PSRC1_HUMAN - dbPTM
PSRC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSRC1_HUMAN
UniProt AC Q6PGN9
Protein Name Proline/serine-rich coiled-coil protein 1
Gene Name PSRC1
Organism Homo sapiens (Human).
Sequence Length 363
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytoskeleton, spindle pole. Detected at the mitotic spindle and spindle poles. Diffusely distributed throughout the cell during interphase.
Protein Description Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate, and for normal rate of chromosomal segregation during anaphase. Plays a role in the regulation of mitotic spindle dynamics. Increases the rate of turnover of microtubules on metaphase spindles, and contributes to the generation of normal tension across sister kinetochores. Recruits KIF2A and ANKRD53 to the mitotic spindle and spindle poles. May participate in p53/TP53-regulated growth suppression..
Protein Sequence MEDLEEDVRFIVDETLDFGGLSPSDSREEEDITVLVTPEKPLRRGLSHRSDPNAVAPAPQGVRLSLGPLSPEKLEEILDEANRLAAQLEQCALQDRESAGEGLGPRRVKPSPRRETFVLKDSPVRDLLPTVNSLTRSTPSPSSLTPRLRSNDRKGSVRALRATSGKRPSNMKRESPTCNLFPASKSPASSPLTRSTPPVRGRAGPSGRAAASEETRAAKLRVSGSGEFVGLTLKFLHPSPPGPPTPIRSVLAPQPSTSNSQRLPRPQGAAAKSSSQLPIPSAIPRPASRMPLTSRSVPPGRGALPPDSLSTRKGLPRPSTAGHRVRESGHKVPVSQRLNLPVMGATRSNLQPPRKVAVPGPTR
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
15PhosphorylationVRFIVDETLDFGGLS
HHHHHHCCCCCCCCC		27.4530266825
22PhosphorylationTLDFGGLSPSDSREE
CCCCCCCCCCCCCCC		26.1530266825
24PhosphorylationDFGGLSPSDSREEED
CCCCCCCCCCCCCCC		44.8630266825
26PhosphorylationGGLSPSDSREEEDIT
CCCCCCCCCCCCCEE		46.0230266825
33PhosphorylationSREEEDITVLVTPEK
CCCCCCEEEEECCCC		21.8027690223
37PhosphorylationEDITVLVTPEKPLRR
CCEEEEECCCCCCCC		22.9030266825
42 (in isoform 4)Phosphorylation-9.6230266825
45 (in isoform 4)Phosphorylation-25.7130266825
47PhosphorylationKPLRRGLSHRSDPNA
CCCCCCCCCCCCCCC		21.4821406692
50PhosphorylationRRGLSHRSDPNAVAP
CCCCCCCCCCCCCCC		52.5829496963
65PhosphorylationAPQGVRLSLGPLSPE
CCCCEEEEECCCCHH		22.2529255136
70PhosphorylationRLSLGPLSPEKLEEI
EEEECCCCHHHHHHH		33.8619664994
98PhosphorylationCALQDRESAGEGLGP
HHHHCHHHCCCCCCC		42.3325159151
111PhosphorylationGPRRVKPSPRRETFV
CCCCCCCCCCCCEEE		25.8924719451
116PhosphorylationKPSPRRETFVLKDSP
CCCCCCCEEEECCCC		19.7530266825
122PhosphorylationETFVLKDSPVRDLLP
CEEEECCCCHHHHHH		24.5730266825
130PhosphorylationPVRDLLPTVNSLTRS
CHHHHHHHHHHHHCC		32.0829449344
133PhosphorylationDLLPTVNSLTRSTPS
HHHHHHHHHHCCCCC		27.1229255136
135PhosphorylationLPTVNSLTRSTPSPS
HHHHHHHHCCCCCHH		23.5329255136
137PhosphorylationTVNSLTRSTPSPSSL
HHHHHHCCCCCHHHC		39.1618669648
138PhosphorylationVNSLTRSTPSPSSLT
HHHHHCCCCCHHHCC		25.2125159151
140PhosphorylationSLTRSTPSPSSLTPR
HHHCCCCCHHHCCCC		37.1925159151
142PhosphorylationTRSTPSPSSLTPRLR
HCCCCCHHHCCCCHH		42.1718669648
143PhosphorylationRSTPSPSSLTPRLRS
CCCCCHHHCCCCHHC		39.3829396449
145PhosphorylationTPSPSSLTPRLRSND
CCCHHHCCCCHHCCC		14.3325159151
175PhosphorylationPSNMKRESPTCNLFP
CCCCCCCCCCCCCCC		29.5530266825
177PhosphorylationNMKRESPTCNLFPAS
CCCCCCCCCCCCCCC		24.2530266825
184PhosphorylationTCNLFPASKSPASSP
CCCCCCCCCCCCCCC		33.6326462736
186PhosphorylationNLFPASKSPASSPLT
CCCCCCCCCCCCCCC		24.1725159151
189PhosphorylationPASKSPASSPLTRST
CCCCCCCCCCCCCCC		35.5522199227
190PhosphorylationASKSPASSPLTRSTP
CCCCCCCCCCCCCCC		26.4925159151
193PhosphorylationSPASSPLTRSTPPVR
CCCCCCCCCCCCCCC		26.4229496963
195PhosphorylationASSPLTRSTPPVRGR
CCCCCCCCCCCCCCC		39.7822199227
196PhosphorylationSSPLTRSTPPVRGRA
CCCCCCCCCCCCCCC		28.4622199227
212PhosphorylationPSGRAAASEETRAAK
CCCCCCCCHHHHHHE		31.1019691289
212 (in isoform 2)Phosphorylation-31.1030266825
215 (in isoform 2)Phosphorylation-22.8930266825
215PhosphorylationRAAASEETRAAKLRV
CCCCCHHHHHHEEEE		22.8920068231
223PhosphorylationRAAKLRVSGSGEFVG
HHHEEEECCCCCEEE		22.3229514088
225PhosphorylationAKLRVSGSGEFVGLT
HEEEECCCCCEEEEE		27.8729514088
232PhosphorylationSGEFVGLTLKFLHPS
CCCEEEEEEEECCCC		23.2129514088
239PhosphorylationTLKFLHPSPPGPPTP
EEEECCCCCCCCCCC		32.7426055452
245PhosphorylationPSPPGPPTPIRSVLA
CCCCCCCCCCCCCCC		34.1918669648
248 (in isoform 3)Phosphorylation-23.1624114839
256PhosphorylationSVLAPQPSTSNSQRL
CCCCCCCCCCCCCCC		38.9428555341
258PhosphorylationLAPQPSTSNSQRLPR
CCCCCCCCCCCCCCC		38.5328555341
260PhosphorylationPQPSTSNSQRLPRPQ
CCCCCCCCCCCCCCC		19.2228555341
274PhosphorylationQGAAAKSSSQLPIPS
CCCCCCCCCCCCCCC		22.7728555341
281PhosphorylationSSQLPIPSAIPRPAS
CCCCCCCCCCCCCHH		39.2824719451
286 (in isoform 3)Phosphorylation-29.27-
292 (in isoform 3)Phosphorylation-5.0627732954
294 (in isoform 3)Phosphorylation-30.1827732954
301MethylationSRSVPPGRGALPPDS
CCCCCCCCCCCCCCC		32.74115489531
308PhosphorylationRGALPPDSLSTRKGL
CCCCCCCCCCCCCCC		29.96-
310PhosphorylationALPPDSLSTRKGLPR
CCCCCCCCCCCCCCC		30.07-
311PhosphorylationLPPDSLSTRKGLPRP
CCCCCCCCCCCCCCC		41.51-
346PhosphorylationNLPVMGATRSNLQPP
CCCCCCCCCCCCCCC		28.97-
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 PSRC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PSRC1_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 PSRC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
S10A9_HUMANS100A9physical
22939629
PTMA_HUMANPTMAphysical
22939629
AURKA_HUMANAURKAphysical
22939629
ANM2_HUMANPRMT2physical
26186194
ASB7_HUMANASB7physical
27697924
ANM2_HUMANPRMT2physical
28514442
FUS_HUMANFUSphysical
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 PSRC1_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-65 AND SER-70, 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 SER-137; SER-142; THR-145;SER-186; SER-190; SER-212 AND THR-245, 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-70 AND SER-122, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND THR-245, ANDMASS SPECTROMETRY.

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