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Protein

Protein RCC2

Gene

Rcc2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • activation of GTPase activity Source: UniProtKB
  • cell division Source: UniProtKB-KW
  • chromosome passenger complex localization to kinetochore Source: MGI
  • establishment of protein localization Source: UniProtKB
  • focal adhesion assembly Source: MGI
  • integrin-mediated signaling pathway Source: MGI
  • mitotic nuclear division Source: UniProtKB-KW
  • negative regulation of focal adhesion assembly Source: UniProtKB
  • negative regulation of GTPase activity Source: UniProtKB
  • negative regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • positive regulation of attachment of spindle microtubules to kinetochore Source: MGI
  • positive regulation of G2/M transition of mitotic cell cycle Source: MGI
  • regulation of cell migration Source: UniProtKB
  • regulation of fibroblast migration Source: UniProtKB
  • regulation of ruffle assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein RCC2
Gene namesi
Name:Rcc2
Synonyms:Kiaa1470
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1919784. Rcc2.

Subcellular locationi

  • Nucleusnucleolus By similarity
  • Chromosomecentromere By similarity
  • Cytoplasmcytoskeletonspindle By similarity

  • 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 (By similarity).By similarity

GO - Cellular componenti

  • chromosome, centromeric core domain Source: MGI
  • early endosome membrane Source: UniProtKB
  • microtubule Source: UniProtKB-KW
  • midbody Source: MGI
  • mitotic spindle midzone Source: MGI
  • nucleolus Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Microtubule, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 520520Protein RCC2PRO_0000206653Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphoserineBy similarity
Modified residuei41 – 411PhosphoserineBy similarity
Modified residuei42 – 421PhosphoserineBy similarity
Modified residuei43 – 431PhosphoserineBy similarity
Modified residuei44 – 441PhosphoserineBy similarity
Modified residuei48 – 481PhosphoserineCombined sources
Modified residuei49 – 491PhosphoserineCombined sources
Modified residuei90 – 901N6-acetyllysineBy similarity
Modified residuei122 – 1221N6-acetyllysineCombined sources
Modified residuei291 – 2911N6-acetyllysineBy similarity
Modified residuei340 – 3401PhosphothreonineBy similarity
Modified residuei375 – 3751N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BK67.
MaxQBiQ8BK67.
PaxDbiQ8BK67.
PRIDEiQ8BK67.

PTM databases

PhosphoSiteiQ8BK67.

Expressioni

Gene expression databases

BgeeiQ8BK67.
CleanExiMM_RCC2.
ExpressionAtlasiQ8BK67. baseline and differential.
GenevisibleiQ8BK67. MM.

Interactioni

Subunit structurei

Binds preferentially to the nucleotide-free form of RAC1. Interacts with microtubules (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi224469. 1 interaction.
IntActiQ8BK67. 2 interactions.
MINTiMINT-4111085.
STRINGi10090.ENSMUSP00000038144.

Structurei

3D structure databases

ProteinModelPortaliQ8BK67.
SMRiQ8BK67. Positions 137-481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati101 – 16363RCC1 1Add
BLAST
Repeati166 – 21752RCC1 2Add
BLAST
Repeati219 – 26951RCC1 3Add
BLAST
Repeati271 – 34575RCC1 4Add
BLAST
Repeati346 – 39954RCC1 5Add
BLAST
Repeati401 – 44545RCC1 6Add
BLAST
Repeati446 – 49954RCC1 7Add
BLAST

Sequence similaritiesi

Contains 7 RCC1 repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1427. Eukaryota.
COG5184. LUCA.
GeneTreeiENSGT00840000129719.
HOGENOMiHOG000232061.
HOVERGENiHBG080538.
InParanoidiQ8BK67.
OMAiVDCKGNL.
OrthoDBiEOG7TTQ7B.
PhylomeDBiQ8BK67.
TreeFamiTF101168.

Family and domain databases

Gene3Di2.130.10.30. 1 hit.
InterProiIPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
[Graphical view]
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.

Q8BK67-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRKKGAAWE EPSSGNGTAR AGPRRRGGPA GRKRERPERC SSSSGGGSSG
60 70 80 90 100
DEDGPELDGA PGGGKRTARP ATAGKAAGAA AIITEPEHTK ERVKLEGSKC
110 120 130 140 150
KGQLLIFGAT NWDLIGRKEV PKQQAAYRNL GQNLWGPHRY GCLSGVRVRT
160 170 180 190 200
VVSGSCAAHS LLITTEGKLW SWGRNEKGQL GHGDTKRVEA PRLIEALSHE
210 220 230 240 250
AIVLAACGRN HTLALTDTGS VFAFGENKMG QLGLGNQTDA VPSPAQIMYN
260 270 280 290 300
GQPITKMACG AEFSMLMDCK GNLYSFGCPE YGQLGHNSDG KFIARAQRIE
310 320 330 340 350
YDCELVPRRV AIFIEKTKDG QILPVPNVVV RDVACGANHT LVLDSQKRVF
360 370 380 390 400
SWGFGGYGRL GHAEQKDEMV PRLVKLFDFP GRGATQIYAG YTCSFAVSEV
410 420 430 440 450
GGLFFWGATN TSRESTMYPK AVQDLCGWRI RSLACGKSSI IVAADESTIS
460 470 480 490 500
WGPSPTFGEL GYGDHKPKSS TAAQEVKTLD GIFSEQVAMG YSHSLVIARD
510 520
ESEAEKEKLQ RLPEYTPRTL
Length:520
Mass (Da):55,983
Last modified:March 1, 2003 - v1
Checksum:i06E7B90EA721C373
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK076040 mRNA. Translation: BAC36140.1.
AL954710 Genomic DNA. Translation: CAM19332.1.
BC086666 mRNA. Translation: AAH86666.1.
AK129370 mRNA. Translation: BAC98180.1.
CCDSiCCDS18852.1.
RefSeqiNP_776292.1. NM_173867.5.
XP_006538534.1. XM_006538471.2.
UniGeneiMm.253.

Genome annotation databases

EnsembliENSMUST00000038893; ENSMUSP00000038144; ENSMUSG00000040945.
ENSMUST00000071169; ENSMUSP00000071163; ENSMUSG00000040945.
GeneIDi108911.
KEGGimmu:108911.
UCSCiuc008vna.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK076040 mRNA. Translation: BAC36140.1.
AL954710 Genomic DNA. Translation: CAM19332.1.
BC086666 mRNA. Translation: AAH86666.1.
AK129370 mRNA. Translation: BAC98180.1.
CCDSiCCDS18852.1.
RefSeqiNP_776292.1. NM_173867.5.
XP_006538534.1. XM_006538471.2.
UniGeneiMm.253.

3D structure databases

ProteinModelPortaliQ8BK67.
SMRiQ8BK67. Positions 137-481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi224469. 1 interaction.
IntActiQ8BK67. 2 interactions.
MINTiMINT-4111085.
STRINGi10090.ENSMUSP00000038144.

PTM databases

PhosphoSiteiQ8BK67.

Proteomic databases

EPDiQ8BK67.
MaxQBiQ8BK67.
PaxDbiQ8BK67.
PRIDEiQ8BK67.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038893; ENSMUSP00000038144; ENSMUSG00000040945.
ENSMUST00000071169; ENSMUSP00000071163; ENSMUSG00000040945.
GeneIDi108911.
KEGGimmu:108911.
UCSCiuc008vna.2. mouse.

Organism-specific databases

CTDi55920.
MGIiMGI:1919784. Rcc2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1427. Eukaryota.
COG5184. LUCA.
GeneTreeiENSGT00840000129719.
HOGENOMiHOG000232061.
HOVERGENiHBG080538.
InParanoidiQ8BK67.
OMAiVDCKGNL.
OrthoDBiEOG7TTQ7B.
PhylomeDBiQ8BK67.
TreeFamiTF101168.

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-68877. Mitotic Prometaphase.

Miscellaneous databases

ChiTaRSiRcc2. mouse.
NextBioi361459.
PROiQ8BK67.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BK67.
CleanExiMM_RCC2.
ExpressionAtlasiQ8BK67. baseline and differential.
GenevisibleiQ8BK67. MM.

Family and domain databases

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

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 37-520.
    Tissue: Embryonic tail.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Pancreas, Spleen and Testis.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRCC2_MOUSE
AccessioniPrimary (citable) accession number: Q8BK67
Secondary accession number(s): A2AWQ3, Q6ZPQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.