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PRC1 (human)

Overview PRC1 translocates to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis. Acts as a microtubule-binding and bundling protein both in vivo and vitro. Interacts with the C-terminal Rho-GAP domain and the basic region of MgcRacGAP. The interaction with MgcRacGAP inhibits its GAP activity towards CDC42 in vitro, which may be required for maintaining normal spindle morphology. Interacts separately via its N-terminal region with the C-terminus of CENPE, KIF4A and KIF23 during late mitosis. Note: This description may include information from UniProtKB. Protein type: Cell cycle regulation; Microtubule binding protein; Motility/polarity/chemotaxis; Cytoskeletal protein Cellular Component: microtubule cytoskeleton; spindle pole; spindle microtubule; cytoplasm; nucleolus; plasma membrane; spindle; nucleus Molecular Function: identical protein binding; protein binding; microtubule binding; protein kinase binding Biological Process: mitotic spindle elongation; cytokinesis Reference #:  O43663 (UniProtKB) Alt. Names/Synonyms: anaphase spindle elongation 1 homolog; ASE1; MGC1671; MGC3669; PRC1; protein regulating cytokinesis 1; Protein regulator of cytokinesis 1 Gene Symbols: PRC1 Molecular weight: 71,607 Da Basal Isoelectric point: 6.29  Predict pI for various phosphorylation states CST Pathways:  Histone Methylation Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below PRC1 3NRX - A/B=341-466 (human) 3NRY - A=341-466 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 3NRX 3NRY  |  Phospho3D  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
cell cycle regulation: T470‑p, T481‑p cytoskeletal reorganization: T470‑p, T481‑p intracellular localization: T470‑p molecular association, regulation: S615‑p, T616‑p phosphorylation: S577‑p, T578‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human ► Hide Isoforms
0	2		S4	____MRRSEVLAEES
0	1		S11	SEVLAEESIVCLQkA
0	3		K17-u	ESIVCLQkALNHLRE
0	1		S195-p	LDHTPDTsFERDVVC
0	1		T262-p	EEREAVAtIMsGSKA
0	1		S265-p	EAVAtIMsGSKAKVR
0	1		T379-p	ASDPNRFtNRGGNLL
0	1		K453-a	AKQERQLkNKKQTET
0	57		Y464-p	QTETEMLyGsAPRtP
0	4		S466-p	ETEMLyGsAPRtPsK
4	51		T470-p	LyGsAPRtPsKRRGL
0	1		S472-p	GsAPRtPsKRRGLAP
3	10		T481-p	RRGLAPNtPGKARKL
0	7		Y511-p	PIFGGTVyHsPVsRL
0	35		S513-p	FGGTVyHsPVsRLPP
0	2		S516-p	TVyHsPVsRLPPSGS
0	12		K534-a	AASTCSGkKtPRTGR
0	6		T536-p	STCSGkKtPRTGRHG
1	3		S554-p	ENLELNGsILSGGYP
1	3		S571-p	APLQRNFsINsVAst
1	0		S574-p	QRNFsINsVAstYSE
1	0		S577-p	FsINsVAstYSEFAK
1	0		T578-p	sINsVAstYSEFAKD
0	7		S587-p	SEFAKDPsLsDsstV
0	4		S589-p	FAKDPsLsDsstVGL
0	4		S591-p	KDPsLsDsstVGLQR
0	7		S592-p	DPsLsDsstVGLQRE
0	1		T593-p	PsLsDsstVGLQREL
0	1		K602-u	GLQRELSkASkSDAT
0	1		K605-u	RELSkASkSDATSGI
2	0		S615-p	ATSGILNstNIQs__
2	1		T616-p	TSGILNstNIQs___
0	1		S620-p	LNstNIQs_______

	PRC1 iso2
S4	____MRRSEVLAEES
S11	SEVLAEESIVCLQKA
K17	ESIVCLQKALNHLRE
S195	LDHTPDTSFERDVVC
T262	EEREAVATIMSGSKA
S265	EAVATIMSGSKAKVR
T379	ASDPNRFTNRGGNLL
K423	AKQERQLKNKKQTET
Y434	QTETEMLYGSAPRtP
S436	ETEMLYGSAPRtPSK
T440-p	LYGSAPRtPSKRRGL
S442	GSAPRtPSKRRGLAP
T451	RRGLAPNTPGKARKL
Y481	PIFGGTVYHSPVSRL
S483	FGGTVYHSPVSRLPP
S486	TVYHSPVSRLPPSGS
K504-a	AASTCSGkKtPRTGR
T506-p	STCSGkKtPRTGRHG
S524	ENLELNGSILSGGYP
S541-p	APLQRNFsINSVAST
S544	QRNFsINSVASTYSE
S547	FsINSVASTYSEFAR
T548	sINSVASTYSEFARE
-	gap
-	gap
-	gap
-	gap
-	gap
K558	EFARELSKASKSDAT
K561	RELSKASKSDATSGI
S571	ATSGILNSTNIQS__
T572	TSGILNSTNIQS___
S576	LNSTNIQS_______

	PRC1 iso3
S4	____MRRSEVLAEES
S11	SEVLAEESIVCLQKA
K17	ESIVCLQKALNHLRE
S154	LDHTPDTSFERDVVC
T221	EEREAVATIMSGSKA
S224	EAVATIMSGSKAKVR
T338	ASDPNRFTNRGGNLL
K412	AKQERQLKNKKQTET
Y423	QTETEMLYGSAPRTP
S425	ETEMLYGSAPRTPSK
T429	LYGSAPRTPSKRRGL
S431	GSAPRTPSKRRGLAP
T440	RRGLAPNTPGKARKL
Y470	PIFGGTVYHSPVSRL
S472	FGGTVYHSPVSRLPP
S475	TVYHSPVSRLPPSGS
K493	AASTCSGKKTPRTGR
T495	STCSGKKTPRTGRHG
S513-p	ENLELNGsILSARTF
-	gap
-	gap
-	gap
-	gap
-	gap
-	gap
-	gap
-	gap
-	gap
-	gap
-	gap
-	gap
-	gap
-	gap

	mouse
S4-p	____MRRsEVLADEs
S11-p	sEVLADEsITCLQKA
K17	EsITCLQKALTHLRE
S195	LEHSPDTSFERDVVC
A262	EEREPVEAIMTGSKT
T265	EPVEAIMTGSKTKIR
T379	ASDPGRFTNRGGNLL
K453	AKQERQLKNKKQTEA
Y464	QTEAEMLYGSTPRTP
S466	EAEMLYGSTPRTPSK
T470	LYGSTPRTPSKRPGQ
S472	GSTPRTPSKRPGQTP
T478	PSKRPGQTPKKSGKM
Y508	PVFGGSVYRSPMSRL
S510	FGGSVYRSPMSRLPP
S513	SVYRSPMSRLPPSGS
K531-a	VTSLCSGkKtPRAAQ
T533-p	SLCSGkKtPRAAQLR
S551	ENLDLNGSILSGGYP
S568	TPLQHNCSIKSVAST
S571	QHNCSIKSVASTYSE
S574	CSIKSVASTYSEFSR
T575	SIKSVASTYSEFSRE
-	gap
-	gap
-	gap
-	gap
-	gap
K585	EFSRELSKASRSDAT
R588	RELSKASRSDATSRI
S598	ATSRILNSTNIQS__
T599	TSRILNSTNIQS___
S603	LNSTNIQS_______

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