O43663 (PRC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein regulator of cytokinesis 1

Gene names

Name:

PRC1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	620 AA.
Sequence status	Complete.
Protein existence	Evidence 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.5 Ref.6 Ref.8 Ref.9 Ref.15 Ref.18
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.6 Ref.7 Ref.8 Ref.9 Ref.15 Ref.18
Subcellular location	Nucleus. Cytoplasm. Cytoplasm › cytoskeleton › spindle 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.5 Ref.11
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.10 Ref.11
Sequence similarities	Belongs to the MAP65/ASE1 family.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cytoplasm Cytoskeleton Microtubule Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokinesis Inferred from direct assay Ref.11. Source: UniProtKB mitotic spindle elongation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA spindle microtubule Traceable author statement Ref.1. Source: ProtInc spindle pole Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRIM37	O94972	3	EBI-741137,EBI-741602

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 620

620

Protein regulator of cytokinesis 1

PRO_0000229737

Regions

Region

1 – 341

341

Dimerization

Region

342 – 466

125

Spectrin-fold

Region

467 – 620

154

Unstructured, Arg/Lys rich

Coiled coil

96 – 133

38

Potential

Coiled coil

211 – 304

94

Potential

Coiled coil

383 – 463

81

Potential

Sites

Binding site

377

1

Tubulin

Binding site

387

1

Tubulin

Amino acid modifications

Modified residue

195

1

Phosphoserine

Modified residue

265

1

Phosphoserine

Modified residue

470

1

Phosphothreonine; by CDK1 Ref.1 Ref.10 Ref.11

Modified residue

481

1

Phosphothreonine; by CDK1 Ref.1 Ref.10 Ref.11

Modified residue

501

1

Phosphoserine

Modified residue

513

1

Phosphoserine Ref.16

Modified residue

571

1

Phosphoserine

Modified residue

592

1

Phosphoserine

Modified residue

615

1

Phosphoserine

Modified residue

616

1

Phosphothreonine; by PLK1 Ref.11

Natural variations

Alternative sequence

50 – 90

41

Missing in isoform 3.

VSP_035875

Alternative sequence

397 – 426

30

Missing in isoform 2. Ref.4

VSP_051979

Alternative sequence

558 – 620

63

GGYPG…TNIQS → ARTFKGFQI in isoform 3.

VSP_035876

Alternative sequence

584 – 597

14

Missing in isoform 2. Ref.4

VSP_051980

Natural variant

187

1

A → E. Ref.1 Ref.2 Ref.4
Corresponds to variant rs7172758 [ dbSNP | Ensembl ].

VAR_047768

Natural variant

511

1

Y → C.
Corresponds to variant rs12911192 [ dbSNP | Ensembl ].

VAR_047769

Experimental info

Mutagenesis

470

1

T → 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.5 Ref.11

Mutagenesis

481

1

T → 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.5 Ref.11

Mutagenesis

577 – 578

2

ST → AA: Weakly reduces binding to the POLO box domains of PLK1.

Mutagenesis

615 – 616

2

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

620

Helix Strand Turn

Details...

Helix

341 – 345

5

Helix

347 – 373

27

Helix

375 – 378

4

Helix

385 – 417

33

Helix

428 – 464

37

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 2. Checksum: 28393C5B1B3662F3	FASTA	620	71,607
	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
	Isoform 2 [UniParc]. Checksum: 99DFC0F36E2BC312	FASTA	576	66,596
	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 QRAKLQKFME YVAEQWEMHR LEKERAKQER 430 440 450 460 470 480 QLKNKKQTET EMLYGSAPRT PSKRRGLAPN TPGKARKLNT TTMSNATANS SIRPIFGGTV 490 500 510 520 530 540 YHSPVSRLPP SGSKPVAAST CSGKKTPRTG RHGANKENLE LNGSILSGGY PGSAPLQRNF 550 560 570 SINSVASTYS EFARELSKAS KSDATSGILN STNIQS
	Isoform 3 [UniParc]. Checksum: 609991EF3214602F	FASTA	525	61,388
	10 20 30 40 50 60 MRRSEVLAEE SIVCLQKALN HLREIWELIG IPEDQRLQRT EVVKKHIKEE GETTILQLEK 70 80 90 100 110 120 DLRTQVELMR KQKKERKQEL KLLQEQDQEL CEILCMPHYD IDSASVPSLE ELNQFRQHVT 130 140 150 160 170 180 TLRETKASRR EEFVSIKRQI ILCMEALDHT PDTSFERDVV CEDEDAFCLS LENIATLQKL 190 200 210 220 230 240 LRQLEMQKSQ NEAVCEGLRT QIRELWDRLQ IPEEEREAVA TIMSGSKAKV RKALQLEVDR 250 260 270 280 290 300 LEELKMQNMK KVIEAIRVEL VQYWDQCFYS QEQRQAFAPF CAEDYTESLL QLHDAEIVRL 310 320 330 340 350 360 KNYYEVHKEL FEGVQKWEET WRLFLEFERK ASDPNRFTNR GGNLLKEEKQ RAKLQKMLPK 370 380 390 400 410 420 LEEELKARIE LWEQEHSKAF MVNGQKFMEY VAEQWEMHRL EKERAKQERQ LKNKKQTETE 430 440 450 460 470 480 MLYGSAPRTP SKRRGLAPNT PGKARKLNTT TMSNATANSS IRPIFGGTVY HSPVSRLPPS 490 500 510 520 GSKPVAASTC SGKKTPRTGR HGANKENLEL NGSILSARTF KGFQI

References

	« Hide 'large scale' referencesShow '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. , 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: Kidney and Placenta.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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].
[18]	"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.

IPI

IPI00022629.
IPI00645623.
IPI00915034.

RefSeq

NP_001254509.1. NM_001267580.1.
NP_003972.1. NM_003981.3.

UniGene

Hs.366401.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3NRX	X-ray	1.75	A/B	341-466	[»]
3NRY	X-ray	2.00	A	341-466	[»]

ProteinModelPortal

O43663.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34436N.

IntAct

O43663. 5 interactions.

MINT

MINT-1459735.

STRING

9606.ENSP00000377793.

PTM databases

PhosphoSite

O43663.

Proteomic databases

PaxDb

O43663.

PRIDE

O43663.

Protocols and materials databases

DNASU

9055.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000394249; ENSP00000377793; ENSG00000198901.
ENST00000442656; ENSP00000409549; ENSG00000198901.

GeneID

9055.

KEGG

hsa:9055.

UCSC

uc002bqm.3. human.
uc010uqs.2. human.

Organism-specific databases

CTD

9055.

GeneCards

GC15M091509.

HGNC

HGNC:9341. PRC1.

HPA

HPA034521.

MIM

603484. gene.

neXtProt

NX_O43663.

PharmGKB

PA33703.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG298643.

HOGENOM

HOG000082534.

HOVERGEN

HBG052963.

InParanoid

O43663.

KO

K16732.

OMA

HYDIDSA.

PhylomeDB

O43663.

Gene expression databases

ArrayExpress

O43663.

Bgee

O43663.

CleanEx

HS_PRC1.

Genevestigator

O43663.

GermOnline

ENSG00000198901. Homo sapiens.

Family and domain databases

InterPro

IPR007145. MAP65_Ase1_PRC1.
[Graphical view]

PANTHER

PTHR19321. PTHR19321. 1 hit.

Pfam

PF03999. MAP65_ASE1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PRC1. human.

EvolutionaryTrace

O43663.

GenomeRNAi

9055.

NextBio

33927.

SOURCE

Search...

Entry information

Entry name

PRC1_HUMAN

Accession

Primary (citable) accession number: O43663
Secondary accession number(s): A6NC44, B4DLR1, Q9BSB6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.