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O43663 (PRC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein regulator of cytokinesis 1
Gene names
Name:PRC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length620 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.6 Ref.7 Ref.9 Ref.10 Ref.16 Ref.20

Subunit structure

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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.16 Ref.20

Subcellular location

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. Ref.1 Ref.6 Ref.12

Domain

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

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. Ref.1 Ref.11 Ref.12

Sequence similarities

Belongs to the MAP65/ASE1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRIM37O949723EBI-741137,EBI-741602

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: 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.
Isoform 2 Ref.4 (identifier: O43663-2)

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.
Isoform 3 (identifier: O43663-3)

The sequence of this isoform differs from the canonical sequence as follows:
     50-90: Missing.
     558-620: GGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQRELSKASKSDATSGILNSTNIQS → ARTFKGFQI
Note: No experimental confirmation available.
Isoform 4 (identifier: O43663-4)

The sequence of this isoform differs from the canonical sequence as follows:
     584-597: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 620620Protein regulator of cytokinesis 1
PRO_0000229737

Regions

Region1 – 341341Dimerization
Region342 – 466125Spectrin-fold
Region467 – 620154Unstructured, Arg/Lys rich
Coiled coil96 – 13338 Potential
Coiled coil211 – 30494 Potential
Coiled coil383 – 46381 Potential

Sites

Binding site3771Tubulin
Binding site3871Tubulin

Amino acid modifications

Modified residue1951Phosphoserine
Modified residue2651Phosphoserine
Modified residue4701Phosphothreonine; by CDK1 Ref.1 Ref.11 Ref.12
Modified residue4811Phosphothreonine; by CDK1 Ref.1 Ref.11 Ref.12
Modified residue5011Phosphoserine
Modified residue5131Phosphoserine Ref.17
Modified residue5711Phosphoserine
Modified residue5921Phosphoserine
Modified residue6151Phosphoserine
Modified residue6161Phosphothreonine; by PLK1 Ref.12

Natural variations

Alternative sequence50 – 9041Missing in isoform 3.
VSP_035875
Alternative sequence397 – 42630Missing in isoform 2. Ref.4
VSP_051979
Alternative sequence558 – 62063GGYPG…TNIQS → ARTFKGFQI in isoform 3.
VSP_035876
Alternative sequence584 – 59714Missing in isoform 2 and isoform 4. Ref.4
VSP_051980
Natural variant1871A → E. Ref.1 Ref.2 Ref.4
Corresponds to variant rs7172758 [ dbSNP | Ensembl ].
VAR_047768
Natural variant5111Y → C.
Corresponds to variant rs12911192 [ dbSNP | Ensembl ].
VAR_047769

Experimental info

Mutagenesis4701T → 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. Ref.1 Ref.6 Ref.12
Mutagenesis4811T → 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. Ref.1 Ref.6 Ref.12
Mutagenesis577 – 5782ST → AA: Weakly reduces binding to the POLO box domains of PLK1.
Mutagenesis615 – 6162ST → AA: Impairs binding to the POLO box domains of PLK1, preventing phosphorylation by PLK1 and recruitment of PLK1 to the spindle.
Sequence conflict4161E → G in BX647317. Ref.5

Secondary structure

.............................. 620
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 28393C5B1B3662F3

FASTA62071,607
        10         20         30         40         50         60 
MRRSEVLAEE SIVCLQKALN HLREIWELIG IPEDQRLQRT EVVKKHIKEL LDMMIAEEES 

        70         80         90        100        110        120 
LKERLIKSIS VCQKELNTLC SELHVEPFQE EGETTILQLE KDLRTQVELM RKQKKERKQE 

       130        140        150        160        170        180 
LKLLQEQDQE LCEILCMPHY DIDSASVPSL EELNQFRQHV TTLRETKASR REEFVSIKRQ 

       190        200        210        220        230        240 
IILCMEALDH TPDTSFERDV VCEDEDAFCL SLENIATLQK LLRQLEMQKS QNEAVCEGLR 

       250        260        270        280        290        300 
TQIRELWDRL QIPEEEREAV ATIMSGSKAK VRKALQLEVD RLEELKMQNM KKVIEAIRVE 

       310        320        330        340        350        360 
LVQYWDQCFY SQEQRQAFAP FCAEDYTESL LQLHDAEIVR LKNYYEVHKE LFEGVQKWEE 

       370        380        390        400        410        420 
TWRLFLEFER KASDPNRFTN RGGNLLKEEK QRAKLQKMLP KLEEELKARI ELWEQEHSKA 

       430        440        450        460        470        480 
FMVNGQKFME YVAEQWEMHR LEKERAKQER QLKNKKQTET EMLYGSAPRT PSKRRGLAPN 

       490        500        510        520        530        540 
TPGKARKLNT TTMSNATANS SIRPIFGGTV YHSPVSRLPP SGSKPVAAST CSGKKTPRTG 

       550        560        570        580        590        600 
RHGANKENLE LNGSILSGGY PGSAPLQRNF SINSVASTYS EFAKDPSLSD SSTVGLQREL 

       610        620 
SKASKSDATS GILNSTNIQS 

« Hide

Isoform 2 [UniParc].

Checksum: 99DFC0F36E2BC312
Show »

FASTA57666,596
Isoform 3 [UniParc].

Checksum: 609991EF3214602F
Show »

FASTA52561,388
Isoform 4 [UniParc].

Checksum: FED638FB918F6A35
Show »

FASTA60670,191

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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: Kidney and Placenta.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS32334.1. [O43663-1]
CCDS45353.2. [O43663-3]
RefSeqNP_001254509.1. NM_001267580.1.
NP_003972.1. NM_003981.3.
UniGeneHs.366401.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3NRXX-ray1.75A/B341-466[»]
3NRYX-ray2.00A341-466[»]
4L3IX-ray3.60A/B1-486[»]
4L6YX-ray3.30A/B1-486[»]
ProteinModelPortalO43663.
SMRO43663. Positions 2-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114517. 22 interactions.
DIPDIP-34436N.
IntActO43663. 8 interactions.
MINTMINT-1459735.
STRING9606.ENSP00000377793.

PTM databases

PhosphoSiteO43663.

Proteomic databases

MaxQBO43663.
PaxDbO43663.
PRIDEO43663.

Protocols and materials databases

DNASU9055.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361188; ENSP00000354679; ENSG00000198901.
ENST00000394249; ENSP00000377793; ENSG00000198901. [O43663-1]
ENST00000442656; ENSP00000409549; ENSG00000198901. [O43663-3]
GeneID9055.
KEGGhsa:9055.
UCSCuc002bqm.4. human. [O43663-1]
uc010uqs.3. human. [O43663-3]

Organism-specific databases

CTD9055.
GeneCardsGC15M091509.
HGNCHGNC:9341. PRC1.
HPAHPA034521.
MIM603484. gene.
neXtProtNX_O43663.
PharmGKBPA33703.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG298643.
HOGENOMHOG000082534.
HOVERGENHBG052963.
InParanoidO43663.
KOK16732.
OMAHYDIDSA.
OrthoDBEOG7QRQTF.
PhylomeDBO43663.
TreeFamTF323976.

Gene expression databases

ArrayExpressO43663.
BgeeO43663.
CleanExHS_PRC1.
GenevestigatorO43663.

Family and domain databases

InterProIPR007145. MAP65_Ase1_PRC1.
[Graphical view]
PANTHERPTHR19321. PTHR19321. 1 hit.
PfamPF03999. MAP65_ASE1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRC1. human.
EvolutionaryTraceO43663.
GeneWikiPRC1.
GenomeRNAi9055.
NextBio33927.
PROO43663.
SOURCESearch...

Entry information

Entry namePRC1_HUMAN
AccessionPrimary (citable) accession number: O43663
Secondary accession number(s): A6NC44 expand/collapse secondary AC list , B4DLR1, H9KV59, Q9BSB6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM