Skip Header

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

Q96SN8

- CK5P2_HUMAN

UniProt

Q96SN8 - CK5P2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

CDK5 regulatory subunit-associated protein 2

Gene

CDK5RAP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Potential regulator of CDK5 activity via its interaction with CDK5R1. Negative regulator of centriole disengagement (licensing) which maintains centriole engagement and cohesion. Involved in regulation of mitotic spindle orientation By similarity. Plays a role in the spindle checkpoint activation by acting as a transcriptional regulator of both BUBR1 and MAD2 promoter. Together with MAPRE1, it may promote microtubule polymerization, bundle formation, growth and dynamics at the plus ends.By similarity4 Publications

GO - Molecular functioni

  1. calmodulin binding Source: UniProtKB
  2. microtubule binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. transcription regulatory region DNA binding Source: UniProtKB
  5. tubulin binding Source: UniProtKB

GO - Biological processi

  1. brain development Source: UniProtKB
  2. centrosome organization Source: UniProtKB
  3. chromosome segregation Source: UniProtKB
  4. establishment of mitotic spindle orientation Source: UniProtKB
  5. G2/M transition of mitotic cell cycle Source: Reactome
  6. microtubule bundle formation Source: UniProtKB
  7. microtubule cytoskeleton organization Source: UniProtKB
  8. mitotic cell cycle Source: Reactome
  9. negative regulation of centriole replication Source: UniProtKB
  10. negative regulation of neuron differentiation Source: Ensembl
  11. neurogenesis Source: UniProtKB
  12. positive regulation of transcription, DNA-templated Source: UniProtKB
  13. regulation of neuron differentiation Source: UniProtKB
  14. regulation of spindle checkpoint Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Names & Taxonomyi

Protein namesi
Recommended name:
CDK5 regulatory subunit-associated protein 2
Alternative name(s):
CDK5 activator-binding protein C48
Centrosome-associated protein 215
Gene namesi
Name:CDK5RAP2
Synonyms:CEP215, KIAA1633
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:18672. CDK5RAP2.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Golgi apparatus. Cytoplasm
Note: Found in the pericentriolar region adhering to the surface of the centrosome and in the region of the centrosomal appendages. Localizes to microtubule plus ends.

GO - Cellular componenti

  1. cell junction Source: HPA
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. cytoskeleton Source: UniProtKB
  5. cytosol Source: Reactome
  6. extracellular vesicular exosome Source: UniProt
  7. Golgi apparatus Source: UniProtKB
  8. microtubule Source: UniProtKB
  9. pericentriolar material Source: UniProtKB
  10. perinuclear region of cytoplasm Source: UniProtKB
  11. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Golgi apparatus, Microtubule

Pathology & Biotechi

Involvement in diseasei

Microcephaly 3, primary, autosomal recessive (MCPH3) [MIM:604804]: A disease defined as a head circumference more than 3 standard deviations below the age-related mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Despite this marked reduction in size, the gyral pattern is relatively well preserved, with no major abnormality in cortical architecture. Affected individuals are mentally retarded. Primary microcephaly is further defined by the absence of other syndromic features or significant neurological deficits due to degenerative brain disorder.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi938 – 9381L → A: Loss of interaction with MAPRE1; when associated with A-939. 1 Publication
Mutagenesisi939 – 9391P → A: Loss of interaction with MAPRE1; when associated with A-938. 1 Publication
Mutagenesisi1865 – 18651K → A: No effect on centrosomal attachment, Golgi localization and loss of interaction with CALM1; when associated with A-1869. 1 Publication
Mutagenesisi1869 – 18691K → A: No effect on centrosomal attachment, Golgi localization and loss of interaction to CALM1; when associated with A-1865. 1 Publication

Keywords - Diseasei

Mental retardation, Primary microcephaly

Organism-specific databases

MIMi604804. phenotype.
Orphaneti2512. Autosomal recessive primary microcephaly.
PharmGKBiPA38632.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18931893CDK5 regulatory subunit-associated protein 2PRO_0000089835Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei547 – 5471Phosphoserine1 Publication
Modified residuei1001 – 10011Phosphothreonine1 Publication
Modified residuei1238 – 12381Phosphoserine2 Publications
Modified residuei1893 – 18931Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated in vitro by CDK5.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96SN8.
PaxDbiQ96SN8.
PRIDEiQ96SN8.

PTM databases

PhosphoSiteiQ96SN8.

Expressioni

Tissue specificityi

Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

BgeeiQ96SN8.
ExpressionAtlasiQ96SN8. baseline and differential.
GenevestigatoriQ96SN8.

Organism-specific databases

HPAiHPA035820.
HPA046529.

Interactioni

Subunit structurei

Interacts with CDK5R1 (p35 form). 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 and Golgi localization of CDK5RAP2 and PCNT. Interacts with AKAP9; the interaction is leading to Golgi localization of CDK5RAP2 and AKAP9. Interacts with MAPRE1; the interaction is leading to microtubule attachment at plus ends of CDK5RAP2 and MAPRE1. Interacts with TUBG1; the interaction is leading to the centrosomal localization of CDK5RAP2 and TUBG1. Interacts with TUBGCP3. Interacts with CALM1. Interacts with CDC20.By similarity4 Publications

Protein-protein interaction databases

BioGridi120873. 45 interactions.
DIPiDIP-31632N.
IntActiQ96SN8. 25 interactions.
MINTiMINT-1369618.

Structurei

3D structure databases

ProteinModelPortaliQ96SN8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni926 – 1208283Interaction with MAPRE1Add
BLAST
Regioni1726 – 1893168Interaction with PCNT and AKAP9Add
BLAST
Regioni1726 – 176843Interaction with CDK5R1By similarityAdd
BLAST
Regioni1861 – 187010Required for centrosomal attachment, Golgi localization and CALM1 interaction

Phylogenomic databases

eggNOGiNOG46262.
GeneTreeiENSGT00530000063845.
HOVERGENiHBG050976.
InParanoidiQ96SN8.
KOiK16542.
OMAiPEPSASH.
OrthoDBiEOG7GBFW3.
PhylomeDBiQ96SN8.
TreeFamiTF329233.

Family and domain databases

InterProiIPR012943. Spindle_assoc.
[Graphical view]
PfamiPF07989. Microtub_assoc. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96SN8-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MMDLVLEEDV TVPGTLSGCS GLVPSVPDDL DGINPNAGLG NGLLPNVSEE
60 70 80 90 100
TVSPTRARNM KDFENQITEL KKENFNLKLR IYFLEERMQQ EFHGPTEHIY
110 120 130 140 150
KTNIELKVEV ESLKRELQER EQLLIKASKA VESLAEAGGS EIQRVKEDAR
160 170 180 190 200
KKVQQVEDLL TKRILLLEKD VTAAQAELEK AFAGTETEKA LRLRLESKLS
210 220 230 240 250
EMKKMHEGDL AMALVLDEKD RLIEELKLSL KSKEALIQCL KEEKSQMACP
260 270 280 290 300
DENVSSGELR GLCAAPREEK ERETEAAQME HQKERNSFEE RIQALEEDLR
310 320 330 340 350
EKEREIATEK KNSLKRDKAI QGLTMALKSK EKKVEELNSE IEKLSAAFAK
360 370 380 390 400
AREALQKAQT QEFQGSEDYE TALSGKEALS AALRSQNLTK STENHRLRRS
410 420 430 440 450
IKKITQELSD LQQERERLEK DLEEAHREKS KGDCTIRDLR NEVEKLRNEV
460 470 480 490 500
NEREKAMENR YKSLLSESNK KLHNQEQVIK HLTESTNQKD VLLQKFNEKD
510 520 530 540 550
LEVIQQNCYL MAAEDLELRS EGLITEKCSS QQPPGSKTIF SKEKKQSSDY
560 570 580 590 600
EELIQVLKKE QDIYTHLVKS LQESDSINNL QAELNKIFAL RKQLEQDVLS
610 620 630 640 650
YQNLRKTLEE QISEIRRREE ESFSLYSDQT SYLSICLEEN NRFQVEHFSQ
660 670 680 690 700
EELKKKVSDL IQLVKELYTD NQHLKKTIFD LSCMGFQGNG FPDRLASTEQ
710 720 730 740 750
TELLASKEDE DTIKIGEDDE INFLSDQHLQ QSNEIMKDLS KGGCKNGYLR
760 770 780 790 800
HTESKISDCD GAHAPGCLEE GAFINLLAPL FNEKATLLLE SRPDLLKVVR
810 820 830 840 850
ELLLGQLFLT EQEVSGEHLD GKTEKTPKQK GELVHFVQTN SFSKPHDELK
860 870 880 890 900
LSCEAQLVKA GEVPKVGLKD ASVQTVATEG DLLRFKHEAT REAWEEKPIN
910 920 930 940 950
TALSAEHRPE NLHGVPGWQA ALLSLPGITN REAKKSRLPI LIKPSRSLGN
960 970 980 990 1000
MYRLPATQEV VTQLQSQILE LQGELKEFKT CNKQLHQKLI LAEAVMEGRP
1010 1020 1030 1040 1050
TPDKTLLNAQ PPVGAAYQDS PGEQKGIKTT SSVWRDKEMD SDQQRSYEID
1060 1070 1080 1090 1100
SEICPPDDLA SLPSCKENPE DVLSPTSVAT YLSSKSQPSA KVSVMGTDQS
1110 1120 1130 1140 1150
ESINTSNETE YLKQKIHDLE TELEGYQNFI FQLQKHSQCS EAIITVLCGT
1160 1170 1180 1190 1200
EGAQDGLSKP KNGSDGEEMT FSSLHQVRYV KHVKILGPLA PEMIDSRVLE
1210 1220 1230 1240 1250
NLKQQLEEQE YKLQKEQNLN MQLFSEIHNL QNKFRDLSPP RYDSLVQSQA
1260 1270 1280 1290 1300
RELSLQRQQI KDGHGICVIS RQHMNTMIKA FEELLQASDV DYCVAEGFQE
1310 1320 1330 1340 1350
QLNQCAELLE KLEKLFLNGK SVGVEMNTQN ELMERIEEDN LTYQHLLPES
1360 1370 1380 1390 1400
PEPSASHALS DYETSEKSFF SRDQKQDNET EKTSVMVNSF SQDLLMEHIQ
1410 1420 1430 1440 1450
EIRTLRKRLE ESIKTNEKLR KQLERQGSEF VQGSTSIFAS GSELHSSLTS
1460 1470 1480 1490 1500
EIHFLRKQNQ ALNAMLIKGS RDKQKENDKL RESLSRKTVS LEHLQREYAS
1510 1520 1530 1540 1550
VKEENERLQK EGSEKERHNQ QLIQEVRCSG QELSRVQEEV KLRQQLLSQN
1560 1570 1580 1590 1600
DKLLQSLRVE LKAYEKLDEE HRRLREASGE GWKGQDPFRD LHSLLMEIQA
1610 1620 1630 1640 1650
LRLQLERSIE TSSTLQSRLK EQLARGAEKA QEGALTLAVQ AVSIPEVPLQ
1660 1670 1680 1690 1700
PDKHDGDKYP MESDNSFDLF DSSQAVTPKS VSETPPLSGN DTDSLSCDSG
1710 1720 1730 1740 1750
SSATSTPCVS RLVTGHHLWA SKNGRHVLGL IEDYEALLKQ ISQGQRLLAE
1760 1770 1780 1790 1800
MDIQTQEAPS STSQELGTKG PHPAPLSKFV SSVSTAKLTL EEAYRRLKLL
1810 1820 1830 1840 1850
WRVSLPEDGQ CPLHCEQIGE MKAEVTKLHK KLFEQEKKLQ NTMKLLQLSK
1860 1870 1880 1890
RQEKVIFDQL VVTHKILRKA RGNLELRPGG AHPGTCSPSR PGS

Note: No experimental confirmation available.

Length:1,893
Mass (Da):215,038
Last modified:May 18, 2010 - v5
Checksum:i833B9F9EF3CE8D07
GO
Isoform 2 (identifier: Q96SN8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     702-733: Missing.

Note: No experimental confirmation available.

Show »
Length:1,861
Mass (Da):211,381
Checksum:iC56C74BE444511C8
GO
Isoform 3 (identifier: Q96SN8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1009-1049: Missing.

Note: No experimental confirmation available.

Show »
Length:1,852
Mass (Da):210,471
Checksum:iD34C2C2D6EABDE08
GO
Isoform 4 (identifier: Q96SN8-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1576-1654: Missing.

Show »
Length:1,814
Mass (Da):206,323
Checksum:iC28575B525292309
GO

Sequence cautioni

The sequence CAD97828.1 differs from that shown. Reason: Frameshift at position 1831.
The sequence AAH04526.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA91865.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAB13459.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
The sequence BAB15263.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAB55253.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAD97663.1 differs from that shown. Reason: Erroneous termination at position 1205. Translated as Gln.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271P → S in CAD97663. (PubMed:17974005)Curated
Sequence conflicti43 – 431L → V in AAP41926. 1 PublicationCurated
Sequence conflicti292 – 2921I → F in CAD97828. (PubMed:17974005)Curated
Sequence conflicti414 – 4141E → K in CAD97828. (PubMed:17974005)Curated
Sequence conflicti1254 – 12541S → F in CAD97663. (PubMed:17974005)Curated
Sequence conflicti1458 – 14581Q → R in BAA91865. (PubMed:14702039)Curated
Sequence conflicti1483 – 14831S → P in CAD97663. (PubMed:17974005)Curated
Sequence conflicti1550 – 15501N → D in BAB55253. (PubMed:14702039)Curated
Sequence conflicti1838 – 18381K → R in BAA91865. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti183 – 1831A → P.
Corresponds to variant rs13287734 [ dbSNP | Ensembl ].
VAR_056831
Natural varianti289 – 2891E → Q.2 Publications
Corresponds to variant rs4836822 [ dbSNP | Ensembl ].
VAR_017443
Natural varianti1045 – 10451R → T.
Corresponds to variant rs3780679 [ dbSNP | Ensembl ].
VAR_032426
Natural varianti1330 – 13301N → I.
Corresponds to variant rs7875294 [ dbSNP | Ensembl ].
VAR_059616
Natural varianti1540 – 15401V → L.2 Publications
Corresponds to variant rs4837768 [ dbSNP | Ensembl ].
VAR_017444
Natural varianti1607 – 16071R → S.
Corresponds to variant rs16909747 [ dbSNP | Ensembl ].
VAR_056832

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei702 – 73332Missing in isoform 2. 1 PublicationVSP_007563Add
BLAST
Alternative sequencei1009 – 104941Missing in isoform 3. 1 PublicationVSP_007564Add
BLAST
Alternative sequencei1576 – 165479Missing in isoform 4. 3 PublicationsVSP_007565Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB046853 mRNA. Translation: BAB13459.2. Different initiation.
AF448860 mRNA. Translation: AAP41926.1.
AL133161 mRNA. Translation: CAB61487.1.
BX537421 mRNA. Translation: CAD97663.1. Sequence problems.
BX537759 mRNA. Translation: CAD97828.1. Frameshift.
AL590642
, AL138836, AL353736, AL391870 Genomic DNA. Translation: CAH70769.1.
AL138836
, AL353736, AL391870, AL590642 Genomic DNA. Translation: CAI16963.1.
AL353736
, AL138836, AL391870, AL590642 Genomic DNA. Translation: CAI40653.1.
AL391870
, AL138836, AL353736, AL590642 Genomic DNA. Translation: CAI40925.1.
AK001729 mRNA. Translation: BAA91865.1. Different initiation.
AK025867 mRNA. Translation: BAB15263.1. Different initiation.
AK027636 mRNA. Translation: BAB55253.1. Different initiation.
BC004526 mRNA. Translation: AAH04526.2. Different initiation.
CCDSiCCDS43871.1. [Q96SN8-4]
CCDS6823.1. [Q96SN8-1]
PIRiT42658.
RefSeqiNP_001011649.1. NM_001011649.2. [Q96SN8-4]
NP_001258968.1. NM_001272039.1.
NP_060719.4. NM_018249.5. [Q96SN8-1]
XP_006717245.1. XM_006717182.1. [Q96SN8-2]
UniGeneiHs.269560.

Genome annotation databases

EnsembliENST00000349780; ENSP00000343818; ENSG00000136861. [Q96SN8-1]
ENST00000360190; ENSP00000353317; ENSG00000136861. [Q96SN8-4]
GeneIDi55755.
KEGGihsa:55755.
UCSCiuc004bkf.4. human. [Q96SN8-1]
uc004bkg.4. human. [Q96SN8-4]
uc004bki.3. human. [Q96SN8-2]

Polymorphism databases

DMDMi296439505.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB046853 mRNA. Translation: BAB13459.2 . Different initiation.
AF448860 mRNA. Translation: AAP41926.1 .
AL133161 mRNA. Translation: CAB61487.1 .
BX537421 mRNA. Translation: CAD97663.1 . Sequence problems.
BX537759 mRNA. Translation: CAD97828.1 . Frameshift.
AL590642
, AL138836 , AL353736 , AL391870 Genomic DNA. Translation: CAH70769.1 .
AL138836
, AL353736 , AL391870 , AL590642 Genomic DNA. Translation: CAI16963.1 .
AL353736
, AL138836 , AL391870 , AL590642 Genomic DNA. Translation: CAI40653.1 .
AL391870
, AL138836 , AL353736 , AL590642 Genomic DNA. Translation: CAI40925.1 .
AK001729 mRNA. Translation: BAA91865.1 . Different initiation.
AK025867 mRNA. Translation: BAB15263.1 . Different initiation.
AK027636 mRNA. Translation: BAB55253.1 . Different initiation.
BC004526 mRNA. Translation: AAH04526.2 . Different initiation.
CCDSi CCDS43871.1. [Q96SN8-4 ]
CCDS6823.1. [Q96SN8-1 ]
PIRi T42658.
RefSeqi NP_001011649.1. NM_001011649.2. [Q96SN8-4 ]
NP_001258968.1. NM_001272039.1.
NP_060719.4. NM_018249.5. [Q96SN8-1 ]
XP_006717245.1. XM_006717182.1. [Q96SN8-2 ]
UniGenei Hs.269560.

3D structure databases

ProteinModelPortali Q96SN8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120873. 45 interactions.
DIPi DIP-31632N.
IntActi Q96SN8. 25 interactions.
MINTi MINT-1369618.

PTM databases

PhosphoSitei Q96SN8.

Polymorphism databases

DMDMi 296439505.

Proteomic databases

MaxQBi Q96SN8.
PaxDbi Q96SN8.
PRIDEi Q96SN8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000349780 ; ENSP00000343818 ; ENSG00000136861 . [Q96SN8-1 ]
ENST00000360190 ; ENSP00000353317 ; ENSG00000136861 . [Q96SN8-4 ]
GeneIDi 55755.
KEGGi hsa:55755.
UCSCi uc004bkf.4. human. [Q96SN8-1 ]
uc004bkg.4. human. [Q96SN8-4 ]
uc004bki.3. human. [Q96SN8-2 ]

Organism-specific databases

CTDi 55755.
GeneCardsi GC09M123151.
GeneReviewsi CDK5RAP2.
H-InvDB HIX0008336.
HGNCi HGNC:18672. CDK5RAP2.
HPAi HPA035820.
HPA046529.
MIMi 604804. phenotype.
608201. gene.
neXtProti NX_Q96SN8.
Orphaneti 2512. Autosomal recessive primary microcephaly.
PharmGKBi PA38632.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46262.
GeneTreei ENSGT00530000063845.
HOVERGENi HBG050976.
InParanoidi Q96SN8.
KOi K16542.
OMAi PEPSASH.
OrthoDBi EOG7GBFW3.
PhylomeDBi Q96SN8.
TreeFami TF329233.

Enzyme and pathway databases

Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

ChiTaRSi CDK5RAP2. human.
GeneWikii CDK5RAP2.
GenomeRNAii 55755.
NextBioi 60757.
PROi Q96SN8.
SOURCEi Search...

Gene expression databases

Bgeei Q96SN8.
ExpressionAtlasi Q96SN8. baseline and differential.
Genevestigatori Q96SN8.

Family and domain databases

InterProi IPR012943. Spindle_assoc.
[Graphical view ]
Pfami PF07989. Microtub_assoc. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT GLN-289.
    Tissue: Brain.
  2. Ohara O., Nagase T., Kikuno R.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Guo J.H., Zan Q., Yu L.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 575-1893 (ISOFORM 2), VARIANTS GLN-289 AND LEU-1540.
    Tissue: Amygdala, Retina and Testis.
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 950-1893 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1576-1654 (ISOFORM 4), VARIANT LEU-1540.
    Tissue: Kidney and Teratocarcinoma.
  7. "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] OF 1401-1893.
    Tissue: Lung.
  8. "Cloning of three novel neuronal Cdk5 activator binding proteins."
    Ching Y.-P., Qi Z., Wang J.H.
    Gene 242:285-294(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  9. "Proteomic characterization of the human centrosome by protein correlation profiling."
    Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.
    Nature 426:570-574(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Lymphoblast.
  10. Cited for: INVOLVEMENT IN MCPH3.
  11. "Cep68 and Cep215 (Cdk5rap2) are required for centrosome cohesion."
    Graser S., Stierhof Y.D., Nigg E.A.
    J. Cell Sci. 120:4321-4331(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "CDK5RAP2 is a pericentriolar protein that functions in centrosomal attachment of the gamma-tubulin ring complex."
    Fong K.W., Choi Y.K., Rattner J.B., Qi R.Z.
    Mol. Biol. Cell 19:115-125(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TUBG1 AND TUBGCP3.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1238 AND SER-1893, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "CDK5RAP2 is required for spindle checkpoint function."
    Zhang X., Liu D., Lv S., Wang H., Zhong X., Liu B., Wang B., Liao J., Li J., Pfeifer G.P., Xu X.
    Cell Cycle 8:1206-1216(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDC20.
  15. "Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to regulate microtubule dynamics."
    Fong K.W., Hau S.Y., Kho Y.S., Jia Y., He L., Qi R.Z.
    Mol. Biol. Cell 20:3660-3670(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-938 AND PRO-939.
  16. "Plk1-dependent recruitment of gamma-tubulin complexes to mitotic centrosomes involves multiple PCM components."
    Haren L., Stearns T., Lueders J.
    PLoS ONE 4:E5976-E5976(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Conserved motif of CDK5RAP2 mediates its localization to centrosomes and the Golgi complex."
    Wang Z., Wu T., Shi L., Zhang L., Zheng W., Qu J.Y., Niu R., Qi R.Z.
    J. Biol. Chem. 285:22658-22665(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AKAP9; CALM1 AND PCNT, MUTAGENESIS OF LYS-1865 AND LYS-1869.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND THR-1001, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCK5P2_HUMAN
AccessioniPrimary (citable) accession number: Q96SN8
Secondary accession number(s): Q5JV18
, Q7Z3L4, Q7Z3U1, Q7Z7I6, Q9BSW0, Q9H6J6, Q9HCD9, Q9NV90, Q9UIW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 129 of the entry and version 5 of the sequence. [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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3