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Protein

Protein RCC2

Gene

RCC2

Organism
Homo sapiens (Human)
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 RAC1.1 Publication

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • Rac GTPase binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • small GTPase binding Source: UniProtKB

GO - Biological processi

  • activation of GTPase activity Source: Ensembl
  • cell division Source: UniProtKB-KW
  • chromosome passenger complex localization to kinetochore Source: UniProtKB
  • establishment of protein localization Source: Ensembl
  • focal adhesion assembly Source: UniProtKB
  • integrin-mediated signaling pathway Source: UniProtKB
  • 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: UniProtKB
  • positive regulation of G2/M transition of mitotic cell cycle Source: UniProtKB
  • regulation of cell migration Source: UniProtKB
  • regulation of fibroblast migration Source: Ensembl
  • regulation of ruffle assembly Source: Ensembl
  • sister chromatid cohesion Source: Reactome

Keywordsi

Biological processCell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-HSA-141444. Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000179051.13.
HGNCiHGNC:30297. RCC2.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Microtubule, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi55920.
OpenTargetsiENSG00000179051.
PharmGKBiPA142671091.

Polymorphism and mutation databases

BioMutaiRCC2.
DMDMi71152033.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002066521 – 522Protein RCC2Add BLAST522

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16PhosphoserineCombined sources1
Modified residuei20PhosphothreonineCombined sources1
Modified residuei43PhosphoserineCombined sources1
Modified residuei44PhosphoserineCombined sources1
Modified residuei45PhosphoserineCombined sources1
Modified residuei46PhosphoserineCombined sources1
Modified residuei50PhosphoserineCombined sources1
Modified residuei51PhosphoserineCombined sources1
Modified residuei92N6-acetyllysineCombined sources1
Modified residuei124N6-acetyllysineBy similarity1
Modified residuei293N6-acetyllysineCombined sources1
Modified residuei342PhosphothreonineCombined sources1
Modified residuei377N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9P258.
MaxQBiQ9P258.
PaxDbiQ9P258.
PeptideAtlasiQ9P258.
PRIDEiQ9P258.

2D gel databases

SWISS-2DPAGEiQ9P258.

PTM databases

iPTMnetiQ9P258.
PhosphoSitePlusiQ9P258.
SwissPalmiQ9P258.

Expressioni

Gene expression databases

BgeeiENSG00000179051.
CleanExiHS_RCC2.
ExpressionAtlasiQ9P258. baseline and differential.
GenevisibleiQ9P258. HS.

Organism-specific databases

HPAiHPA072281.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • microtubule binding Source: UniProtKB
  • protein domain specific binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • Rac GTPase binding Source: UniProtKB
  • small GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121001. 49 interactors.
IntActiQ9P258. 18 interactors.
MINTiMINT-3037281.
STRINGi9606.ENSP00000364582.

Structurei

Secondary structure

1522
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi104 – 111Combined sources8
Turni114 – 118Combined sources5
Beta strandi119 – 121Combined sources3
Helixi124 – 129Combined sources6
Beta strandi135 – 142Combined sources8
Helixi143 – 145Combined sources3
Beta strandi150 – 154Combined sources5
Beta strandi160 – 166Combined sources7
Beta strandi171 – 175Combined sources5
Beta strandi184 – 186Combined sources3
Beta strandi190 – 195Combined sources6
Helixi197 – 199Combined sources3
Beta strandi204 – 209Combined sources6
Beta strandi211 – 218Combined sources8
Beta strandi223 – 229Combined sources7
Beta strandi236 – 238Combined sources3
Beta strandi240 – 248Combined sources9
Beta strandi256 – 261Combined sources6
Beta strandi263 – 270Combined sources8
Beta strandi275 – 279Combined sources5
Helixi282 – 284Combined sources3
Beta strandi287 – 289Combined sources3
Beta strandi306 – 311Combined sources6
Beta strandi316 – 318Combined sources3
Beta strandi324 – 326Combined sources3
Beta strandi332 – 337Combined sources6
Beta strandi339 – 346Combined sources8
Beta strandi351 – 355Combined sources5
Helixi358 – 360Combined sources3
Beta strandi364 – 366Combined sources3
Beta strandi370 – 375Combined sources6
Helixi377 – 380Combined sources4
Beta strandi386 – 392Combined sources7
Beta strandi395 – 400Combined sources6
Beta strandi405 – 409Combined sources5
Turni413 – 415Combined sources3
Beta strandi418 – 423Combined sources6
Helixi425 – 427Combined sources3
Beta strandi432 – 437Combined sources6
Beta strandi442 – 446Combined sources5
Beta strandi449 – 454Combined sources6
Beta strandi472 – 477Combined sources6
Helixi479 – 481Combined sources3
Beta strandi486 – 491Combined sources6
Beta strandi493 – 501Combined sources9
Helixi505 – 513Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GWNX-ray1.31A89-522[»]
ProteinModelPortaliQ9P258.
SMRiQ9P258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati103 – 165RCC1 1Add BLAST63
Repeati168 – 219RCC1 2Add BLAST52
Repeati221 – 271RCC1 3Add BLAST51
Repeati273 – 347RCC1 4Add BLAST75
Repeati348 – 401RCC1 5Add BLAST54
Repeati403 – 447RCC1 6Add BLAST45
Repeati448 – 501RCC1 7Add BLAST54

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1427. Eukaryota.
COG5184. LUCA.
GeneTreeiENSGT00900000140783.
HOGENOMiHOG000232061.
HOVERGENiHBG080538.
InParanoidiQ9P258.
OMAiVDCKGNL.
OrthoDBiEOG091G07AD.
PhylomeDBiQ9P258.
TreeFamiTF101168.

Family and domain databases

Gene3Di2.130.10.30. 2 hits.
InterProiView protein in InterPro
IPR009091. RCC1/BLIP-II.
IPR000408. Reg_chr_condens.
PfamiView protein in Pfam
PF00415. RCC1. 4 hits.
PRINTSiPR00633. RCCNDNSATION.
SUPFAMiSSF50985. SSF50985. 1 hit.
PROSITEiView protein in PROSITE
PS00626. RCC1_2. 2 hits.
PS50012. RCC1_3. 5 hits.

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti145 – 148LAGV → RTRG (PubMed:17974005).Curated4

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.
ENST00000628984; ENSP00000486099; ENSG00000281540.
ENST00000631021; ENSP00000486447; ENSG00000281540.
GeneIDi55920.
KEGGihsa:55920.
UCSCiuc001bal.4. human.

Similar proteinsi

Entry informationi

Entry nameiRCC2_HUMAN
AccessioniPrimary (citable) accession number: Q9P258
Secondary accession number(s): Q8IVL9, Q9BSN6, Q9NPV8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: November 22, 2017
This is version 151 of the entry and version 2 of the sequence. See 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references