SHRM1_HUMAN - dbPTM
SHRM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHRM1_HUMAN
UniProt AC Q2M3G4
Protein Name Protein Shroom1
Gene Name SHROOM1
Organism Homo sapiens (Human).
Sequence Length 852
Subcellular Localization Cytoplasm, cytoskeleton.
Protein Description May be involved in the assembly of microtubule arrays during cell elongation..
Protein Sequence MEALGPGGDRASPASSTSSLDLWHLSMRADSAYSSFSAASGGPEPRTQSPGTDLLPYLDWDYVRVVWGGPGPAPPDAALCTSPRPRPAVAARSGPQPTEVPGTPGPLNRQATPLLYALAAEAEAAAQAAEPPSPPASRAAYRQRLQGAQRRVLRETSFQRKELRMSLPARLRPTVPARPPATHPRSASLSHPGGEGEPARSRAPAPGTAGRGPLANQQRKWCFSEPGKLDRVGRGGGPARECLGEACSSSGLPGPEPLEFQHPALAKFEDHEVGWLPETQPQGSMNLDSGSLKLGDAFRPASRSRSASGEVLGSWGGSGGTIPIVQAVPQGAETPRPLFQTKLSRFLPQKEAAVMYPAELPQSSPADSEQRVSETCIVPAWLPSLPDEVFLEEAPLVRMRSPPDPHASQGPPASVHASDQPYGTGLGQRTGQVTVPTEYPLHECPGTAGADDCWQGVNGSVGISRPTSHTPTGTANDNIPTIDPTGLTTNPPTAAESDLLKPVPADALGLSGNDTPGPSHNTALARGTGQPGSRPTWPSQCLEELVQELARLDPSLCDPLASQPSPEPPLGLLDGLIPLAEVRAAMRPACGEAGEEAASTFEPGSYQFSFTQLLPAPREETRLENPATHPVLDQPCGQGLPAPNNSIQGKKVELAARLQKMLQDLHTEQERLQGEAQAWARRQAALEAAVRQACAPQELERFSRFMADLERVLGLLLLLGSRLARVRRALARAASDSDPDEQASLLQRLRLLQRQEEDAKELKEHVARRERAVREVLVRALPVEELRVYCALLAGKAAVLAQQRNLDERIRLLQDQLDAIRDDLGHHAPSPSPARPPGTCPPVQPPFPLLLT
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
1Acetylation-------MEALGPGG
-------CCCCCCCC		6.4922814378
12PhosphorylationGPGGDRASPASSTSS
CCCCCCCCCCCCCCH		23.1522199227
15PhosphorylationGDRASPASSTSSLDL
CCCCCCCCCCCHHHH		37.2222199227
16PhosphorylationDRASPASSTSSLDLW
CCCCCCCCCCHHHHH		34.1222199227
17PhosphorylationRASPASSTSSLDLWH
CCCCCCCCCHHHHHH		21.6022199227
18PhosphorylationASPASSTSSLDLWHL
CCCCCCCCHHHHHHH		30.7429083192
19PhosphorylationSPASSTSSLDLWHLS
CCCCCCCHHHHHHHH		26.4523186163
26PhosphorylationSLDLWHLSMRADSAY
HHHHHHHHHHCHHHH		8.0424719451
31PhosphorylationHLSMRADSAYSSFSA
HHHHHCHHHHHCHHH		28.2821945579
33PhosphorylationSMRADSAYSSFSAAS
HHHCHHHHHCHHHHH		14.5921945579
34PhosphorylationMRADSAYSSFSAASG
HHCHHHHHCHHHHHC		25.3221945579
35PhosphorylationRADSAYSSFSAASGG
HCHHHHHCHHHHHCC		15.5621945579
37PhosphorylationDSAYSSFSAASGGPE
HHHHHCHHHHHCCCC		25.5221945579
40PhosphorylationYSSFSAASGGPEPRT
HHCHHHHHCCCCCCC		43.9621945579
47PhosphorylationSGGPEPRTQSPGTDL
HCCCCCCCCCCCCCC		44.0826657352
49PhosphorylationGPEPRTQSPGTDLLP
CCCCCCCCCCCCCCC		25.3723898821
52PhosphorylationPRTQSPGTDLLPYLD
CCCCCCCCCCCCCCC		27.1925106551
57PhosphorylationPGTDLLPYLDWDYVR
CCCCCCCCCCCCEEE		19.7723090842
62PhosphorylationLPYLDWDYVRVVWGG
CCCCCCCEEEEEECC		5.9627259358
81PhosphorylationPPDAALCTSPRPRPA
CCCHHHCCCCCCCCC		42.4929978859
82PhosphorylationPDAALCTSPRPRPAV
CCHHHCCCCCCCCCC		20.2226657352
98PhosphorylationARSGPQPTEVPGTPG
CCCCCCCCCCCCCCC		44.3525850435
103PhosphorylationQPTEVPGTPGPLNRQ
CCCCCCCCCCCCCCC		20.9925159151
133PhosphorylationAQAAEPPSPPASRAA
HHHCCCCCCHHHHHH		54.9830278072
137PhosphorylationEPPSPPASRAAYRQR
CCCCCHHHHHHHHHH		28.3830278072
156PhosphorylationQRRVLRETSFQRKEL
HHHHHHHHHCCCHHH		28.5427282143
164MethylationSFQRKELRMSLPARL
HCCCHHHHHCCCCCC		17.46115916965
166PhosphorylationQRKELRMSLPARLRP
CCHHHHHCCCCCCCC		25.4323927012
186PhosphorylationPPATHPRSASLSHPG
CCCCCCCCCCCCCCC		27.0230266825
188PhosphorylationATHPRSASLSHPGGE
CCCCCCCCCCCCCCC		31.4829255136
190PhosphorylationHPRSASLSHPGGEGE
CCCCCCCCCCCCCCC		25.7430266825
202MethylationEGEPARSRAPAPGTA
CCCCCCCCCCCCCCC		38.75115916969
224PhosphorylationQQRKWCFSEPGKLDR
CCCCCCCCCCCCCCC		39.4825159151
228UbiquitinationWCFSEPGKLDRVGRG
CCCCCCCCCCCCCCC		58.9129967540
234MethylationGKLDRVGRGGGPARE
CCCCCCCCCCCCHHH		37.41115916973
240MethylationGRGGGPARECLGEAC
CCCCCCHHHHHHHHH		37.99115916977
248PhosphorylationECLGEACSSSGLPGP
HHHHHHHHCCCCCCC		34.2928348404
249PhosphorylationCLGEACSSSGLPGPE
HHHHHHHCCCCCCCC		28.4528348404
250PhosphorylationLGEACSSSGLPGPEP
HHHHHHCCCCCCCCC		28.2328348404
279PhosphorylationEVGWLPETQPQGSMN
CCCCCCCCCCCCCEE		43.5423186163
284PhosphorylationPETQPQGSMNLDSGS
CCCCCCCCEECCCCC		10.1523186163
289PhosphorylationQGSMNLDSGSLKLGD
CCCEECCCCCEECCC		33.1923186163
291PhosphorylationSMNLDSGSLKLGDAF
CEECCCCCEECCCCC		26.7025159151
302PhosphorylationGDAFRPASRSRSASG
CCCCCCCCCCCCCCC		33.2123312004
304PhosphorylationAFRPASRSRSASGEV
CCCCCCCCCCCCCCE		28.2627282143
306PhosphorylationRPASRSRSASGEVLG
CCCCCCCCCCCCEEE		28.2129116813
308PhosphorylationASRSRSASGEVLGSW
CCCCCCCCCCEEECC		36.4129496963
314PhosphorylationASGEVLGSWGGSGGT
CCCCEEECCCCCCCC		20.5624114839
318PhosphorylationVLGSWGGSGGTIPIV
EEECCCCCCCCCCEE		30.0625002506
321PhosphorylationSWGGSGGTIPIVQAV
CCCCCCCCCCEEEEC		27.4025002506
334PhosphorylationAVPQGAETPRPLFQT
ECCCCCCCCCCHHHH		24.8625002506
344PhosphorylationPLFQTKLSRFLPQKE
CHHHHHHHHHCCCHH		23.6520068231
363PhosphorylationYPAELPQSSPADSEQ
EECCCCCCCCCCCCH		36.0329507054
364PhosphorylationPAELPQSSPADSEQR
ECCCCCCCCCCCCHH		20.8921815630
368PhosphorylationPQSSPADSEQRVSET
CCCCCCCCCHHHCCC		37.4227251275
401PhosphorylationAPLVRMRSPPDPHAS
CCCEECCCCCCCCHH		31.2929496963
515PhosphorylationLGLSGNDTPGPSHNT
HCCCCCCCCCCCCCC		33.8625159151
562PhosphorylationSLCDPLASQPSPEPP
HHCCCCCCCCCCCCC		50.7528348404
565PhosphorylationDPLASQPSPEPPLGL
CCCCCCCCCCCCCCH		33.9728348404
651UbiquitinationNNSIQGKKVELAARL
CCCCCCHHHHHHHHH		48.0029967540
735PhosphorylationRALARAASDSDPDEQ
HHHHHHHCCCCHHHH		36.3429978859
735 (in isoform 2)Phosphorylation-36.34-
737 (in isoform 2)Phosphorylation-48.85-
737PhosphorylationLARAASDSDPDEQAS
HHHHHCCCCHHHHHH		48.8524114839
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 SHRM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHRM1_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 SHRM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SHRM1_HUMAN !!
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 SHRM1_HUMAN

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Related Literatures of Post-Translational Modification
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-166, AND MASSSPECTROMETRY.
"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 THR-103, AND MASSSPECTROMETRY.

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