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Q9P258 (RCC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein RCC2
Alternative name(s):
RCC1-like protein TD-60
Telophase disk protein of 60 kDa
Gene names
Name:RCC2
Synonyms:KIAA1470, TD60
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length522 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Nucleusnucleolus. Chromosomecentromere. Cytoplasmcytoskeletonspindle. 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 processCell cycle
Cell division
Mitosis
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Microtubule
Nucleus
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromosome passenger complex localization to kinetochore

Inferred from mutant phenotype Ref.1. Source: UniProt

focal adhesion assembly

Inferred from direct assay PubMed 19738201. Source: UniProt

integrin-mediated signaling pathway

Inferred from direct assay PubMed 19738201. Source: UniProt

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of GTPase activity

Inferred from sequence or structural similarity. Source: UniProt

negative regulation of focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProt

negative regulation of substrate adhesion-dependent cell spreading

Inferred from sequence or structural similarity. Source: UniProt

positive regulation of G2/M transition of mitotic cell cycle

Inferred from mutant phenotype Ref.1. Source: UniProt

positive regulation of attachment of spindle microtubules to kinetochore

Inferred from mutant phenotype Ref.1. Source: UniProt

regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProt

   Cellular_componentchromosome, centromeric core region

Inferred from direct assay Ref.1. Source: UniProt

cytosol

Traceable author statement. Source: Reactome

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

midbody

Inferred from direct assay Ref.1. Source: UniProt

mitotic spindle midzone

Inferred from direct assay Ref.1. Source: UniProt

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRac GTPase binding

Inferred from physical interaction Ref.1. Source: UniProt

microtubule binding

Inferred from mutant phenotype Ref.1. Source: UniProt

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 22282019. Source: UniProt

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 522522Protein RCC2
PRO_0000206652

Regions

Repeat103 – 16563RCC1 1
Repeat168 – 21952RCC1 2
Repeat221 – 27151RCC1 3
Repeat273 – 34775RCC1 4
Repeat348 – 40154RCC1 5
Repeat403 – 44745RCC1 6
Repeat448 – 50154RCC1 7

Amino acid modifications

Modified residue161Phosphoserine Ref.12
Modified residue431Phosphoserine Ref.9
Modified residue441Phosphoserine Ref.9
Modified residue451Phosphoserine Ref.9
Modified residue461Phosphoserine Ref.9
Modified residue501Phosphoserine Ref.9
Modified residue511Phosphoserine Ref.9 Ref.10
Modified residue921N6-acetyllysine Ref.13
Modified residue1241N6-acetyllysine By similarity
Modified residue2931N6-acetyllysine Ref.13
Modified residue3421Phosphothreonine Ref.12
Modified residue3471Phosphoserine Ref.12
Modified residue3771N6-acetyllysine Ref.13

Experimental info

Sequence conflict145 – 1484LAGV → RTRG Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9P258 [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: 7065F70AEA98EDC3

FASTA52256,085
        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 

« Hide

References

« Hide '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].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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.
[15]"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].
[16]"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.
CCDSCCDS181.1.
PIRT50630.
RefSeqNP_001129676.1. NM_001136204.2.
NP_061185.1. NM_018715.3.
UniGeneHs.380857.

3D structure databases

ProteinModelPortalQ9P258.
SMRQ9P258. Positions 101-483.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121001. 17 interactions.
IntActQ9P258. 6 interactions.
MINTMINT-3037281.
STRING9606.ENSP00000364582.

PTM databases

PhosphoSiteQ9P258.

Polymorphism databases

DMDM71152033.

2D gel databases

SWISS-2DPAGEQ9P258.

Proteomic databases

MaxQBQ9P258.
PaxDbQ9P258.
PeptideAtlasQ9P258.
PRIDEQ9P258.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375433; ENSP00000364582; ENSG00000179051.
ENST00000375436; ENSP00000364585; ENSG00000179051.
GeneID55920.
KEGGhsa:55920.
UCSCuc001bal.3. human.

Organism-specific databases

CTD55920.
GeneCardsGC01M017733.
HGNCHGNC:30297. RCC2.
HPAHPA056177.
MIM609587. gene.
neXtProtNX_Q9P258.
PharmGKBPA142671091.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5184.
HOGENOMHOG000232061.
HOVERGENHBG080538.
InParanoidQ9P258.
OMAVDCKGNL.
OrthoDBEOG7TTQ7B.
PhylomeDBQ9P258.
TreeFamTF101168.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

BgeeQ9P258.
CleanExHS_RCC2.
GenevestigatorQ9P258.

Family and domain databases

Gene3D2.130.10.30. 1 hit.
InterProIPR009091. RCC1/BLIP-II.
IPR028641. RCC2.
IPR000408. Reg_chr_condens.
[Graphical view]
PANTHERPTHR22870:SF146. PTHR22870:SF146. 1 hit.
PfamPF00415. RCC1. 4 hits.
[Graphical view]
PRINTSPR00633. RCCNDNSATION.
SUPFAMSSF50985. SSF50985. 1 hit.
PROSITEPS00626. RCC1_2. 2 hits.
PS50012. RCC1_3. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRCC2.
GenomeRNAi55920.
NextBio61323.
PROQ9P258.
SOURCESearch...

Entry information

Entry nameRCC2_HUMAN
AccessionPrimary (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: 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

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM