O43663 · PRC1_HUMAN
- ProteinProtein regulator of cytokinesis 1
- GenePRC1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids620 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 377 | Tubulin binding | ||||
Sequence: R | ||||||
Site | 387 | Tubulin binding | ||||
Sequence: K |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | contractile ring | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | intercellular bridge | |
Cellular Component | microtubule cytoskeleton | |
Cellular Component | midbody | |
Cellular Component | mitotic spindle midzone | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Cellular Component | spindle | |
Cellular Component | spindle microtubule | |
Cellular Component | spindle pole | |
Molecular Function | identical protein binding | |
Molecular Function | kinesin binding | |
Molecular Function | microtubule binding | |
Molecular Function | protein kinase binding | |
Biological Process | cell division | |
Biological Process | microtubule cytoskeleton organization | |
Biological Process | mitotic spindle elongation | |
Biological Process | mitotic spindle midzone assembly | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | regulation of cytokinesis |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein regulator of cytokinesis 1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO43663
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: 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 the midzone in late anaphase and at the contractile ring in telophase (PubMed:17409436).
Predominantly localized to the nucleus of interphase cells. During mitosis becomes associated with the mitotic spindle poles and localizes with the cell midbody during cytokinesis. Co-localizes with PRC1 in early mitosis and at the spindle midzone from anaphase B to telophase (PubMed:15297875, PubMed:15625105).
Predominantly localized to the nucleus of interphase cells. During mitosis becomes associated with the mitotic spindle poles and localizes with the cell midbody during cytokinesis. Co-localizes with PRC1 in early mitosis and at the spindle midzone from anaphase B to telophase (PubMed:15297875, PubMed:15625105).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_047768 | 187 | in dbSNP:rs7172758 | |||
Sequence: A → E | ||||||
Mutagenesis | 470 | 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. | ||||
Sequence: T → A | ||||||
Mutagenesis | 481 | No effect. Reduces in vitro cyclin E-CDK2 phosphorylation and causes extensive bundling of microtubules to the mitotic spindle; when associated with A-470. | ||||
Sequence: T → A | ||||||
Natural variant | VAR_047769 | 511 | in dbSNP:rs12911192 | |||
Sequence: Y → C | ||||||
Mutagenesis | 577-578 | Weakly reduces binding to the POLO box domains of PLK1. | ||||
Sequence: ST → AA | ||||||
Mutagenesis | 615-616 | Impairs binding to the POLO box domains of PLK1, preventing phosphorylation by PLK1 and recruitment of PLK1 to the spindle. | ||||
Sequence: ST → AA |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 695 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000229737 | 1-620 | UniProt | Protein regulator of cytokinesis 1 | |||
Sequence: MRRSEVLAEESIVCLQKALNHLREIWELIGIPEDQRLQRTEVVKKHIKELLDMMIAEEESLKERLIKSISVCQKELNTLCSELHVEPFQEEGETTILQLEKDLRTQVELMRKQKKERKQELKLLQEQDQELCEILCMPHYDIDSASVPSLEELNQFRQHVTTLRETKASRREEFVSIKRQIILCMEALDHTPDTSFERDVVCEDEDAFCLSLENIATLQKLLRQLEMQKSQNEAVCEGLRTQIRELWDRLQIPEEEREAVATIMSGSKAKVRKALQLEVDRLEELKMQNMKKVIEAIRVELVQYWDQCFYSQEQRQAFAPFCAEDYTESLLQLHDAEIVRLKNYYEVHKELFEGVQKWEETWRLFLEFERKASDPNRFTNRGGNLLKEEKQRAKLQKMLPKLEEELKARIELWEQEHSKAFMVNGQKFMEYVAEQWEMHRLEKERAKQERQLKNKKQTETEMLYGSAPRTPSKRRGLAPNTPGKARKLNTTTMSNATANSSIRPIFGGTVYHSPVSRLPPSGSKPVAASTCSGKKTPRTGRHGANKENLELNGSILSGGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQRELSKASKSDATSGILNSTNIQS | |||||||
Modified residue (large scale data) | 4 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 265 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 267 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 460 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 464 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 466 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 470 | UniProt | Phosphothreonine; by CDK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 470 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 481 | UniProt | Phosphothreonine; by CDK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 481 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 491 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 494 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 501 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 509 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 511 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 513 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 513 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 516 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 532 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 541 | UniProt | In isoform O43663-2; Phosphoserine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 554 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 557 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 560 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 563 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 571 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 571 | UniProt | In isoform O43663-4; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 571 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 578 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 587 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 589 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 592 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 601 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 610 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 615 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 616 | UniProt | Phosphothreonine; by PLK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 616 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 620 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Overexpressed in bladder cancer cells (PubMed:17409436).
Gene expression databases
Organism-specific databases
Interaction
Subunit
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 (via N-terminus) with the C-terminus of CENPE (via C-terminus); the interaction occurs during late mitosis (PubMed:15297875).
Interacts (via N-terminus) with KIF4A (via C-terminus); the interaction is required for the progression of mitosis (PubMed:15297875, PubMed:16431929, PubMed:29848660).
Interacts (via N-terminus) with KIF23 (via C-terminus); the interaction occurs during late mitosis (PubMed:15297875).
Interacts with KIF14 and KIF20A (PubMed:15625105, PubMed:16431929).
Interacts with PLK1 (PubMed:19468300).
Interacts with KIF20B (PubMed:17409436).
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 (via N-terminus) with the C-terminus of CENPE (via C-terminus); the interaction occurs during late mitosis (PubMed:15297875).
Interacts (via N-terminus) with KIF4A (via C-terminus); the interaction is required for the progression of mitosis (PubMed:15297875, PubMed:16431929, PubMed:29848660).
Interacts (via N-terminus) with KIF23 (via C-terminus); the interaction occurs during late mitosis (PubMed:15297875).
Interacts with KIF14 and KIF20A (PubMed:15625105, PubMed:16431929).
Interacts with PLK1 (PubMed:19468300).
Interacts with KIF20B (PubMed:17409436).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O43663 | ACSM1 Q08AH1 | 2 | EBI-741137, EBI-2818055 | |
BINARY | O43663 | CINP Q9BW66 | 3 | EBI-741137, EBI-739784 | |
BINARY | O43663 | MAT2A P31153 | 3 | EBI-741137, EBI-1050743 | |
BINARY | O43663 | PKIA P61925 | 3 | EBI-741137, EBI-2682139 | |
BINARY | O43663 | TRIM37 O94972 | 3 | EBI-741137, EBI-741602 | |
BINARY | O43663-1 | PRC1 O43663-1 | 7 | EBI-1503979, EBI-1503979 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-303 | Required for the interaction with KIF4A | ||||
Sequence: MRRSEVLAEESIVCLQKALNHLREIWELIGIPEDQRLQRTEVVKKHIKELLDMMIAEEESLKERLIKSISVCQKELNTLCSELHVEPFQEEGETTILQLEKDLRTQVELMRKQKKERKQELKLLQEQDQELCEILCMPHYDIDSASVPSLEELNQFRQHVTTLRETKASRREEFVSIKRQIILCMEALDHTPDTSFERDVVCEDEDAFCLSLENIATLQKLLRQLEMQKSQNEAVCEGLRTQIRELWDRLQIPEEEREAVATIMSGSKAKVRKALQLEVDRLEELKMQNMKKVIEAIRVELVQ | ||||||
Region | 1-341 | Dimerization | ||||
Sequence: MRRSEVLAEESIVCLQKALNHLREIWELIGIPEDQRLQRTEVVKKHIKELLDMMIAEEESLKERLIKSISVCQKELNTLCSELHVEPFQEEGETTILQLEKDLRTQVELMRKQKKERKQELKLLQEQDQELCEILCMPHYDIDSASVPSLEELNQFRQHVTTLRETKASRREEFVSIKRQIILCMEALDHTPDTSFERDVVCEDEDAFCLSLENIATLQKLLRQLEMQKSQNEAVCEGLRTQIRELWDRLQIPEEEREAVATIMSGSKAKVRKALQLEVDRLEELKMQNMKKVIEAIRVELVQYWDQCFYSQEQRQAFAPFCAEDYTESLLQLHDAEIVRL | ||||||
Coiled coil | 96-133 | |||||
Sequence: ILQLEKDLRTQVELMRKQKKERKQELKLLQEQDQELCE | ||||||
Coiled coil | 211-304 | |||||
Sequence: SLENIATLQKLLRQLEMQKSQNEAVCEGLRTQIRELWDRLQIPEEEREAVATIMSGSKAKVRKALQLEVDRLEELKMQNMKKVIEAIRVELVQY | ||||||
Region | 342-466 | Spectrin-fold | ||||
Sequence: KNYYEVHKELFEGVQKWEETWRLFLEFERKASDPNRFTNRGGNLLKEEKQRAKLQKMLPKLEEELKARIELWEQEHSKAFMVNGQKFMEYVAEQWEMHRLEKERAKQERQLKNKKQTETEMLYGS | ||||||
Coiled coil | 383-463 | |||||
Sequence: GNLLKEEKQRAKLQKMLPKLEEELKARIELWEQEHSKAFMVNGQKFMEYVAEQWEMHRLEKERAKQERQLKNKKQTETEML | ||||||
Region | 446-488 | Disordered | ||||
Sequence: AKQERQLKNKKQTETEMLYGSAPRTPSKRRGLAPNTPGKARKL | ||||||
Region | 467-620 | Unstructured, Arg/Lys rich | ||||
Sequence: APRTPSKRRGLAPNTPGKARKLNTTTMSNATANSSIRPIFGGTVYHSPVSRLPPSGSKPVAASTCSGKKTPRTGRHGANKENLELNGSILSGGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQRELSKASKSDATSGILNSTNIQS | ||||||
Region | 517-545 | Disordered | ||||
Sequence: RLPPSGSKPVAASTCSGKKTPRTGRHGAN | ||||||
Region | 600-620 | Disordered | ||||
Sequence: LSKASKSDATSGILNSTNIQS |
Domain
Microtubule binding occurs via a basic patch in the central spectrin-like domain and requires also the unstructured C-terminal domain.
Sequence similarities
Belongs to the MAP65/ASE1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
O43663-1
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.
- Name1
- Length620
- Mass (Da)71,607
- Last updated2008-11-25 v2
- Checksum28393C5B1B3662F3
O43663-2
- Name2
O43663-3
- Name3
O43663-4
- Name4
- Differences from canonical
- 584-597: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_035875 | 50-90 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_051979 | 397-426 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 416 | in Ref. 5; BX647317 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_035876 | 558-620 | in isoform 3 | |||
Sequence: GGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQRELSKASKSDATSGILNSTNIQS → ARTFKGFQI | ||||||
Alternative sequence | VSP_051980 | 584-597 | in isoform 2 and isoform 4 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF044588 EMBL· GenBank· DDBJ | AAC02688.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297117 EMBL· GenBank· DDBJ | BAG59623.1 EMBL· GenBank· DDBJ | mRNA | ||
AC068831 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC003138 EMBL· GenBank· DDBJ | AAH03138.1 EMBL· GenBank· DDBJ | mRNA | ||
BC005140 EMBL· GenBank· DDBJ | AAH05140.1 EMBL· GenBank· DDBJ | mRNA | ||
BX647317 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |