dbPTM

PRC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRC1_HUMAN
UniProt AC	O43663
Protein Name	Protein regulator of cytokinesis 1 {ECO:0000312\|HGNC:HGNC:9341}
Gene Name	PRC1 {ECO:0000312\|HGNC:HGNC:9341}
Organism	Homo sapiens (Human).
Sequence Length	620
Subcellular Localization	Nucleus . Cytoplasm. Cytoplasm, cytoskeleton, spindle pole. Midbody . Colocalized with KIF20B in the nucleus of bladder carcinoma cells at the interphase. Colocalized with KIF20B in bladder carcinoma cells at prophase, metaphase, early anaphase, at t
Protein Description	Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression. [PubMed: 17409436]
Protein Sequence	MRRSEVLAEESIVCLQKALNHLREIWELIGIPEDQRLQRTEVVKKHIKELLDMMIAEEESLKERLIKSISVCQKELNTLCSELHVEPFQEEGETTILQLEKDLRTQVELMRKQKKERKQELKLLQEQDQELCEILCMPHYDIDSASVPSLEELNQFRQHVTTLRETKASRREEFVSIKRQIILCMEALDHTPDTSFERDVVCEDEDAFCLSLENIATLQKLLRQLEMQKSQNEAVCEGLRTQIRELWDRLQIPEEEREAVATIMSGSKAKVRKALQLEVDRLEELKMQNMKKVIEAIRVELVQYWDQCFYSQEQRQAFAPFCAEDYTESLLQLHDAEIVRLKNYYEVHKELFEGVQKWEETWRLFLEFERKASDPNRFTNRGGNLLKEEKQRAKLQKMLPKLEEELKARIELWEQEHSKAFMVNGQKFMEYVAEQWEMHRLEKERAKQERQLKNKKQTETEMLYGSAPRTPSKRRGLAPNTPGKARKLNTTTMSNATANSSIRPIFGGTVYHSPVSRLPPSGSKPVAASTCSGKKTPRTGRHGANKENLELNGSILSGGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQRELSKASKSDATSGILNSTNIQS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MRRSEVLAEES ----CCHHHHHHHHH	22.99	25159151
11	Phosphorylation	SEVLAEESIVCLQKA HHHHHHHHHHHHHHH	16.30	28985074
17	Ubiquitination	ESIVCLQKALNHLRE HHHHHHHHHHHHHHH	41.72	-
17	Acetylation	ESIVCLQKALNHLRE HHHHHHHHHHHHHHH	41.72	26051181
67	Ubiquitination	SLKERLIKSISVCQK HHHHHHHHHHHHHHH	46.45	-
70	Phosphorylation	ERLIKSISVCQKELN HHHHHHHHHHHHHHH	24.75	27251275
74	Ubiquitination	KSISVCQKELNTLCS HHHHHHHHHHHHHHH	60.07	-
101	Ubiquitination	TTILQLEKDLRTQVE EEEEHHHHHHHHHHH	71.32	-
105	Phosphorylation	QLEKDLRTQVELMRK HHHHHHHHHHHHHHH	44.24	22468782
111	Methylation	RTQVELMRKQKKERK HHHHHHHHHHHHHHH	51.37	115488669
178	Ubiquitination	REEFVSIKRQIILCM HHHHHHHHHHHHHHH	30.64	-
191	Phosphorylation	CMEALDHTPDTSFER HHHHHCCCCCCCCCC	23.64	17081983
194	Phosphorylation	ALDHTPDTSFERDVV HHCCCCCCCCCCCEE	36.20	23663014
195	Phosphorylation	LDHTPDTSFERDVVC HCCCCCCCCCCCEEC	32.27	23663014
229	Ubiquitination	LRQLEMQKSQNEAVC HHHHHHHHHHHHHHH	53.34	-
249	Methylation	QIRELWDRLQIPEEE HHHHHHHHCCCCHHH	19.53	115488663
262	Phosphorylation	EEREAVATIMSGSKA HHHHHHHHHHHCCHH	15.60	29978859
265	Phosphorylation	EAVATIMSGSKAKVR HHHHHHHHCCHHHHH	35.74	25159151
267	Phosphorylation	VATIMSGSKAKVRKA HHHHHHCCHHHHHHH	23.33	25159151
268	Ubiquitination	ATIMSGSKAKVRKAL HHHHHCCHHHHHHHH	56.61	-
273	Ubiquitination	GSKAKVRKALQLEVD CCHHHHHHHHHCHHH	57.34	-
281	Methylation	ALQLEVDRLEELKMQ HHHCHHHHHHHHHHH	49.53	115488657
286	Ubiquitination	VDRLEELKMQNMKKV HHHHHHHHHHHHHHH	41.54	-
326	Phosphorylation	APFCAEDYTESLLQL CHHHHCHHHHHHHHH	12.15	28102081
327	Phosphorylation	PFCAEDYTESLLQLH HHHHCHHHHHHHHHC	31.27	28348404
329	Phosphorylation	CAEDYTESLLQLHDA HHCHHHHHHHHHCCH	26.95	28348404
349	Ubiquitination	KNYYEVHKELFEGVQ CCHHHHHHHHHHHHH	62.38	-
379	Phosphorylation	ASDPNRFTNRGGNLL CCCCCCCCCCCCCHH	22.29	-
387	Sumoylation	NRGGNLLKEEKQRAK CCCCCHHHHHHHHHH	67.98	-
387	Sumoylation	NRGGNLLKEEKQRAK CCCCCHHHHHHHHHH	67.98	-
387	Ubiquitination	NRGGNLLKEEKQRAK CCCCCHHHHHHHHHH	67.98	-
387	Acetylation	NRGGNLLKEEKQRAK CCCCCHHHHHHHHHH	67.98	25953088
390	Ubiquitination	GNLLKEEKQRAKLQK CCHHHHHHHHHHHHH	46.29	-
401	Sumoylation	KLQKMLPKLEEELKA HHHHHHHHHHHHHHH	65.65	-
401	Sumoylation	KLQKMLPKLEEELKA HHHHHHHHHHHHHHH	65.65	-
401	Ubiquitination	KLQKMLPKLEEELKA HHHHHHHHHHHHHHH	65.65	-
407	Acetylation	PKLEEELKARIELWE HHHHHHHHHHHHHHH	38.61	26051181
419	Ubiquitination	LWEQEHSKAFMVNGQ HHHHHHHHHEEECHH	47.77	-
419	Acetylation	LWEQEHSKAFMVNGQ HHHHHHHHHEEECHH	47.77	26051181
453	Acetylation	AKQERQLKNKKQTET HHHHHHHHHHHHHHH	59.38	12656465
456	Ubiquitination	ERQLKNKKQTETEML HHHHHHHHHHHHHHH	72.37	-
458	Phosphorylation	QLKNKKQTETEMLYG HHHHHHHHHHHHHHC	54.47	23403867
460	Phosphorylation	KNKKQTETEMLYGSA HHHHHHHHHHHHCCC	30.04	21945579
464	Phosphorylation	QTETEMLYGSAPRTP HHHHHHHHCCCCCCC	14.02	21945579
466	Phosphorylation	ETEMLYGSAPRTPSK HHHHHHCCCCCCCCC	22.88	21945579
470	Phosphorylation	LYGSAPRTPSKRRGL HHCCCCCCCCCCCCC	30.75	23401153
472	Phosphorylation	GSAPRTPSKRRGLAP CCCCCCCCCCCCCCC	37.88	25159151
475	Methylation	PRTPSKRRGLAPNTP CCCCCCCCCCCCCCC	48.49	81471811
481	Phosphorylation	RRGLAPNTPGKARKL CCCCCCCCCCCCCCC	32.15	29255136
484	Ubiquitination	LAPNTPGKARKLNTT CCCCCCCCCCCCCCC	46.34	-
484	Acetylation	LAPNTPGKARKLNTT CCCCCCCCCCCCCCC	46.34	25953088
487	Ubiquitination	NTPGKARKLNTTTMS CCCCCCCCCCCCCCC	51.45	-
490	Phosphorylation	GKARKLNTTTMSNAT CCCCCCCCCCCCCCC	33.80	24732914
491	Phosphorylation	KARKLNTTTMSNATA CCCCCCCCCCCCCCC	21.30	24732914
492	Phosphorylation	ARKLNTTTMSNATAN CCCCCCCCCCCCCCC	19.30	24732914
494	Phosphorylation	KLNTTTMSNATANSS CCCCCCCCCCCCCCC	22.63	24732914
497	Phosphorylation	TTTMSNATANSSIRP CCCCCCCCCCCCCCC	30.53	24732914
500	Phosphorylation	MSNATANSSIRPIFG CCCCCCCCCCCCCCC	25.36	24732914
501	Phosphorylation	SNATANSSIRPIFGG CCCCCCCCCCCCCCC	23.56	9885575
509	Phosphorylation	IRPIFGGTVYHSPVS CCCCCCCEEEECCCC	20.47	23927012
511	Phosphorylation	PIFGGTVYHSPVSRL CCCCCEEEECCCCCC	9.09	23927012
513	Phosphorylation	FGGTVYHSPVSRLPP CCCEEEECCCCCCCC	14.87	25159151
513 (in isoform 3)	Phosphorylation	-	14.87	25849741
516	Phosphorylation	TVYHSPVSRLPPSGS EEEECCCCCCCCCCC	31.33	23927012
516 (in isoform 3)	Phosphorylation	-	31.33	19691289
521	Phosphorylation	PVSRLPPSGSKPVAA CCCCCCCCCCCCCEE	54.48	27732954
523	Phosphorylation	SRLPPSGSKPVAAST CCCCCCCCCCCEEEC	37.82	28985074
524	Ubiquitination	RLPPSGSKPVAASTC CCCCCCCCCCEEECC	47.22	-
524	Acetylation	RLPPSGSKPVAASTC CCCCCCCCCCEEECC	47.22	26051181
529	Phosphorylation	GSKPVAASTCSGKKT CCCCCEEECCCCCCC	21.87	30576142
530	Phosphorylation	SKPVAASTCSGKKTP CCCCEEECCCCCCCC	13.13	30576142
532	Phosphorylation	PVAASTCSGKKTPRT CCEEECCCCCCCCCC	54.45	30576142
534	Acetylation	AASTCSGKKTPRTGR EEECCCCCCCCCCCC	36.86	25953088
536	Phosphorylation	STCSGKKTPRTGRHG ECCCCCCCCCCCCCC	22.84	30576142
539	Phosphorylation	SGKKTPRTGRHGANK CCCCCCCCCCCCCCH	39.51	22468782
541 (in isoform 2)	Phosphorylation	-	25.18	22617229
544 (in isoform 2)	Phosphorylation	-	20.14	27050516
547 (in isoform 2)	Phosphorylation	-	67.84	20068231
548 (in isoform 2)	Phosphorylation	-	40.19	20068231
549 (in isoform 2)	Phosphorylation	-	9.21	20068231
550 (in isoform 2)	Phosphorylation	-	52.34	20068231
554	Phosphorylation	ENLELNGSILSGGYP HCEEECCEECCCCCC	21.20	25159151
557	Phosphorylation	ELNGSILSGGYPGSA EECCEECCCCCCCCC	28.62	25159151
558 (in isoform 2)	Ubiquitination	-	35.89	21906983
560	Phosphorylation	GSILSGGYPGSAPLQ CEECCCCCCCCCCCC	14.14	20068231
561 (in isoform 2)	Ubiquitination	-	33.27	21906983
563	Phosphorylation	LSGGYPGSAPLQRNF CCCCCCCCCCCCCCC	23.39	20068231
571	Phosphorylation	APLQRNFSINSVAST CCCCCCCCHHHHHHH	25.14	26055452
571 (in isoform 4)	Phosphorylation	-	25.14	22617229
574	Phosphorylation	QRNFSINSVASTYSE CCCCCHHHHHHHHHH	19.86	20068231
574 (in isoform 4)	Phosphorylation	-	19.86	27050516
577	Phosphorylation	FSINSVASTYSEFAK CCHHHHHHHHHHHHC	26.23	20068231
577 (in isoform 4)	Phosphorylation	-	26.23	20068231
578	Phosphorylation	SINSVASTYSEFAKD CHHHHHHHHHHHHCC	22.71	20068231
578 (in isoform 4)	Phosphorylation	-	22.71	20068231
579	Phosphorylation	INSVASTYSEFAKDP HHHHHHHHHHHHCCC	12.05	20068231
579 (in isoform 4)	Phosphorylation	-	12.05	20068231
580	Phosphorylation	NSVASTYSEFAKDPS HHHHHHHHHHHCCCC	26.73	20068231
580 (in isoform 4)	Phosphorylation	-	26.73	20068231
587	Phosphorylation	SEFAKDPSLSDSSTV HHHHCCCCCCCCCHH	51.11	19691289
588	Ubiquitination	EFAKDPSLSDSSTVG HHHCCCCCCCCCHHH	8.85	21906983
589	Phosphorylation	FAKDPSLSDSSTVGL HHCCCCCCCCCHHHH	39.52	19691289
591	Phosphorylation	KDPSLSDSSTVGLQR CCCCCCCCCHHHHHH	25.24	19691289
591	Ubiquitination	KDPSLSDSSTVGLQR CCCCCCCCCHHHHHH	25.24	21906983
592	Phosphorylation	DPSLSDSSTVGLQRE CCCCCCCCHHHHHHH	31.91	25159151
593	Phosphorylation	PSLSDSSTVGLQREL CCCCCCCHHHHHHHH	23.65	19691289
601	Phosphorylation	VGLQRELSKASKSDA HHHHHHHHHHCCHHH	22.79	18691976
602	Ubiquitination	GLQRELSKASKSDAT HHHHHHHHHCCHHHC	70.11	21906983
602 (in isoform 1)	Ubiquitination	-	70.11	21906983
605	Ubiquitination	RELSKASKSDATSGI HHHHHHCCHHHCCCC	58.16	21906983
605 (in isoform 1)	Ubiquitination	-	58.16	21906983
606	Phosphorylation	ELSKASKSDATSGIL HHHHHCCHHHCCCCC	29.95	24732914
609	Phosphorylation	KASKSDATSGILNST HHCCHHHCCCCCCCC	32.26	20860994
610	Phosphorylation	ASKSDATSGILNSTN HCCHHHCCCCCCCCC	26.09	24732914
615	Phosphorylation	ATSGILNSTNIQS-- HCCCCCCCCCCCC--	21.27	25159151
616	Phosphorylation	TSGILNSTNIQS--- CCCCCCCCCCCC---	34.96	25159151
620	Phosphorylation	LNSTNIQS------- CCCCCCCC-------	38.09	25159151

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
470	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
470	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
481	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
481	T	Phosphorylation	Kinase	CDK16	Q00536	PSP
481	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
615	S	Phosphorylation	Kinase	PLK1	P53350	PSP
616	T	Phosphorylation	Kinase	PLK1	P53350	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PRC1_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 PRC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
USBP1_HUMAN	USHBP1	physical	16189514
K1C20_HUMAN	KRT20	physical	16189514
CC85B_HUMAN	CCDC85B	physical	16189514
KIF4A_HUMAN	KIF4A	physical	15297875
KIF23_HUMAN	KIF23	physical	15297875
CENPE_HUMAN	CENPE	physical	15297875
TACC2_HUMAN	TACC2	physical	22939629
USBP1_HUMAN	USHBP1	physical	19447967
TRI37_HUMAN	TRIM37	physical	19447967
ACSM1_HUMAN	ACSM1	physical	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 PRC1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615 AND THR-616, ANDMASS SPECTROMETRY.	19369195 [Abstract]
"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-571, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-481 AND SER-513, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265; SER-501 ANDSER-513, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195 AND SER-592, ANDMASS SPECTROMETRY.	16565220 [Abstract]
"Choice of Plk1 docking partners during mitosis and cytokinesis iscontrolled by the activation state of Cdk1."; Neef R., Gruneberg U., Kopajtich R., Li X., Nigg E.A., Sillje H.,Barr F.A.; Nat. Cell Biol. 9:436-444(2007). Cited for: PHOSPHORYLATION AT THR-470; THR-481 AND THR-616, SUBCELLULAR LOCATION,AND MUTAGENESIS OF THR-470; THR-481; 577-SER-THR-578 AND615-SER-THR-616.	17351640 [Abstract]
"Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1oligomerization and proper central spindle organization."; Fu C., Yan F., Wu F., Wu Q., Whittaker J., Hu H., Hu R., Yao X.; Cell Res. 17:449-457(2007). Cited for: PHOSPHORYLATION AT THR-470 AND THR-481.	17438553 [Abstract]
"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 THR-481, AND MASSSPECTROMETRY.	16964243 [Abstract]
"PRC1: a human mitotic spindle-associated CDK substrate proteinrequired for cytokinesis."; Jiang W., Jimenez G., Wells N.J., Hope T.J., Wahl G.M., Hunter T.,Fukunaga R.; Mol. Cell 2:877-885(1998). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OFTHR-470 AND THR-481, SUBCELLULAR LOCATION, PHOSPHORYLATION, ANDVARIANT GLU-187.	9885575 [Abstract]