGKQSNFS
HHHHHHCCCCCCCCC		38.9925159151
385PhosphorylationAATSGKQSNFSRKSS
HHCCCCCCCCCCCCC		43.2422798277
391PhosphorylationQSNFSRKSSTHNKPS
CCCCCCCCCCCCCCC		39.0826657352
392PhosphorylationSNFSRKSSTHNKPSE
CCCCCCCCCCCCCCC		36.4026657352
393PhosphorylationNFSRKSSTHNKPSEG
CCCCCCCCCCCCCCC		36.2424275569
398PhosphorylationSSTHNKPSEGKAANP
CCCCCCCCCCCCCCH		61.6724275569
409PhosphorylationAANPKMVSSLPSTAD
CCCHHHHHCCCCCCC		23.7418767875
410PhosphorylationANPKMVSSLPSTADP
CCHHHHHCCCCCCCC		32.6523312004
413PhosphorylationKMVSSLPSTADPSHQ
HHHHCCCCCCCCCCC		41.3328857561
414PhosphorylationMVSSLPSTADPSHQT
HHHCCCCCCCCCCCC		32.8923312004
418PhosphorylationLPSTADPSHQTMPAN
CCCCCCCCCCCCCCC		28.8628857561
421PhosphorylationTADPSHQTMPANKQN
CCCCCCCCCCCCCCC		21.5023312004
430PhosphorylationPANKQNGSSNQRRRF
CCCCCCCCCHHHHCC		33.3920860994
431PhosphorylationANKQNGSSNQRRRFN
CCCCCCCCHHHHCCC		38.0820860994
441PhosphorylationRRRFNPQYHNNRLNG
HHCCCHHHCCCCCCC		14.05-
451MethylationNRLNGPAKSQGSGNE
CCCCCCCCCCCCCCC		46.58-
451UbiquitinationNRLNGPAKSQGSGNE
CCCCCCCCCCCCCCC		46.58-
452PhosphorylationRLNGPAKSQGSGNEA
CCCCCCCCCCCCCCC		41.7129255136
455PhosphorylationGPAKSQGSGNEAEPL
CCCCCCCCCCCCCCC		30.7029255136
464MethylationNEAEPLGKGNSRHEH
CCCCCCCCCCCCCCC		63.70-
467PhosphorylationEPLGKGNSRHEHRRQ
CCCCCCCCCCCCCCC		43.6228857561
493PhosphorylationGAKNQEASLGMKTPE
CCCCHHHCCCCCCCC		25.3825850435
498PhosphorylationEASLGMKTPEAPAHS
HHCCCCCCCCCCCCC		19.9125159151
505PhosphorylationTPEAPAHSEKPRRRQ
CCCCCCCCCCCCHHH		49.8028555341
507AcetylationEAPAHSEKPRRRQHA
CCCCCCCCCCHHHHC		47.0026051181
517PhosphorylationRRQHAADTSEARPFR
HHHHCCCCCCCCCCC		24.6023403867
518PhosphorylationRQHAADTSEARPFRG
HHHCCCCCCCCCCCC		29.7923403867
524MethylationTSEARPFRGSVGRVS
CCCCCCCCCCCCCHH		38.88-
526PhosphorylationEARPFRGSVGRVSQC
CCCCCCCCCCCHHCC		19.6921955146
531PhosphorylationRGSVGRVSQCNLCPT
CCCCCCHHCCCCCCC		27.8822617229
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 SPS2L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPS2L_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 SPS2L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUX1_HUMANCUX1physical
26496610
CASP_HUMANCUX1physical
26496610
RPGF1_HUMANRAPGEF1physical
26496610
SET_HUMANSETphysical
26496610
PLXA3_HUMANPLXNA3physical
26496610
USMG5_HUMANUSMG5physical
26496610
SGO2_HUMANSGOL2physical
26496610
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 SPS2L_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-120, AND MASSSPECTROMETRY.

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