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Q96SN8 (CK5P2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CDK5 regulatory subunit-associated protein 2
Alternative name(s):
CDK5 activator-binding protein C48
Centrosome-associated protein 215
Gene names
Name:CDK5RAP2
Synonyms:CEP215, KIAA1633
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1893 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.13 Ref.15 Ref.16

Subunit structure

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. Ref.13 Ref.15 Ref.16 Ref.19

Subcellular location

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. Ref.9 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19

Tissue specificity

Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.8

Post-translational modification

Phosphorylated in vitro by CDK5 By similarity.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence caution

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.

The sequence CAD97828.1 differs from that shown. Reason: Frameshift at position 1831.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Golgi apparatus
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseMental retardation
Primary microcephaly
   LigandCalmodulin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

brain development

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome organization

Inferred from mutant phenotype Ref.12. Source: UniProtKB

chromosome segregation

Inferred from mutant phenotype Ref.15. Source: UniProtKB

establishment of mitotic spindle orientation

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule bundle formation

Inferred from direct assay Ref.16. Source: UniProtKB

microtubule cytoskeleton organization

Inferred from direct assay Ref.13. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of centriole replication

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.15. Source: UniProtKB

regulation of neuron differentiation

Non-traceable author statement Ref.8. Source: UniProtKB

regulation of spindle checkpoint

Inferred from direct assay Ref.15. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.19. Source: UniProtKB

cell junction

Inferred from direct assay. Source: HPA

centrosome

Inferred from direct assay Ref.9Ref.13Ref.12Ref.15Ref.17Ref.16Ref.19PubMed 21399614. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.13Ref.15Ref.16. Source: UniProtKB

cytoskeleton

Non-traceable author statement Ref.8. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

microtubule

Inferred from direct assay Ref.16. Source: UniProtKB

pericentriolar material

Inferred from direct assay Ref.13. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.13. Source: UniProtKB

spindle pole

Inferred from direct assay Ref.13Ref.15. Source: UniProtKB

   Molecular_functioncalmodulin binding

Inferred from physical interaction Ref.19. Source: UniProtKB

microtubule binding

Inferred from direct assay Ref.9. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.8. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay Ref.15. Source: UniProtKB

tubulin binding

Inferred from physical interaction Ref.13. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96SN8-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q96SN8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     702-733: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q96SN8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1009-1049: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q96SN8-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18931893CDK5 regulatory subunit-associated protein 2
PRO_0000089835

Regions

Region926 – 1208283Interaction with MAPRE1
Region1726 – 1893168Interaction with PCNT and AKAP9
Region1726 – 176843Interaction with CDK5R1 By similarity
Region1861 – 187010Required for centrosomal attachment, Golgi localization and CALM1 interaction

Amino acid modifications

Modified residue5471Phosphoserine Ref.20
Modified residue10011Phosphothreonine Ref.20
Modified residue12381Phosphoserine Ref.14 Ref.18
Modified residue18931Phosphoserine Ref.14

Natural variations

Alternative sequence702 – 73332Missing in isoform 2.
VSP_007563
Alternative sequence1009 – 104941Missing in isoform 3.
VSP_007564
Alternative sequence1576 – 165479Missing in isoform 4.
VSP_007565
Natural variant1831A → P.
Corresponds to variant rs13287734 [ dbSNP | Ensembl ].
VAR_056831
Natural variant2891E → Q. Ref.1 Ref.4
Corresponds to variant rs4836822 [ dbSNP | Ensembl ].
VAR_017443
Natural variant10451R → T.
Corresponds to variant rs3780679 [ dbSNP | Ensembl ].
VAR_032426
Natural variant13301N → I.
Corresponds to variant rs7875294 [ dbSNP | Ensembl ].
VAR_059616
Natural variant15401V → L. Ref.4 Ref.6
Corresponds to variant rs4837768 [ dbSNP | Ensembl ].
VAR_017444
Natural variant16071R → S.
Corresponds to variant rs16909747 [ dbSNP | Ensembl ].
VAR_056832

Experimental info

Mutagenesis9381L → A: Loss of interaction with MAPRE1; when associated with A-939. Ref.16
Mutagenesis9391P → A: Loss of interaction with MAPRE1; when associated with A-938. Ref.16
Mutagenesis18651K → A: No effect on centrosomal attachment, Golgi localization and loss of interaction with CALM1; when associated with A-1869. Ref.19
Mutagenesis18691K → A: No effect on centrosomal attachment, Golgi localization and loss of interaction to CALM1; when associated with A-1865. Ref.19
Sequence conflict271P → S in CAD97663. Ref.4
Sequence conflict431L → V in AAP41926. Ref.3
Sequence conflict2921I → F in CAD97828. Ref.4
Sequence conflict4141E → K in CAD97828. Ref.4
Sequence conflict12541S → F in CAD97663. Ref.4
Sequence conflict14581Q → R in BAA91865. Ref.6
Sequence conflict14831S → P in CAD97663. Ref.4
Sequence conflict15501N → D in BAB55253. Ref.6
Sequence conflict18381K → R in BAA91865. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 5.
Checksum: 833B9F9EF3CE8D07

FASTA1,893215,038
        10         20         30         40         50         60 
MMDLVLEEDV TVPGTLSGCS GLVPSVPDDL DGINPNAGLG NGLLPNVSEE TVSPTRARNM 

        70         80         90        100        110        120 
KDFENQITEL KKENFNLKLR IYFLEERMQQ EFHGPTEHIY KTNIELKVEV ESLKRELQER 

       130        140        150        160        170        180 
EQLLIKASKA VESLAEAGGS EIQRVKEDAR KKVQQVEDLL TKRILLLEKD VTAAQAELEK 

       190        200        210        220        230        240 
AFAGTETEKA LRLRLESKLS EMKKMHEGDL AMALVLDEKD RLIEELKLSL KSKEALIQCL 

       250        260        270        280        290        300 
KEEKSQMACP DENVSSGELR GLCAAPREEK ERETEAAQME HQKERNSFEE RIQALEEDLR 

       310        320        330        340        350        360 
EKEREIATEK KNSLKRDKAI QGLTMALKSK EKKVEELNSE IEKLSAAFAK AREALQKAQT 

       370        380        390        400        410        420 
QEFQGSEDYE TALSGKEALS AALRSQNLTK STENHRLRRS IKKITQELSD LQQERERLEK 

       430        440        450        460        470        480 
DLEEAHREKS KGDCTIRDLR NEVEKLRNEV NEREKAMENR YKSLLSESNK KLHNQEQVIK 

       490        500        510        520        530        540 
HLTESTNQKD VLLQKFNEKD LEVIQQNCYL MAAEDLELRS EGLITEKCSS QQPPGSKTIF 

       550        560        570        580        590        600 
SKEKKQSSDY EELIQVLKKE QDIYTHLVKS LQESDSINNL QAELNKIFAL RKQLEQDVLS 

       610        620        630        640        650        660 
YQNLRKTLEE QISEIRRREE ESFSLYSDQT SYLSICLEEN NRFQVEHFSQ EELKKKVSDL 

       670        680        690        700        710        720 
IQLVKELYTD NQHLKKTIFD LSCMGFQGNG FPDRLASTEQ TELLASKEDE DTIKIGEDDE 

       730        740        750        760        770        780 
INFLSDQHLQ QSNEIMKDLS KGGCKNGYLR HTESKISDCD GAHAPGCLEE GAFINLLAPL 

       790        800        810        820        830        840 
FNEKATLLLE SRPDLLKVVR ELLLGQLFLT EQEVSGEHLD GKTEKTPKQK GELVHFVQTN 

       850        860        870        880        890        900 
SFSKPHDELK LSCEAQLVKA GEVPKVGLKD ASVQTVATEG DLLRFKHEAT REAWEEKPIN 

       910        920        930        940        950        960 
TALSAEHRPE NLHGVPGWQA ALLSLPGITN REAKKSRLPI LIKPSRSLGN MYRLPATQEV 

       970        980        990       1000       1010       1020 
VTQLQSQILE LQGELKEFKT CNKQLHQKLI LAEAVMEGRP TPDKTLLNAQ PPVGAAYQDS 

      1030       1040       1050       1060       1070       1080 
PGEQKGIKTT SSVWRDKEMD SDQQRSYEID SEICPPDDLA SLPSCKENPE DVLSPTSVAT 

      1090       1100       1110       1120       1130       1140 
YLSSKSQPSA KVSVMGTDQS ESINTSNETE YLKQKIHDLE TELEGYQNFI FQLQKHSQCS 

      1150       1160       1170       1180       1190       1200 
EAIITVLCGT EGAQDGLSKP KNGSDGEEMT FSSLHQVRYV KHVKILGPLA PEMIDSRVLE 

      1210       1220       1230       1240       1250       1260 
NLKQQLEEQE YKLQKEQNLN MQLFSEIHNL QNKFRDLSPP RYDSLVQSQA RELSLQRQQI 

      1270       1280       1290       1300       1310       1320 
KDGHGICVIS RQHMNTMIKA FEELLQASDV DYCVAEGFQE QLNQCAELLE KLEKLFLNGK 

      1330       1340       1350       1360       1370       1380 
SVGVEMNTQN ELMERIEEDN LTYQHLLPES PEPSASHALS DYETSEKSFF SRDQKQDNET 

      1390       1400       1410       1420       1430       1440 
EKTSVMVNSF SQDLLMEHIQ EIRTLRKRLE ESIKTNEKLR KQLERQGSEF VQGSTSIFAS 

      1450       1460       1470       1480       1490       1500 
GSELHSSLTS EIHFLRKQNQ ALNAMLIKGS RDKQKENDKL RESLSRKTVS LEHLQREYAS 

      1510       1520       1530       1540       1550       1560 
VKEENERLQK EGSEKERHNQ QLIQEVRCSG QELSRVQEEV KLRQQLLSQN DKLLQSLRVE 

      1570       1580       1590       1600       1610       1620 
LKAYEKLDEE HRRLREASGE GWKGQDPFRD LHSLLMEIQA LRLQLERSIE TSSTLQSRLK 

      1630       1640       1650       1660       1670       1680 
EQLARGAEKA QEGALTLAVQ AVSIPEVPLQ PDKHDGDKYP MESDNSFDLF DSSQAVTPKS 

      1690       1700       1710       1720       1730       1740 
VSETPPLSGN DTDSLSCDSG SSATSTPCVS RLVTGHHLWA SKNGRHVLGL IEDYEALLKQ 

      1750       1760       1770       1780       1790       1800 
ISQGQRLLAE MDIQTQEAPS STSQELGTKG PHPAPLSKFV SSVSTAKLTL EEAYRRLKLL 

      1810       1820       1830       1840       1850       1860 
WRVSLPEDGQ CPLHCEQIGE MKAEVTKLHK KLFEQEKKLQ NTMKLLQLSK RQEKVIFDQL 

      1870       1880       1890 
VVTHKILRKA RGNLELRPGG AHPGTCSPSR PGS 

« Hide

Isoform 2 [UniParc].

Checksum: C56C74BE444511C8
Show »

FASTA1,861211,381
Isoform 3 [UniParc].

Checksum: D34C2C2D6EABDE08
Show »

FASTA1,852210,471
Isoform 4 [UniParc].

Checksum: C28575B525292309
Show »

FASTA1,814206,323

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"A centrosomal mechanism involving CDK5RAP2 and CENPJ controls brain size."
Bond J., Roberts E., Springell K., Lizarraga S.B., Scott S., Higgins J., Hampshire D.J., Morrison E.E., Leal G.F., Silva E.O., Costa S.M.R., Baralle D., Raponi M., Karbani G., Rashid Y., Jafri H., Bennett C., Corry P., Walsh C.A., Woods C.G.
Nat. Genet. 37:353-355(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MCPH3.
[11]Erratum
Bond J., Roberts E., Springell K., Lizarraga S.B., Scott S., Higgins J., Hampshire D.J., Morrison E.E., Leal G.F., Silva E.O., Costa S.M.R., Baralle D., Raponi M., Karbani G., Rashid Y., Jafri H., Bennett C., Corry P., Walsh C.A., Woods C.G.
Nat. Genet. 37:555-555(2005)
[12]"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.
[13]"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.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1238 AND SER-1893, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , AL138836, AL353736, AL391870 Genomic DNA. Translation: CAH70769.1.
AL138836 expand/collapse EMBL AC list , AL353736, AL391870, AL590642 Genomic DNA. Translation: CAI16963.1.
AL353736 expand/collapse EMBL AC list , AL138836, AL391870, AL590642 Genomic DNA. Translation: CAI40653.1.
AL391870 expand/collapse EMBL AC list , 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.
PIRT42658.
RefSeqNP_001011649.1. NM_001011649.2.
NP_001258968.1. NM_001272039.1.
NP_060719.4. NM_018249.5.
UniGeneHs.269560.

3D structure databases

ProteinModelPortalQ96SN8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120873. 36 interactions.
DIPDIP-31632N.
IntActQ96SN8. 23 interactions.
MINTMINT-1369618.

PTM databases

PhosphoSiteQ96SN8.

Polymorphism databases

DMDM296439505.

Proteomic databases

PaxDbQ96SN8.
PRIDEQ96SN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000349780; ENSP00000343818; ENSG00000136861. [Q96SN8-1]
ENST00000359309; ENSP00000352258; ENSG00000136861. [Q96SN8-3]
ENST00000360190; ENSP00000353317; ENSG00000136861. [Q96SN8-4]
ENST00000360822; ENSP00000354065; ENSG00000136861. [Q96SN8-2]
GeneID55755.
KEGGhsa:55755.
UCSCuc004bkf.4. human. [Q96SN8-1]
uc004bkg.4. human. [Q96SN8-4]
uc004bki.3. human. [Q96SN8-2]

Organism-specific databases

CTD55755.
GeneCardsGC09M123151.
H-InvDBHIX0008336.
HGNCHGNC:18672. CDK5RAP2.
HPAHPA035820.
HPA046529.
MIM604804. phenotype.
608201. gene.
neXtProtNX_Q96SN8.
Orphanet2512. Autosomal recessive primary microcephaly.
PharmGKBPA38632.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46262.
HOVERGENHBG050976.
InParanoidQ96SN8.
KOK16542.
OMAPEPSASH.
OrthoDBEOG7GBFW3.
PhylomeDBQ96SN8.
TreeFamTF329233.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.

Gene expression databases

ArrayExpressQ96SN8.
BgeeQ96SN8.
GenevestigatorQ96SN8.

Family and domain databases

InterProIPR012943. Spindle_assoc.
[Graphical view]
PfamPF07989. Microtub_assoc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDK5RAP2. human.
GeneWikiCDK5RAP2.
GenomeRNAi55755.
NextBio60757.
PROQ96SN8.
SOURCESearch...

Entry information

Entry nameCK5P2_HUMAN
AccessionPrimary (citable) accession number: Q96SN8
Secondary accession number(s): Q5JV18 expand/collapse secondary AC list , Q7Z3L4, Q7Z3U1, Q7Z7I6, Q9BSW0, Q9H6J6, Q9HCD9, Q9NV90, Q9UIW9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 123 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM