Q9P258 (RCC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein RCC2

Alternative name(s):
RCC1-like protein TD-60
Telophase disk protein of 60 kDa

Gene names

Name:	RCC2
Synonyms:	KIAA1470, TD60

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	522 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for completion of mitosis and cytokinesis. May function as a guanine nucleotide exchange factor for the small GTPase RAC1. Ref.1
Subunit structure	Binds preferentially to the nucleotide-free form of RAC1. Interacts with microtubules. Ref.1
Subcellular location	Nucleus › nucleolus. Chromosome › centromere. Cytoplasm › cytoskeleton › spindle. Note: Appears in the nucleus at G2, then concentrates at the inner centromere region of chromosomes during prophase. Redistributes to the midzone of the mitotic spindle during anaphase. Here, the protein covers the entire equatorial diameter from cortex to cortex. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8
Sequence similarities	Contains 7 RCC1 repeats.
Sequence caution	The sequence BAA95994.1 differs from that shown. Reason: Erroneous initiation. The sequence CAB94882.1 differs from that shown. Reason: Frameshift at position 477.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Microtubule Nucleus
Domain	Repeat
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitotic prometaphase Traceable author statement. Source: Reactome
Cellular_component	chromosome, centromeric region Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 522	522	Protein RCC2		PRO_0000206652
Regions
	Repeat	103 – 165	63	RCC1 1
	Repeat	168 – 219	52	RCC1 2
	Repeat	221 – 271	51	RCC1 3
	Repeat	273 – 347	75	RCC1 4
	Repeat	348 – 401	54	RCC1 5
	Repeat	403 – 447	45	RCC1 6
	Repeat	448 – 501	54	RCC1 7
Amino acid modifications
	Modified residue	16	1	Phosphoserine Ref.11
	Modified residue	43	1	Phosphoserine Ref.9
	Modified residue	44	1	Phosphoserine Ref.9
	Modified residue	45	1	Phosphoserine Ref.9
	Modified residue	46	1	Phosphoserine Ref.9
	Modified residue	50	1	Phosphoserine Ref.9
	Modified residue	51	1	Phosphoserine Ref.9 Ref.10
	Modified residue	92	1	N6-acetyllysine Ref.12
	Modified residue	293	1	N6-acetyllysine Ref.12
	Modified residue	342	1	Phosphothreonine Ref.11
	Modified residue	347	1	Phosphoserine Ref.11
	Modified residue	377	1	N6-acetyllysine Ref.12
Experimental info
	Sequence conflict	145 – 148	4	LAGV → RTRG Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9P258 [UniParc]. Last modified July 19, 2005. Version 2. Checksum: 7065F70AEA98EDC3	FASTA	522	56,085
	10 20 30 40 50 60 MPRKKAAAAA WEEPSSGNGT ARAGPRKRGG PAGRKRERPE RCSSSSGGGS SGDEDGLELD 70 80 90 100 110 120 GAPGGGKRAA RPATAGKAGG AAVVITEPEH TKERVKLEGS KCKGQLLIFG ATNWDLIGRK 130 140 150 160 170 180 EVPKQQAAYR NLGQNLWGPH RYGCLAGVRV RTVVSGSCAA HSLLITTEGK LWSWGRNEKG 190 200 210 220 230 240 QLGHGDTKRV EAPRLIEGLS HEVIVSAACG RNHTLALTET GSVFAFGENK MGQLGLGNQT 250 260 270 280 290 300 DAVPSPAQIM YNGQPITKMA CGAEFSMIMD CKGNLYSFGC PEYGQLGHNS DGKFIARAQR 310 320 330 340 350 360 IEYDCELVPR RVAIFIEKTK DGQILPVPNV VVRDVACGAN HTLVLDSQKR VFSWGFGGYG 370 380 390 400 410 420 RLGHAEQKDE MVPRLVKLFD FPGRGASQIY AGYTCSFAVS EVGGLFFWGA TNTSRESTMY 430 440 450 460 470 480 PKAVQDLCGW RIRSLACGKS SIIVAADEST ISWGPSPTFG ELGYGDHKPK SSTAAQEVKT 490 500 510 520 LDGIFSEQVA MGYSHSLVIA RDESETEKEK IKKLPEYNPR TL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mammalian passenger protein TD-60 is an RCC1 family member with an essential role in prometaphase to metaphase progression." Mollinari C., Reynaud C., Martineau-Thuillier S., Monier S., Kieffer S., Garin J., Andreassen P.R., Boulet A., Goud B., Kleman J.-P., Margolis R.L. Dev. Cell 5:295-307(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH MICROTUBULES AND RAC1.
[2]	"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"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]. Tissue: Muscle, Natural killer cell and Uterus.
[4]	"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 145-477. Tissue: Melanoma.
[5]	"Telophase disc: a new mammalian mitotic organelle that bisects telophase cells with a possible function in cytokinesis." Andreassen P.R., Palmer D.K., Wener M.H., Margolis R.L. J. Cell Sci. 99:523-534(1991) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[6]	"Delay of HeLa cell cleavage into interphase using dihydrocytochalasin B: retention of a postmitotic spindle and telophase disc correlates with synchronous cleavage recovery." Martineau S.N., Andreassen P.R., Margolis R.L. J. Cell Biol. 131:191-205(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"Colocalization of TD-60 and INCENP throughout G2 and mitosis: evidence for their possible interaction in signalling cytokinesis." Martineau-Thuillier S., Andreassen P.R., Margolis R.L. Chromosoma 107:461-470(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-44; SER-45; SER-46; SER-50 AND SER-51, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-51, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-342 AND SER-347, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-92; LYS-293 AND LYS-377, MASS SPECTROMETRY.
[13]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ421269 mRNA. Translation: CAD13148.1. AB040903 mRNA. Translation: BAA95994.1. Different initiation. BC004933 mRNA. Translation: AAH04933.1. BC042141 mRNA. Translation: AAH42141.1. BC053908 mRNA. Translation: AAH53908.1. AL359612 mRNA. Translation: CAB94882.1. Frameshift.
IPI	IPI00465044.
PIR	T50630.
RefSeq	NP_001129676.1. NM_001136204.2. NP_061185.1. NM_018715.3.
UniGene	Hs.380857.
3D structure databases
ProteinModelPortal	Q9P258.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9P258. 6 interactions.
STRING	9606.ENSP00000364582.
PTM databases
PhosphoSite	Q9P258.
Polymorphism databases
DMDM	71152033.
2D gel databases
SWISS-2DPAGE	Q9P258.
Proteomic databases
PaxDb	Q9P258.
PeptideAtlas	Q9P258.
PRIDE	Q9P258.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000375433; ENSP00000364582; ENSG00000179051. ENST00000375436; ENSP00000364585; ENSG00000179051.
GeneID	55920.
KEGG	hsa:55920.
UCSC	uc001bal.3. human.
Organism-specific databases
CTD	55920.
GeneCards	GC01M017733.
HGNC	HGNC:30297. RCC2.
MIM	609587. gene.
neXtProt	NX_Q9P258.
PharmGKB	PA142671091.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5184.
HOGENOM	HOG000232061.
HOVERGEN	HBG080538.
InParanoid	Q9P258.
OMA	FGENKLG.
OrthoDB	EOG4DNF4B.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases.
Gene expression databases
Bgee	Q9P258.
CleanEx	HS_RCC2.
Genevestigator	Q9P258.
GermOnline	ENSG00000179051. Homo sapiens.
Family and domain databases
Gene3D	2.130.10.30. 1 hit.
InterPro	IPR009091. RCC1/BLIP-II. IPR000408. Reg_chr_condens. [Graphical view]
Pfam	PF00415. RCC1. 4 hits. [Graphical view]
PRINTS	PR00633. RCCNDNSATION.
SUPFAM	SSF50985. RCC1/BLIP-II. 1 hit.
PROSITE	PS00625. RCC1_1. False negative. PS00626. RCC1_2. 2 hits. PS50012. RCC1_3. 5 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	55920.
NextBio	61323.
SOURCE	Search...

Entry information

Entry name

RCC2_HUMAN

Accession

Primary (citable) accession number: Q9P258
Secondary accession number(s): Q8IVL9, Q9BSN6, Q9NPV8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
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.