Skip Header

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

Cell division cycle protein 123 homolog

Gene

Cdc123

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Required for S phase entry of the cell cycle.

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division cycle protein 123 homolog
Short name:
Protein D123
Gene namesi
Name:Cdc123
Synonyms:D123
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi619766. Cdc123.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Cell division cycle protein 123 homologPRO_0000228665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated.1 Publication
The Val-109 variant is degraded by the proteasome suggesting that it is polyubiquitinated.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ62834.

Expressioni

Tissue specificityi

Frequently detected in granular vesicles, in the cytoplasm of some epithelial, stromal and sperm cells and in varicosities lining nervous fibers, while it appears to be absent in endothelial and smooth muscle cells (at protein level). Widely expressed. Expressed at high level in testis.1 Publication

Gene expression databases

ExpressionAtlasiQ62834. baseline and differential.
GenevisibleiQ62834. RN.

Family & Domainsi

Sequence similaritiesi

Belongs to the CDC123 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000003057.
HOGENOMiHOG000231938.
HOVERGENiHBG080491.
InParanoidiQ62834.
OrthoDBiEOG7673B4.
PhylomeDBiQ62834.
TreeFamiTF323348.

Family and domain databases

InterProiIPR009772. CDC123.
[Graphical view]
PANTHERiPTHR15323:SF6. PTHR15323:SF6. 1 hit.
PfamiPF07065. D123. 1 hit.
[Graphical view]
PIRSFiPIRSF007807. Cdc123. 1 hit.

Sequencei

Sequence statusi: Complete.

Q62834-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKEHVSHCQ FSAWYPLFRS LTIKSVILPL PQNVKDYLLD DGTLVVSGRE
60 70 80 90 100
DPPTCSQPDS GDEAEETQWS DDESTATLTA PEFPEFNTQV QEAINSLGGS
110 120 130 140 150
VFPKLNWSAP RDAYWIAMNS SLKCKSLSDI FLLFKSSDFI THDFTQPFIH
160 170 180 190 200
CNDDSPDPCI EYELVLRKWC ELIPGAEFRC FVKENKLIGI SQRDYTQYYD
210 220 230 240 250
HISKQKEEIC RCIQDFFKEH LQYKFLDEDF VFDIYRDSRG KVWLIDFNPF
260 270 280 290 300
GEVTDSLLFT WEELTSENNL RGDVSEADAL EQDSPAFRCT NSEVTVQPSP
310 320 330
YLSYGLPKDF VDLSTGEDAH KLIDFLKLKR NQQEDD
Length:336
Mass (Da):38,812
Last modified:November 1, 1996 - v1
Checksum:i6E1D1379A2612934
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti109 – 1091A → V in 3Y1tsD123 cell line; reversibly arrested in G1 phase of cell cycle at the restrictive temperature of 39.8 degrees Celsius; due to extensive degradation by the proteasome. 3 Publications

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34843 mRNA. Translation: AAB60521.1.
BC061527 mRNA. Translation: AAH61527.1.
RefSeqiNP_446329.1. NM_053877.3.
UniGeneiRn.11096.

Genome annotation databases

EnsembliENSRNOT00000024016; ENSRNOP00000024016; ENSRNOG00000017770.
GeneIDi116656.
KEGGirno:116656.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34843 mRNA. Translation: AAB60521.1.
BC061527 mRNA. Translation: AAH61527.1.
RefSeqiNP_446329.1. NM_053877.3.
UniGeneiRn.11096.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ62834.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024016; ENSRNOP00000024016; ENSRNOG00000017770.
GeneIDi116656.
KEGGirno:116656.

Organism-specific databases

CTDi8872.
RGDi619766. Cdc123.

Phylogenomic databases

GeneTreeiENSGT00390000003057.
HOGENOMiHOG000231938.
HOVERGENiHBG080491.
InParanoidiQ62834.
OrthoDBiEOG7673B4.
PhylomeDBiQ62834.
TreeFamiTF323348.

Miscellaneous databases

PROiQ62834.

Gene expression databases

ExpressionAtlasiQ62834. baseline and differential.
GenevisibleiQ62834. RN.

Family and domain databases

InterProiIPR009772. CDC123.
[Graphical view]
PANTHERiPTHR15323:SF6. PTHR15323:SF6. 1 hit.
PfamiPF07065. D123. 1 hit.
[Graphical view]
PIRSFiPIRSF007807. Cdc123. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "An amino acid change in novel protein D123 is responsible for temperature-sensitive G1-phase arrest in a mutant of rat fibroblast line 3Y1."
    Okuda A., Kimura G.
    Exp. Cell Res. 223:242-249(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-109.
    Strain: Fischer.
  2. "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: Pituitary.
  3. "Expression study on D123 gene product: evidence for high positivity in testis."
    Onisto M., Zeilante P., Scannapieco P., Pellati D., Pozza M., Caenazzo C., Negro A., Garbisa S.
    Exp. Cell Res. 242:451-459(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Extensive degradation of mutant-type D123 protein is responsible for temperature-sensitive proliferation inhibition in 3Y1tsD123 cells."
    Okuda A., Ohtsu M., Kimura G.
    Cell Struct. Funct. 24:443-449(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEGRADATION OF VARIANT VAL-109.
  5. "Reversion of temperature-sensitive mutation by inhibition of proteasome-mediated degradation of mutated D123 protein."
    Okuda A., Ohtsu M., Kimura G.
    Cell Struct. Funct. 26:205-214(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEGRADATION OF VARIANT VAL-109, PHOSPHORYLATION.

Entry informationi

Entry nameiCD123_RAT
AccessioniPrimary (citable) accession number: Q62834
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 89 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. 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.