Skip Header

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

Q9P258

- RCC2_HUMAN

UniProt

Q9P258 - RCC2_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 RCC2

Gene

RCC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Required for completion of mitosis and cytokinesis. May function as a guanine nucleotide exchange factor for the small GTPase RAC1.1 Publication

GO - Molecular functioni

  1. microtubule binding Source: UniProt
  2. poly(A) RNA binding Source: UniProtKB
  3. Rac GTPase binding Source: UniProt

GO - Biological processi

  1. chromosome passenger complex localization to kinetochore Source: UniProt
  2. endosome organization Source: InterPro
  3. focal adhesion assembly Source: UniProt
  4. integrin-mediated signaling pathway Source: UniProt
  5. mitotic cell cycle Source: Reactome
  6. mitotic nuclear division Source: UniProtKB-KW
  7. negative regulation of focal adhesion assembly Source: UniProt
  8. negative regulation of GTPase activity Source: UniProt
  9. negative regulation of substrate adhesion-dependent cell spreading Source: UniProt
  10. positive regulation of attachment of spindle microtubules to kinetochore Source: UniProt
  11. positive regulation of G2/M transition of mitotic cell cycle Source: UniProt
  12. regulation of cell migration Source: UniProt
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiREACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein RCC2
Alternative name(s):
RCC1-like protein TD-60
Telophase disk protein of 60 kDa
Gene namesi
Name:RCC2
Synonyms:KIAA1470, TD60
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:30297. RCC2.

Subcellular locationi

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.

GO - Cellular componenti

  1. chromosome, centromeric core domain Source: UniProt
  2. cytosol Source: Reactome
  3. microtubule Source: UniProtKB-KW
  4. midbody Source: UniProt
  5. mitotic spindle midzone Source: UniProt
  6. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671091.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 522522Protein RCC2PRO_0000206652Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Phosphoserine1 Publication
Modified residuei43 – 431Phosphoserine1 Publication
Modified residuei44 – 441Phosphoserine1 Publication
Modified residuei45 – 451Phosphoserine1 Publication
Modified residuei46 – 461Phosphoserine1 Publication
Modified residuei50 – 501Phosphoserine1 Publication
Modified residuei51 – 511Phosphoserine2 Publications
Modified residuei92 – 921N6-acetyllysine1 Publication
Modified residuei124 – 1241N6-acetyllysineBy similarity
Modified residuei293 – 2931N6-acetyllysine1 Publication
Modified residuei342 – 3421Phosphothreonine1 Publication
Modified residuei347 – 3471Phosphoserine1 Publication
Modified residuei377 – 3771N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9P258.
PaxDbiQ9P258.
PeptideAtlasiQ9P258.
PRIDEiQ9P258.

2D gel databases

SWISS-2DPAGEQ9P258.

PTM databases

PhosphoSiteiQ9P258.

Expressioni

Gene expression databases

BgeeiQ9P258.
CleanExiHS_RCC2.
GenevestigatoriQ9P258.

Organism-specific databases

HPAiHPA056177.

Interactioni

Subunit structurei

Binds preferentially to the nucleotide-free form of RAC1. Interacts with microtubules.1 Publication

Protein-protein interaction databases

BioGridi121001. 17 interactions.
IntActiQ9P258. 6 interactions.
MINTiMINT-3037281.
STRINGi9606.ENSP00000364582.

Structurei

3D structure databases

ProteinModelPortaliQ9P258.
SMRiQ9P258. Positions 101-503.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati103 – 16563RCC1 1Add
BLAST
Repeati168 – 21952RCC1 2Add
BLAST
Repeati221 – 27151RCC1 3Add
BLAST
Repeati273 – 34775RCC1 4Add
BLAST
Repeati348 – 40154RCC1 5Add
BLAST
Repeati403 – 44745RCC1 6Add
BLAST
Repeati448 – 50154RCC1 7Add
BLAST

Sequence similaritiesi

Contains 7 RCC1 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5184.
GeneTreeiENSGT00770000120483.
HOGENOMiHOG000232061.
HOVERGENiHBG080538.
InParanoidiQ9P258.
OMAiVDCKGNL.
OrthoDBiEOG7TTQ7B.
PhylomeDBiQ9P258.
TreeFamiTF101168.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR009091. RCC1/BLIP-II.
IPR028641. RCC2.
IPR000408. Reg_chr_condens.
[Graphical view]
PANTHERiPTHR22870:SF146. PTHR22870:SF146. 1 hit.
PfamiPF00415. RCC1. 4 hits.
[Graphical view]
PRINTSiPR00633. RCCNDNSATION.
SUPFAMiSSF50985. SSF50985. 1 hit.
PROSITEiPS00626. RCC1_2. 2 hits.
PS50012. RCC1_3. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9P258-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRKKAAAAA WEEPSSGNGT ARAGPRKRGG PAGRKRERPE RCSSSSGGGS
60 70 80 90 100
SGDEDGLELD GAPGGGKRAA RPATAGKAGG AAVVITEPEH TKERVKLEGS
110 120 130 140 150
KCKGQLLIFG ATNWDLIGRK EVPKQQAAYR NLGQNLWGPH RYGCLAGVRV
160 170 180 190 200
RTVVSGSCAA HSLLITTEGK LWSWGRNEKG QLGHGDTKRV EAPRLIEGLS
210 220 230 240 250
HEVIVSAACG RNHTLALTET GSVFAFGENK MGQLGLGNQT DAVPSPAQIM
260 270 280 290 300
YNGQPITKMA CGAEFSMIMD CKGNLYSFGC PEYGQLGHNS DGKFIARAQR
310 320 330 340 350
IEYDCELVPR RVAIFIEKTK DGQILPVPNV VVRDVACGAN HTLVLDSQKR
360 370 380 390 400
VFSWGFGGYG RLGHAEQKDE MVPRLVKLFD FPGRGASQIY AGYTCSFAVS
410 420 430 440 450
EVGGLFFWGA TNTSRESTMY PKAVQDLCGW RIRSLACGKS SIIVAADEST
460 470 480 490 500
ISWGPSPTFG ELGYGDHKPK SSTAAQEVKT LDGIFSEQVA MGYSHSLVIA
510 520
RDESETEKEK IKKLPEYNPR TL
Length:522
Mass (Da):56,085
Last modified:July 19, 2005 - v2
Checksum:i7065F70AEA98EDC3
GO

Sequence cautioni

The sequence BAA95994.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAB94882.1 differs from that shown. Reason: Frameshift at position 477. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1484LAGV → RTRG(PubMed:17974005)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS181.1.
PIRiT50630.
RefSeqiNP_001129676.1. NM_001136204.2.
NP_061185.1. NM_018715.3.
UniGeneiHs.380857.

Genome annotation databases

EnsembliENST00000375433; ENSP00000364582; ENSG00000179051.
ENST00000375436; ENSP00000364585; ENSG00000179051.
GeneIDi55920.
KEGGihsa:55920.
UCSCiuc001bal.3. human.

Polymorphism databases

DMDMi71152033.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS181.1.
PIRi T50630.
RefSeqi NP_001129676.1. NM_001136204.2.
NP_061185.1. NM_018715.3.
UniGenei Hs.380857.

3D structure databases

ProteinModelPortali Q9P258.
SMRi Q9P258. Positions 101-503.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121001. 17 interactions.
IntActi Q9P258. 6 interactions.
MINTi MINT-3037281.
STRINGi 9606.ENSP00000364582.

PTM databases

PhosphoSitei Q9P258.

Polymorphism databases

DMDMi 71152033.

2D gel databases

SWISS-2DPAGE Q9P258.

Proteomic databases

MaxQBi Q9P258.
PaxDbi Q9P258.
PeptideAtlasi Q9P258.
PRIDEi Q9P258.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375433 ; ENSP00000364582 ; ENSG00000179051 .
ENST00000375436 ; ENSP00000364585 ; ENSG00000179051 .
GeneIDi 55920.
KEGGi hsa:55920.
UCSCi uc001bal.3. human.

Organism-specific databases

CTDi 55920.
GeneCardsi GC01M017733.
HGNCi HGNC:30297. RCC2.
HPAi HPA056177.
MIMi 609587. gene.
neXtProti NX_Q9P258.
PharmGKBi PA142671091.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5184.
GeneTreei ENSGT00770000120483.
HOGENOMi HOG000232061.
HOVERGENi HBG080538.
InParanoidi Q9P258.
OMAi VDCKGNL.
OrthoDBi EOG7TTQ7B.
PhylomeDBi Q9P258.
TreeFami TF101168.

Enzyme and pathway databases

Reactomei REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_682. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSi RCC2. human.
GeneWikii RCC2.
GenomeRNAii 55920.
NextBioi 61323.
PROi Q9P258.
SOURCEi Search...

Gene expression databases

Bgeei Q9P258.
CleanExi HS_RCC2.
Genevestigatori Q9P258.

Family and domain databases

Gene3Di 2.130.10.30. 1 hit.
InterProi IPR009091. RCC1/BLIP-II.
IPR028641. RCC2.
IPR000408. Reg_chr_condens.
[Graphical view ]
PANTHERi PTHR22870:SF146. PTHR22870:SF146. 1 hit.
Pfami PF00415. RCC1. 4 hits.
[Graphical view ]
PRINTSi PR00633. RCCNDNSATION.
SUPFAMi SSF50985. SSF50985. 1 hit.
PROSITEi PS00626. RCC1_2. 2 hits.
PS50012. RCC1_3. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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].

Entry informationi

Entry nameiRCC2_HUMAN
AccessioniPrimary (citable) accession number: Q9P258
Secondary accession number(s): Q8IVL9, Q9BSN6, Q9NPV8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: November 26, 2014
This is version 119 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3