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Protein

CDK5 regulatory subunit-associated protein 3

Gene

Cdk5rap3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable tumor suppressor initially identified as a CDK5R1 interactor controlling cell proliferation. Negatively regulates NF-kappa-B-mediated gene transcription through the control of RELA phosphorylation. Also regulates mitotic G2/M transition checkpoint and mitotic G2 DNA damage checkpoint. Through its interaction with CDKN2A/ARF and MDM2 may induce MDM2-dependent p53/TP53 ubiquitination, stabilization and activation in the nucleus, thereby promoting G1 cell cycle arrest and inhibition of cell proliferation. May play a role in the unfolded protein response, mediating the ufmylation of multiple proteins in response to endoplasmic reticulum stress. May also play a role in the rupture of the nuclear envelope during apoptosis. May regulate MAPK14 activity by regulating its dephosphorylation by PPM1D/WIP1.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
CDK5 regulatory subunit-associated protein 3Curated
Gene namesi
Name:Cdk5rap3Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1933126. Cdk5rap3.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity

  • Note: Colocalizes and associates with microtubules.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503CDK5 regulatory subunit-associated protein 3PRO_0000220517Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki447 – 447Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

May be phosphorylated by CDK5.By similarity
May be ufmylated.1 Publication
Ubiquitinated. Probably triggers proteasomal degradation and is negatively regulated by UFL1.By similarity
Cleaved by caspases early during apoptosis, the resulting peptides may play a role in rupture of the nuclear envelope.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ99LM2.
MaxQBiQ99LM2.
PaxDbiQ99LM2.
PRIDEiQ99LM2.

PTM databases

iPTMnetiQ99LM2.
PhosphoSiteiQ99LM2.

Expressioni

Tissue specificityi

Widely expressed with higher expression in secretory tissues.1 Publication

Gene expression databases

BgeeiQ99LM2.
CleanExiMM_CDK5RAP3.
ExpressionAtlasiQ99LM2. baseline and differential.
GenevisibleiQ99LM2. MM.

Interactioni

Subunit structurei

Interacts with CDK5R1; competes with CDK5RAP1 and CDK5RAP2. Interacts with RELA. Interacts with CHEK1; may negatively regulate CHEK1 and thereby stimulate entry into mitosis. Interacts with CDKN2A/ARF and MDM2; forms a ternary complex involved in regulation of p53/TP53 (By similarity). Interacts with UFL1; the interaction is direct (PubMed:21494687). Interacts with DDRGK1. Interacts with MAPK14. Interacts with CCNB1. Interacts with TUBG1; may regulate CDK5RAP3 in mitotic G2/M transition checkpoint (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ99LM2. 1 interaction.
STRINGi10090.ENSMUSP00000099441.

Structurei

3D structure databases

ProteinModelPortaliQ99LM2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni268 – 503236Required for interaction with UFL1 and mediates interaction with CHEK1By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the CDK5RAP3 family.Curated

Phylogenomic databases

eggNOGiKOG2607. Eukaryota.
ENOG410XSWB. LUCA.
GeneTreeiENSGT00390000000713.
HOGENOMiHOG000231047.
HOVERGENiHBG050978.
InParanoidiQ99LM2.
OMAiEIPIDIH.
OrthoDBiEOG7ZKS9X.
PhylomeDBiQ99LM2.

Family and domain databases

InterProiIPR008491. DUF773.
[Graphical view]
PANTHERiPTHR14894. PTHR14894. 1 hit.
PfamiPF05600. DUF773. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99LM2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQDHQHVPID IQTSKLLDWL VDRRHCNLKW QSLVLTIREK INTAIQDMPE
60 70 80 90 100
SQEIAQLLSG SYIHYFHCLR IVDLLKGTEA STKNIFGRYS SQRMKDWQEI
110 120 130 140 150
VSLYEKDNTY LVELCSLLVR NVSYEIPSLK KQIAKCQQLQ QEYSRKEEEG
160 170 180 190 200
QAGAAEMREQ FYHSCKQYGI TGDNVRRELL ALVKDLPSQL AEIGAGAQSL
210 220 230 240 250
GEAIDLYQAC VEFVCDSPTE QVLPMLRYVQ KKGNSTVYEW RTGTEPSVVE
260 270 280 290 300
RPQLEEPPEQ VQEDEIDWGD FGVEAVSDSG IVAETPGIDW GISLESEAKD
310 320 330 340 350
AGADKIDWGD DAAAASEITV LETGTEAPEG VARGSDALTL LEYPETRNQF
360 370 380 390 400
IDELMELEIF LSQRAVEMSE EADILSVSQF QLAPAILQGQ TKEKMLSLVS
410 420 430 440 450
TLQQLIGRLT SLRMQHLFMI LASPRYVDRV TEFLQQKLKQ SQLLALKKEL
460 470 480 490 500
MVEKQQEALQ EQAALEPKLD LLLEKTRELQ KLIEADISKR YSGRPVNLMG

TSL
Length:503
Mass (Da):56,991
Last modified:June 1, 2001 - v1
Checksum:i61428829BAB406E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075771 mRNA. Translation: BAC35945.1.
AK075791 mRNA. Translation: BAC35961.1.
AK077853 mRNA. Translation: BAC37034.1.
AK149765 mRNA. Translation: BAE29070.1.
BC002318 mRNA. Translation: AAH02318.1.
CCDSiCCDS25306.1.
RefSeqiNP_084524.1. NM_030248.2.
UniGeneiMm.28297.
Mm.404690.

Genome annotation databases

EnsembliENSMUST00000103152; ENSMUSP00000099441; ENSMUSG00000018669.
GeneIDi80280.
KEGGimmu:80280.
UCSCiuc007lcv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075771 mRNA. Translation: BAC35945.1.
AK075791 mRNA. Translation: BAC35961.1.
AK077853 mRNA. Translation: BAC37034.1.
AK149765 mRNA. Translation: BAE29070.1.
BC002318 mRNA. Translation: AAH02318.1.
CCDSiCCDS25306.1.
RefSeqiNP_084524.1. NM_030248.2.
UniGeneiMm.28297.
Mm.404690.

3D structure databases

ProteinModelPortaliQ99LM2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99LM2. 1 interaction.
STRINGi10090.ENSMUSP00000099441.

PTM databases

iPTMnetiQ99LM2.
PhosphoSiteiQ99LM2.

Proteomic databases

EPDiQ99LM2.
MaxQBiQ99LM2.
PaxDbiQ99LM2.
PRIDEiQ99LM2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103152; ENSMUSP00000099441; ENSMUSG00000018669.
GeneIDi80280.
KEGGimmu:80280.
UCSCiuc007lcv.1. mouse.

Organism-specific databases

CTDi80279.
MGIiMGI:1933126. Cdk5rap3.

Phylogenomic databases

eggNOGiKOG2607. Eukaryota.
ENOG410XSWB. LUCA.
GeneTreeiENSGT00390000000713.
HOGENOMiHOG000231047.
HOVERGENiHBG050978.
InParanoidiQ99LM2.
OMAiEIPIDIH.
OrthoDBiEOG7ZKS9X.
PhylomeDBiQ99LM2.

Miscellaneous databases

NextBioi349961.
PROiQ99LM2.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LM2.
CleanExiMM_CDK5RAP3.
ExpressionAtlasiQ99LM2. baseline and differential.
GenevisibleiQ99LM2. MM.

Family and domain databases

InterProiIPR008491. DUF773.
[Graphical view]
PANTHERiPTHR14894. PTHR14894. 1 hit.
PfamiPF05600. DUF773. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    Tissue: Bone marrow, Forelimb and Pancreas.
  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: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "Ubiquitin fold modifier 1 (UFM1) and its target UFBP1 protect pancreatic beta cells from ER stress-induced apoptosis."
    Lemaire K., Moura R.F., Granvik M., Igoillo-Esteve M., Hohmeier H.E., Hendrickx N., Newgard C.B., Waelkens E., Cnop M., Schuit F.
    PLoS ONE 6:E18517-E18517(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UFL1, UFMYLATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCK5P3_MOUSE
AccessioniPrimary (citable) accession number: Q99LM2
Secondary accession number(s): Q3UE41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 101 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.