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Protein

Protein regulator of cytokinesis 1

Gene

PRC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).8 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei377 – 3771Tubulin
Binding sitei387 – 3871Tubulin

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • kinesin binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • cytokinesis Source: UniProtKB
  • microtubule bundle formation Source: InterPro
  • mitotic spindle elongation Source: ProtInc
  • positive regulation of cell proliferation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

ReactomeiR-HSA-5625900. RHO GTPases activate CIT.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein regulator of cytokinesis 1Imported
Gene namesi
Name:PRC1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:9341. PRC1.

Subcellular locationi

GO - Cellular componenti

  • contractile ring Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • microtubule cytoskeleton Source: HPA
  • midbody Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
  • spindle Source: UniProtKB
  • spindle microtubule Source: ProtInc
  • spindle pole Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi470 – 4701T → A: No effect. Abolishes CDK1-mediated phosphorylation, leading to prematurely recruit PLK1 to the spindle during prometaphase and blocking mitotic progression; when associated with A-481. 3 Publications
Mutagenesisi481 – 4811T → A: No effect. Reduces in vitro cyclin E-CDK2 phosphorylation and causes extensive bundling of microtubules to the mitotic spindle; when associated with A-470. 3 Publications
Mutagenesisi577 – 5782ST → AA: Weakly reduces binding to the POLO box domains of PLK1. 1 Publication
Mutagenesisi615 – 6162ST → AA: Impairs binding to the POLO box domains of PLK1, preventing phosphorylation by PLK1 and recruitment of PLK1 to the spindle. 1 Publication

Keywords - Diseasei

Oncogene

Organism-specific databases

PharmGKBiPA33703.

Polymorphism and mutation databases

BioMutaiPRC1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Protein regulator of cytokinesis 1PRO_0000229737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei195 – 1951Phosphoserine1 Publication
Modified residuei265 – 2651Phosphoserine1 Publication
Modified residuei470 – 4701Phosphothreonine; by CDK1Combined sources2 Publications
Modified residuei481 – 4811Phosphothreonine; by CDK1Combined sources2 Publications
Modified residuei501 – 5011Phosphoserine1 Publication
Modified residuei513 – 5131PhosphoserineCombined sources
Modified residuei571 – 5711PhosphoserineCombined sources1 Publication
Modified residuei592 – 5921Phosphoserine1 Publication
Modified residuei615 – 6151Phosphoserine1 Publication
Modified residuei616 – 6161Phosphothreonine; by PLK11 Publication
Isoform 21 Publication (identifier: O43663-2)
Modified residuei541 – 5411PhosphoserineCombined sources
Isoform 4 (identifier: O43663-4)
Modified residuei571 – 5711PhosphoserineCombined sources

Post-translational modificationi

Phosphorylation by CDK1 in early mitosis holds PRC1 in an inactive monomeric state, during the metaphase to anaphase transition, PRC1 is dephosphorylated, promoting interaction with KIF4A, which then translocates PRC1 along mitotic spindles to the plus ends of antiparallel interdigitating microtubules. Dephosphorylation also promotes MT-bundling activity by allowing dimerization. Phosphorylation by CDK1 prevents PLK1-binding: upon degradation of CDK1 at anaphase and dephosphorylation, it is then phosphorylated by PLK1, leading to cytokinesis.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO43663.
MaxQBiO43663.
PaxDbiO43663.
PeptideAtlasiO43663.
PRIDEiO43663.

PTM databases

iPTMnetiO43663.
PhosphoSiteiO43663.

Expressioni

Tissue specificityi

Overexpressed in bladder cancer cells (PubMed:17409436).1 Publication

Gene expression databases

BgeeiENSG00000198901.
CleanExiHS_PRC1.
ExpressionAtlasiO43663. baseline and differential.
GenevisibleiO43663. HS.

Organism-specific databases

HPAiHPA034521.

Interactioni

Subunit structurei

Homodimer (PubMed:20691902). Interacts with the C-terminal Rho-GAP domain and the basic region of RACGAP1 (PubMed:14744859). The interaction with RACGAP1 inhibits its GAP activity towards CDC42 in vitro, which may be required for maintaining normal spindle morphology (PubMed:14744859). Interacts separately via its N-terminal region with the C-terminus of CENPE, KIF4A and KIF23 during late mitosis (PubMed:15297875, PubMed:16431929). Interacts with KIF14 and KIF20A (PubMed:15625105, PubMed:16431929). Interacts with PLK1 (PubMed:19468300). Interacts with KIF20B (PubMed:17409436).7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TRIM37O949723EBI-741137,EBI-741602

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • kinesin binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114517. 29 interactions.
DIPiDIP-34436N.
IntActiO43663. 11 interactions.
MINTiMINT-1459735.
STRINGi9606.ENSP00000377793.

Structurei

Secondary structure

1
620
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2826Combined sources
Helixi33 – 8250Combined sources
Helixi96 – 13540Combined sources
Helixi150 – 18839Combined sources
Helixi195 – 2017Combined sources
Helixi212 – 24938Combined sources
Helixi254 – 26310Combined sources
Helixi271 – 30636Combined sources
Helixi312 – 3165Combined sources
Helixi341 – 3455Combined sources
Helixi347 – 37327Combined sources
Helixi375 – 3784Combined sources
Helixi385 – 41733Combined sources
Beta strandi425 – 4273Combined sources
Helixi428 – 46437Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NRXX-ray1.75A/B341-466[»]
3NRYX-ray2.00A341-466[»]
4L3IX-ray3.60A/B1-486[»]
4L6YX-ray3.30A/B1-486[»]
ProteinModelPortaliO43663.
SMRiO43663. Positions 2-450.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43663.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 341341DimerizationAdd
BLAST
Regioni342 – 466125Spectrin-foldAdd
BLAST
Regioni467 – 620154Unstructured, Arg/Lys richAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili96 – 13338Sequence analysisAdd
BLAST
Coiled coili211 – 30494Sequence analysisAdd
BLAST
Coiled coili383 – 46381Sequence analysisAdd
BLAST

Domaini

Microtubule binding occurs via a basic patch in the central spectrin-like domain and requires also the unstructured C-terminal domain.

Sequence similaritiesi

Belongs to the MAP65/ASE1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4302. Eukaryota.
ENOG410YZBK. LUCA.
GeneTreeiENSGT00390000009453.
HOGENOMiHOG000082534.
HOVERGENiHBG052963.
InParanoidiO43663.
KOiK16732.
OMAiRYGANKE.
OrthoDBiEOG091G0EY7.
PhylomeDBiO43663.
TreeFamiTF323976.

Family and domain databases

InterProiIPR007145. MAP65_Ase1_PRC1.
IPR032921. PRC1.
[Graphical view]
PANTHERiPTHR19321. PTHR19321. 1 hit.
PTHR19321:SF1. PTHR19321:SF1. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: O43663-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRRSEVLAEE SIVCLQKALN HLREIWELIG IPEDQRLQRT EVVKKHIKEL
60 70 80 90 100
LDMMIAEEES LKERLIKSIS VCQKELNTLC SELHVEPFQE EGETTILQLE
110 120 130 140 150
KDLRTQVELM RKQKKERKQE LKLLQEQDQE LCEILCMPHY DIDSASVPSL
160 170 180 190 200
EELNQFRQHV TTLRETKASR REEFVSIKRQ IILCMEALDH TPDTSFERDV
210 220 230 240 250
VCEDEDAFCL SLENIATLQK LLRQLEMQKS QNEAVCEGLR TQIRELWDRL
260 270 280 290 300
QIPEEEREAV ATIMSGSKAK VRKALQLEVD RLEELKMQNM KKVIEAIRVE
310 320 330 340 350
LVQYWDQCFY SQEQRQAFAP FCAEDYTESL LQLHDAEIVR LKNYYEVHKE
360 370 380 390 400
LFEGVQKWEE TWRLFLEFER KASDPNRFTN RGGNLLKEEK QRAKLQKMLP
410 420 430 440 450
KLEEELKARI ELWEQEHSKA FMVNGQKFME YVAEQWEMHR LEKERAKQER
460 470 480 490 500
QLKNKKQTET EMLYGSAPRT PSKRRGLAPN TPGKARKLNT TTMSNATANS
510 520 530 540 550
SIRPIFGGTV YHSPVSRLPP SGSKPVAAST CSGKKTPRTG RHGANKENLE
560 570 580 590 600
LNGSILSGGY PGSAPLQRNF SINSVASTYS EFAKDPSLSD SSTVGLQREL
610 620
SKASKSDATS GILNSTNIQS
Length:620
Mass (Da):71,607
Last modified:November 25, 2008 - v2
Checksum:i28393C5B1B3662F3
GO
Isoform 21 Publication (identifier: O43663-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     397-426: Missing.
     584-597: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:576
Mass (Da):66,596
Checksum:i99DFC0F36E2BC312
GO
Isoform 3 (identifier: O43663-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     50-90: Missing.
     558-620: GGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQRELSKASKSDATSGILNSTNIQS → ARTFKGFQI

Note: No experimental confirmation available.
Show »
Length:525
Mass (Da):61,388
Checksum:i609991EF3214602F
GO
Isoform 4 (identifier: O43663-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     584-597: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:606
Mass (Da):70,191
Checksum:iFED638FB918F6A35
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti416 – 4161E → G in BX647317 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti187 – 1871A → E.3 Publications
Corresponds to variant rs7172758 [ dbSNP | Ensembl ].
VAR_047768
Natural varianti511 – 5111Y → C.
Corresponds to variant rs12911192 [ dbSNP | Ensembl ].
VAR_047769

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei50 – 9041Missing in isoform 3. 1 PublicationVSP_035875Add
BLAST
Alternative sequencei397 – 42630Missing in isoform 2. 1 PublicationVSP_051979Add
BLAST
Alternative sequencei558 – 62063GGYPG…TNIQS → ARTFKGFQI in isoform 3. 1 PublicationVSP_035876Add
BLAST
Alternative sequencei584 – 59714Missing in isoform 2 and isoform 4. 2 PublicationsVSP_051980Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044588 mRNA. Translation: AAC02688.1.
AK297117 mRNA. Translation: BAG59623.1.
AC068831 Genomic DNA. No translation available.
BC003138 mRNA. Translation: AAH03138.1.
BC005140 mRNA. Translation: AAH05140.1.
BX647317 mRNA. No translation available.
CCDSiCCDS32334.1. [O43663-1]
CCDS45352.1. [O43663-4]
CCDS45353.2. [O43663-3]
RefSeqiNP_001254509.1. NM_001267580.1.
NP_003972.1. NM_003981.3.
UniGeneiHs.366401.

Genome annotation databases

EnsembliENST00000361188; ENSP00000354679; ENSG00000198901. [O43663-4]
ENST00000394249; ENSP00000377793; ENSG00000198901. [O43663-1]
ENST00000442656; ENSP00000409549; ENSG00000198901. [O43663-3]
GeneIDi9055.
KEGGihsa:9055.
UCSCiuc002bqm.5. human. [O43663-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF044588 mRNA. Translation: AAC02688.1.
AK297117 mRNA. Translation: BAG59623.1.
AC068831 Genomic DNA. No translation available.
BC003138 mRNA. Translation: AAH03138.1.
BC005140 mRNA. Translation: AAH05140.1.
BX647317 mRNA. No translation available.
CCDSiCCDS32334.1. [O43663-1]
CCDS45352.1. [O43663-4]
CCDS45353.2. [O43663-3]
RefSeqiNP_001254509.1. NM_001267580.1.
NP_003972.1. NM_003981.3.
UniGeneiHs.366401.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NRXX-ray1.75A/B341-466[»]
3NRYX-ray2.00A341-466[»]
4L3IX-ray3.60A/B1-486[»]
4L6YX-ray3.30A/B1-486[»]
ProteinModelPortaliO43663.
SMRiO43663. Positions 2-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114517. 29 interactions.
DIPiDIP-34436N.
IntActiO43663. 11 interactions.
MINTiMINT-1459735.
STRINGi9606.ENSP00000377793.

PTM databases

iPTMnetiO43663.
PhosphoSiteiO43663.

Polymorphism and mutation databases

BioMutaiPRC1.

Proteomic databases

EPDiO43663.
MaxQBiO43663.
PaxDbiO43663.
PeptideAtlasiO43663.
PRIDEiO43663.

Protocols and materials databases

DNASUi9055.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361188; ENSP00000354679; ENSG00000198901. [O43663-4]
ENST00000394249; ENSP00000377793; ENSG00000198901. [O43663-1]
ENST00000442656; ENSP00000409549; ENSG00000198901. [O43663-3]
GeneIDi9055.
KEGGihsa:9055.
UCSCiuc002bqm.5. human. [O43663-1]

Organism-specific databases

CTDi9055.
GeneCardsiPRC1.
HGNCiHGNC:9341. PRC1.
HPAiHPA034521.
MIMi603484. gene.
neXtProtiNX_O43663.
PharmGKBiPA33703.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4302. Eukaryota.
ENOG410YZBK. LUCA.
GeneTreeiENSGT00390000009453.
HOGENOMiHOG000082534.
HOVERGENiHBG052963.
InParanoidiO43663.
KOiK16732.
OMAiRYGANKE.
OrthoDBiEOG091G0EY7.
PhylomeDBiO43663.
TreeFamiTF323976.

Enzyme and pathway databases

ReactomeiR-HSA-5625900. RHO GTPases activate CIT.

Miscellaneous databases

ChiTaRSiPRC1. human.
EvolutionaryTraceiO43663.
GeneWikiiPRC1.
GenomeRNAii9055.
PROiO43663.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000198901.
CleanExiHS_PRC1.
ExpressionAtlasiO43663. baseline and differential.
GenevisibleiO43663. HS.

Family and domain databases

InterProiIPR007145. MAP65_Ase1_PRC1.
IPR032921. PRC1.
[Graphical view]
PANTHERiPTHR19321. PTHR19321. 1 hit.
PTHR19321:SF1. PTHR19321:SF1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPRC1_HUMAN
AccessioniPrimary (citable) accession number: O43663
Secondary accession number(s): A6NC44
, B4DLR1, H9KV59, Q9BSB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 25, 2008
Last modified: September 7, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.