Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O43663

- PRC1_HUMAN

UniProt

O43663 - PRC1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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 kinase binding Source: UniProtKB

GO - Biological processi

  1. cytokinesis Source: UniProtKB
  2. mitotic spindle elongation Source: ProtInc
Complete GO annotation...

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
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

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 CDK12 Publications
Modified residuei481 – 4811Phosphothreonine; by CDK12 Publications
Modified residuei501 – 5011Phosphoserine1 Publication
Modified residuei513 – 5131Phosphoserine1 Publication
Modified residuei571 – 5711Phosphoserine1 Publication
Modified residuei592 – 5921Phosphoserine1 Publication
Modified residuei615 – 6151Phosphoserine1 Publication
Modified residuei616 – 6161Phosphothreonine; by PLK11 Publication

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

BgeeiO43663.
CleanExiHS_PRC1.
ExpressionAtlasiO43663. baseline and differential.
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. 24 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.
GeneTreeiENSGT00390000009453.
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

        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. 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. 24 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.
GeneTreei ENSGT00390000009453.
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

Bgeei O43663.
CleanExi HS_PRC1.
ExpressionAtlasi O43663. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 118 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