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Protein

CDK5 regulatory subunit-associated protein 2

Gene

Cdk5rap2

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

Functioni

Potential regulator of CDK5 activity via its interaction with CDK5R1. Involved in regulation of mitotic spindle orientation (By similarity). Negative regulator of centriole disengagement (licensing) which maintains centriole engagement and cohesion. Involved in regulation of mitotic spindle orientation and brain development. Regulates centrosomal maturation by recruitment of a gamma-tubulin ring complex onto centrosomes (By similarity).By similarity3 Publications

GO - Molecular functioni

GO - Biological processi

  • brain development Source: UniProtKB
  • centriole replication Source: MGI
  • centrosome organization Source: UniProtKB
  • chromosome segregation Source: UniProtKB
  • establishment of mitotic spindle orientation Source: UniProtKB
  • microtubule bundle formation Source: UniProtKB
  • microtubule cytoskeleton organization Source: MGI
  • microtubule organizing center organization Source: UniProtKB
  • negative regulation of centriole replication Source: UniProtKB
  • negative regulation of neuron differentiation Source: UniProtKB
  • neurogenesis Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of spindle checkpoint Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-8854518. AURKA Activation by TPX2.

Names & Taxonomyi

Protein namesi
Recommended name:
CDK5 regulatory subunit-associated protein 2
Alternative name(s):
CDK5 activator-binding protein C48
Gene namesi
Name:Cdk5rap2
Synonyms:Kiaa1633
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2384875. Cdk5rap2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000898371 – 1822CDK5 regulatory subunit-associated protein 2Add BLAST1822

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei485PhosphoserineCombined sources1
Modified residuei544PhosphoserineBy similarity1
Modified residuei1195PhosphothreonineCombined sources1
Modified residuei1243PhosphoserineBy similarity1
Modified residuei1245PhosphoserineCombined sources1
Modified residuei1497PhosphoserineCombined sources1
Modified residuei1822PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated in vitro by CDK5.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8K389.
MaxQBiQ8K389.
PaxDbiQ8K389.
PRIDEiQ8K389.

PTM databases

iPTMnetiQ8K389.
PhosphoSitePlusiQ8K389.

Expressioni

Tissue specificityi

Expressed in testis, thymus, heart and brain.1 Publication

Developmental stagei

Expressed from E9.5 in the developing cortex. Its expression peaks during periods of active neurogenesis.2 Publications

Gene expression databases

BgeeiENSMUSG00000039298.
CleanExiMM_CDK5RAP2.
ExpressionAtlasiQ8K389. baseline and differential.
GenevisibleiQ8K389. MM.

Interactioni

Subunit structurei

Interacts with CDK5R1 (p35 form) (By similarity). CDK5RAP1, CDK5RAP2 and CDK5RAP3 show competitive binding to CDK5R1. Probably forms a complex with CDK5R1 and CDK5 (By similarity). Interacts with PCNT; the interaction is leading to centrosomal localization of CDK5RAP2 and PCNT. Interacts with AKAP9; the interaction is leading to Golgi localization of CDK5RAP2 and AKAP9 (By similarity). Interacts with TUBG1; the interaction is leading to centrosomal localization of CDK5RAP2 and TUBG1. Interacts with TUBGCP3 (By similarity). Interacts with CALM1 (By similarity). Interacts with CDC20 (By similarity). According to PubMed:19553473, CDK5RAP2 does not interact with MAPRE1. Interacts with CEP68; degradation of CEP68 in early mitosis leads to removal of CDK5RAP2 from the centrosome which promotes centriole disengagement and subsequent centriole separation. Interacts with NCKAP5L (By similarity).By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi229527. 19 interactors.
IntActiQ8K389. 20 interactors.
STRINGi10090.ENSMUSP00000119891.

Structurei

3D structure databases

ProteinModelPortaliQ8K389.
SMRiQ8K389.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni57 – 195Interaction with NCKAP5LBy similarityAdd BLAST139
Regioni1201 – 1822Interaction with PCNT and AKAP91 PublicationAdd BLAST622
Regioni1655 – 1822Required for centrosomal attachment, Golgi targeting and CALM1 interactionBy similarityAdd BLAST168
Regioni1655 – 1697Interaction with CDK5R1By similarityAdd BLAST43
Regioni1790 – 1799Required for centrosomal attachment, Golgi localization and CALM1 interactionBy similarity10

Phylogenomic databases

eggNOGiENOG410J2NR. Eukaryota.
ENOG411281S. LUCA.
GeneTreeiENSGT00530000063845.
HOVERGENiHBG050976.
InParanoidiQ8K389.
KOiK16542.
OMAiPEPSASH.
OrthoDBiEOG091G008W.
PhylomeDBiQ8K389.
TreeFamiTF329233.

Family and domain databases

InterProiIPR012943. Cnn_1N.
[Graphical view]
PfamiPF07989. Cnn_1N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K389-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSGMEEEGA LPGTLSGCSG LHPVLPSDLD VISDTSGLGN GVLPSMSEEK
60 70 80 90 100
VSPTRARNMK DFENQITELK KENFNLKLRI YFLEERIQQE FAGPTEHIYK
110 120 130 140 150
TNIELKVEVE SLKRELQEKD QLLVKASKAV ESLAERGGSE VQRVKEDARK
160 170 180 190 200
KVQQVEDLLT KRIHLLEEDV KAAQAELEKA FAGTETEKAL RLSLESKLSA
210 220 230 240 250
MKKMQEGDLE MTLALEEKDR LIEELKLSLK SKEALIQCLK EEKSQMASPD
260 270 280 290 300
ENVSSGELRG LSATLREEKE RDAEEWQKER NHFEERIQAL QEDLREKERE
310 320 330 340 350
IATEKKNNLK SYKAIQGLTM ALKSKEREVE ELDSKIKEVT TDSTKGREDP
360 370 380 390 400
LKTQIPRFQL REGSEDCEAA LVEKEALLAK LHSENVTKST ENHRLLRNVK
410 420 430 440 450
KVTQELNDLK KEKLRLEQAL EEAHQEGNRG ARTIHDLRNE VEKLRKEVSE
460 470 480 490 500
REKAVEKHYK SLPGESKTKF HTQEQVVRSL TGSGSQEDLL LQKSNEKDLE
510 520 530 540 550
AIQQNCYLMT AEELKFGSDG LITEKCSQQS PDSKLIFSKE KQQSEYEGLT
560 570 580 590 600
GDLKAEQNIY AHLAKTQDTD SVSNLQAELK EVLALRKQLE QDVLAYRNLQ
610 620 630 640 650
KALQEQLSEI RSREEEPFSF YSDQTSYLSI CLEEHNQFQL EHFSQEELKK
660 670 680 690 700
KVSDLIQLVK DLHTDNQHLK KTIFDLSSVG FQGSDRLELT KQEELVASKE
710 720 730 740 750
DEDTLKFEAD VETPFQSDQH LEQSREIMED YAEGGCKSGY GRHMDSNILG
760 770 780 790 800
HDGAQTPGAS EEHTLEDELL GLLATLFSKK ATPLLESRPD LLKALGALLL
810 820 830 840 850
ERICLAEQGR PGDHLDSKTE KALQQVAVQL RDELGHSFPA NSFSKSYNEV
860 870 880 890 900
KSMWGNWLVK TGDEDTVELK SVSVQTMAIE DTPHGFKPQS KRDAWAEKQE
910 920 930 940 950
EAIFSTELES EALGEMPGQQ ATHLSFPSAI NPDAEKTGLL IQLKTPELLE
960 970 980 990 1000
NLYNLPASPE VVVAQLQGQV LELQRELKEF KTRNKQLHEK LILAEAMMEG
1010 1020 1030 1040 1050
LPVPNSALVN VPAAQAVVRT AFQDNPGEQE GPETTQSAGR DKDMDSDQYT
1060 1070 1080 1090 1100
SFEIDSEICP PDDLALLPAC KENLEDLLGP SSIATYLDSK SQLSVKVSVN
1110 1120 1130 1140 1150
GTDQSENINI PDDTEDLKQK IHDLQTELEG YRNIIVQLLK HSQCSEAIIT
1160 1170 1180 1190 1200
VLCGTEGAQD GLNKPKGHID EEEMTFSSLH QVRYVKHMKI LRPLTPEMID
1210 1220 1230 1240 1250
GKMLESLKQQ LVDQEQELQK EQDLNLELFG EIHDLQNKFQ DLSPSRYDSL
1260 1270 1280 1290 1300
VQSQARELSL QRQQIKDSHG ICVIYRQHMS TMIKAFEELL QASDVDSCVA
1310 1320 1330 1340 1350
EGFREQLTQC AGLLEQLERL FLHGKSARVE PHPQNELLKG LRTVEGNLPY
1360 1370 1380 1390 1400
HHLLPESPEP SASHALSDDE MSEKSFLSRD PKPDSDTEKY PAMASHFPQD
1410 1420 1430 1440 1450
LLMEHIQEIR TLRKHLEESI KTNEKLRKQL ERQGSETDQG SRNVSACGLA
1460 1470 1480 1490 1500
LHSSLTSEIH FLRKQNEALS MMLEKGSKDK QKESEKLRES LARKAESLEQ
1510 1520 1530 1540 1550
LQLEYTSVRE ENERLQRDII EKERHNQELT EEVCSSRQEL SRVQEEAKSR
1560 1570 1580 1590 1600
QQLLSQKDKL LQSLQMELKV YEKLAEEHPR LQQDGSKCPE ASDNSFDLFE
1610 1620 1630 1640 1650
STQAMAPKSA SETPLLSGTD VDSLSCDSTS SATSPTSMPC LVAGHHMWAS
1660 1670 1680 1690 1700
KSGHHMLGLI EDYDALYKQI SWGQTLLAKM DVQTQEALSP TSHKLGPKGS
1710 1720 1730 1740 1750
SSVPLSKFLS SMNTAKLVLE KASRLLKLFW RVSVPTNGQC SLHCEQIGEM
1760 1770 1780 1790 1800
KAENTKLHKK LFEQEKKLQN TAKLLQQSKH QEKVIFDQLV ITHQVLRKAR
1810 1820
GNLELRPGAT RPGASSPSRP GS
Length:1,822
Mass (Da):205,945
Last modified:December 20, 2005 - v3
Checksum:iDDD6CD7B8CFC8DA9
GO

Sequence cautioni

The sequence BAC98221 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129411 mRNA. Translation: BAC98221.1. Different initiation.
AL929409, AL845502 Genomic DNA. Translation: CAM23429.1.
BC059253 mRNA. Translation: AAH59253.1.
CCDSiCCDS38779.1.
RefSeqiNP_666102.2. NM_145990.4.
UniGeneiMm.370777.
Mm.379344.

Genome annotation databases

EnsembliENSMUST00000144099; ENSMUSP00000119891; ENSMUSG00000039298.
GeneIDi214444.
KEGGimmu:214444.
UCSCiuc008thy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129411 mRNA. Translation: BAC98221.1. Different initiation.
AL929409, AL845502 Genomic DNA. Translation: CAM23429.1.
BC059253 mRNA. Translation: AAH59253.1.
CCDSiCCDS38779.1.
RefSeqiNP_666102.2. NM_145990.4.
UniGeneiMm.370777.
Mm.379344.

3D structure databases

ProteinModelPortaliQ8K389.
SMRiQ8K389.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229527. 19 interactors.
IntActiQ8K389. 20 interactors.
STRINGi10090.ENSMUSP00000119891.

PTM databases

iPTMnetiQ8K389.
PhosphoSitePlusiQ8K389.

Proteomic databases

EPDiQ8K389.
MaxQBiQ8K389.
PaxDbiQ8K389.
PRIDEiQ8K389.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000144099; ENSMUSP00000119891; ENSMUSG00000039298.
GeneIDi214444.
KEGGimmu:214444.
UCSCiuc008thy.1. mouse.

Organism-specific databases

CTDi55755.
MGIiMGI:2384875. Cdk5rap2.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410J2NR. Eukaryota.
ENOG411281S. LUCA.
GeneTreeiENSGT00530000063845.
HOVERGENiHBG050976.
InParanoidiQ8K389.
KOiK16542.
OMAiPEPSASH.
OrthoDBiEOG091G008W.
PhylomeDBiQ8K389.
TreeFamiTF329233.

Enzyme and pathway databases

ReactomeiR-MMU-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-MMU-380259. Loss of Nlp from mitotic centrosomes.
R-MMU-380270. Recruitment of mitotic centrosome proteins and complexes.
R-MMU-5620912. Anchoring of the basal body to the plasma membrane.
R-MMU-8854518. AURKA Activation by TPX2.

Miscellaneous databases

ChiTaRSiCdk5rap2. mouse.
PROiQ8K389.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000039298.
CleanExiMM_CDK5RAP2.
ExpressionAtlasiQ8K389. baseline and differential.
GenevisibleiQ8K389. MM.

Family and domain databases

InterProiIPR012943. Cnn_1N.
[Graphical view]
PfamiPF07989. Cnn_1N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCK5P2_MOUSE
AccessioniPrimary (citable) accession number: Q8K389
Secondary accession number(s): A2AVA1, Q6PCN1, Q6ZPL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: December 20, 2005
Last modified: November 2, 2016
This is version 107 of the entry and version 3 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

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.