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O43663

- PRC1_HUMAN

UniProt

O43663 - PRC1_HUMAN

Protein

Protein regulator of cytokinesis 1

Gene

PRC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    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.7 Publications

    Sites

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

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: UniProtKB

    GO - Biological processi

    1. cytokinesis Source: UniProtKB
    2. mitotic spindle elongation Source: ProtInc

    Keywords - Biological processi

    Cell cycle, Cell division

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein regulator of cytokinesis 1
    Gene namesi
    Name:PRC1Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:9341. PRC1.

    Subcellular locationi

    Nucleus. Cytoplasm. Cytoplasmcytoskeletonspindle pole
    Note: 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.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. microtubule cytoskeleton Source: HPA
    3. nucleus Source: HPA
    4. plasma membrane Source: HPA
    5. spindle Source: UniProtKB
    6. spindle microtubule Source: ProtInc
    7. spindle pole Source: UniProtKB-SubCell

    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.
    Mutagenesisi615 – 6162ST → AA: Impairs binding to the POLO box domains of PLK1, preventing phosphorylation by PLK1 and recruitment of PLK1 to the spindle.

    Organism-specific databases

    PharmGKBiPA33703.

    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 CDK13 Publications
    Modified residuei481 – 4811Phosphothreonine; by CDK13 Publications
    Modified residuei501 – 5011Phosphoserine1 Publication
    Modified residuei513 – 5131Phosphoserine2 Publications
    Modified residuei571 – 5711Phosphoserine1 Publication
    Modified residuei592 – 5921Phosphoserine1 Publication
    Modified residuei615 – 6151Phosphoserine1 Publication
    Modified residuei616 – 6161Phosphothreonine; by PLK12 Publications

    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.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO43663.
    PaxDbiO43663.
    PRIDEiO43663.

    PTM databases

    PhosphoSiteiO43663.

    Expressioni

    Gene expression databases

    ArrayExpressiO43663.
    BgeeiO43663.
    CleanExiHS_PRC1.
    GenevestigatoriO43663.

    Organism-specific databases

    HPAiHPA034521.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with the C-terminal Rho-GAP domain and the basic region of RACGAP1. The interaction with RACGAP1 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. Interacts with KIF14 and KIF20A. Interacts with PLK1.6 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi114517. 22 interactions.
    DIPiDIP-34436N.
    IntActiO43663. 8 interactions.
    MINTiMINT-1459735.
    STRINGi9606.ENSP00000377793.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    eggNOGiNOG298643.
    HOGENOMiHOG000082534.
    HOVERGENiHBG052963.
    InParanoidiO43663.
    KOiK16732.
    OMAiHYDIDSA.
    OrthoDBiEOG7QRQTF.
    PhylomeDBiO43663.
    TreeFamiTF323976.

    Family and domain databases

    InterProiIPR007145. MAP65_Ase1_PRC1.
    [Graphical view]
    PANTHERiPTHR19321. PTHR19321. 1 hit.
    PfamiPF03999. MAP65_ASE1. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    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

    MRRSEVLAEE SIVCLQKALN HLREIWELIG IPEDQRLQRT EVVKKHIKEL    50
    LDMMIAEEES LKERLIKSIS VCQKELNTLC SELHVEPFQE EGETTILQLE 100
    KDLRTQVELM RKQKKERKQE LKLLQEQDQE LCEILCMPHY DIDSASVPSL 150
    EELNQFRQHV TTLRETKASR REEFVSIKRQ IILCMEALDH TPDTSFERDV 200
    VCEDEDAFCL SLENIATLQK LLRQLEMQKS QNEAVCEGLR TQIRELWDRL 250
    QIPEEEREAV ATIMSGSKAK VRKALQLEVD RLEELKMQNM KKVIEAIRVE 300
    LVQYWDQCFY SQEQRQAFAP FCAEDYTESL LQLHDAEIVR LKNYYEVHKE 350
    LFEGVQKWEE TWRLFLEFER KASDPNRFTN RGGNLLKEEK QRAKLQKMLP 400
    KLEEELKARI ELWEQEHSKA FMVNGQKFME YVAEQWEMHR LEKERAKQER 450
    QLKNKKQTET EMLYGSAPRT PSKRRGLAPN TPGKARKLNT TTMSNATANS 500
    SIRPIFGGTV YHSPVSRLPP SGSKPVAAST CSGKKTPRTG RHGANKENLE 550
    LNGSILSGGY PGSAPLQRNF SINSVASTYS EFAKDPSLSD SSTVGLQREL 600
    SKASKSDATS GILNSTNIQS 620
    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. Contains a phosphoserine at position 541.

    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.

    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:
    EMBL
    GenBank
    DDBJ
    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.4. human. [O43663-1]
    uc010uqs.3. human. [O43663-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS32334.1. [O43663-1 ]
    CCDS45352.1. [O43663-4 ]
    CCDS45353.2. [O43663-3 ]
    RefSeqi NP_001254509.1. NM_001267580.1.
    NP_003972.1. NM_003981.3.
    UniGenei Hs.366401.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3NRX X-ray 1.75 A/B 341-466 [» ]
    3NRY X-ray 2.00 A 341-466 [» ]
    4L3I X-ray 3.60 A/B 1-486 [» ]
    4L6Y X-ray 3.30 A/B 1-486 [» ]
    ProteinModelPortali O43663.
    SMRi O43663. Positions 2-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114517. 22 interactions.
    DIPi DIP-34436N.
    IntActi O43663. 8 interactions.
    MINTi MINT-1459735.
    STRINGi 9606.ENSP00000377793.

    PTM databases

    PhosphoSitei O43663.

    Proteomic databases

    MaxQBi O43663.
    PaxDbi O43663.
    PRIDEi O43663.

    Protocols and materials databases

    DNASUi 9055.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361188 ; ENSP00000354679 ; ENSG00000198901 . [O43663-4 ]
    ENST00000394249 ; ENSP00000377793 ; ENSG00000198901 . [O43663-1 ]
    ENST00000442656 ; ENSP00000409549 ; ENSG00000198901 . [O43663-3 ]
    GeneIDi 9055.
    KEGGi hsa:9055.
    UCSCi uc002bqm.4. human. [O43663-1 ]
    uc010uqs.3. human. [O43663-3 ]

    Organism-specific databases

    CTDi 9055.
    GeneCardsi GC15M091509.
    HGNCi HGNC:9341. PRC1.
    HPAi HPA034521.
    MIMi 603484. gene.
    neXtProti NX_O43663.
    PharmGKBi PA33703.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG298643.
    HOGENOMi HOG000082534.
    HOVERGENi HBG052963.
    InParanoidi O43663.
    KOi K16732.
    OMAi HYDIDSA.
    OrthoDBi EOG7QRQTF.
    PhylomeDBi O43663.
    TreeFami TF323976.

    Miscellaneous databases

    ChiTaRSi PRC1. human.
    EvolutionaryTracei O43663.
    GeneWikii PRC1.
    GenomeRNAii 9055.
    NextBioi 33927.
    PROi O43663.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43663.
    Bgeei O43663.
    CleanExi HS_PRC1.
    Genevestigatori O43663.

    Family and domain databases

    InterProi IPR007145. MAP65_Ase1_PRC1.
    [Graphical view ]
    PANTHERi PTHR19321. PTHR19321. 1 hit.
    Pfami PF03999. MAP65_ASE1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "PRC1: a human mitotic spindle-associated CDK substrate protein required 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF THR-470 AND THR-481, SUBCELLULAR LOCATION, PHOSPHORYLATION, VARIANT GLU-187.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT GLU-187.
    3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT GLU-187.
      Tissue: KidneyImported and PlacentaImported.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 411-620 (ISOFORM 4).
    6. "PRC1 is a microtubule binding and bundling protein essential to maintain the mitotic spindle midzone."
      Mollinari C., Kleman J.-P., Jiang W., Schoehn G., Hunter T., Margolis R.L.
      J. Cell Biol. 157:1175-1186(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF THR-470 AND THR-481, SUBCELLULAR LOCATION.
    7. "Essential roles of KIF4 and its binding partner PRC1 in organized central spindle midzone formation."
      Kurasawa Y., Earnshaw W.C., Mochizuki Y., Dohmae N., Todokoro K.
      EMBO J. 23:3237-3248(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CENPE; KIF4A AND KIF23.
    8. "Human mitotic spindle-associated protein PRC1 inhibits MgcRacGAP activity toward Cdc42 during the metaphase."
      Ban R., Irino Y., Fukami K., Tanaka H.
      J. Biol. Chem. 279:16394-16402(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RACGAP1.
    9. "Cell cycle-dependent translocation of PRC1 on the spindle by Kif4 is essential for midzone formation and cytokinesis."
      Zhu C., Jiang W.
      Proc. Natl. Acad. Sci. U.S.A. 102:343-348(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KIF4A.
    10. "KIF14 and citron kinase act together to promote efficient cytokinesis."
      Gruneberg U., Neef R., Li X., Chan E.H.Y., Chalamalasetty R.B., Nigg E.A., Barr F.A.
      J. Cell Biol. 172:363-372(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KIF4A; KIF14; KIF20A AND KIF23.
    11. "Mitotic phosphorylation of PRC1 at Thr470 is required for PRC1 oligomerization 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-470 AND THR-481.
    12. "Choice of Plk1 docking partners during mitosis and cytokinesis is controlled 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-470; THR-481 AND THR-616, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-470; THR-481; 577-SER-THR-578 AND 615-SER-THR-616.
    13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEF complex to initiate cleavage furrow formation."
      Wolfe B.A., Takaki T., Petronczki M., Glotzer M.
      PLoS Biol. 7:E1000110-E1000110(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PLK1.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Insights into antiparallel microtubule crosslinking by PRC1, a conserved nonmotor microtubule binding protein."
      Subramanian R., Wilson-Kubalek E.M., Arthur C.P., Bick M.J., Campbell E.A., Darst S.A., Milligan R.A., Kapoor T.M.
      Cell 142:433-443(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 341-466, ELECTRON MICROSCOPY, TUBULIN-BINDING SITES, FUNCTION, SUBUNIT.

    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: October 1, 2014
    This is version 117 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

    External Data

    Dasty 3