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CDK5 regulatory subunit-associated protein 3 (CDK5 activator-binding protein C53) (LXXLL/leucine-zipper-containing ARF-binding protein) (Protein HSF-27)

 CK5P3_HUMAN             Reviewed;         506 AA.
Q96JB5; B7Z6N4; D3DTU1; D3DTU2; F5H3I5; Q53FA2; Q9H3F8; Q9H8G0;
Q9HBR9;
16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
16-JUN-2003, sequence version 2.
25-OCT-2017, entry version 146.
RecName: Full=CDK5 regulatory subunit-associated protein 3 {ECO:0000312};
AltName: Full=CDK5 activator-binding protein C53 {ECO:0000305|PubMed:10721722};
AltName: Full=LXXLL/leucine-zipper-containing ARF-binding protein {ECO:0000303|PubMed:20164180};
AltName: Full=Protein HSF-27 {ECO:0000312|EMBL:AAK69655.1};
Name=CDK5RAP3 {ECO:0000312|HGNC:HGNC:18673};
Synonyms=IC53 {ECO:0000303|PubMed:20164180},
LZAP {ECO:0000303|PubMed:20164180};
ORFNames=MSTP016, OK/SW-cl.114, PP1553;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Aorta;
PubMed=12054757; DOI=10.1016/S0006-291X(02)00446-1;
Chen J., Liu B., Liu Y.Q., Han Y., Yu H., Zhang Y., Lu L., Zhen Y.,
Hui R.T.;
"A novel gene IC53 stimulates ECV304 cell proliferation and is
upregulated in failing heart.";
Biochem. Biophys. Res. Commun. 294:161-166(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH
CDK5R1, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=12737517; DOI=10.1038/sj.cr.7290153;
Xie Y.H., He X.H., Tang Y.T., Li J.J., Pan Z.M., Qin W.X., Wan da F.,
Gu J.R.;
"Cloning and characterization of human IC53-2, a novel CDK5 activator
binding protein.";
Cell Res. 13:83-91(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
Favier A.-L., Harsi C., Chrobozcek J.;
"Protein interacting with the receptor binding domain of enteric
adenovirus serotype 41 fiber protein.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
TISSUE=Placenta, and Rectum;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Synovial cell;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
TISSUE SPECIFICITY.
PubMed=10721722; DOI=10.1016/S0378-1119(99)00499-0;
Ching Y.-P., Qi Z., Wang J.H.;
"Cloning of three novel neuronal Cdk5 activator binding proteins.";
Gene 242:285-294(2000).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCNB1.
PubMed=15790566; DOI=10.1074/jbc.M413431200;
Jiang H., Luo S., Li H.;
"Cdk5 activator-binding protein C53 regulates apoptosis induced by
genotoxic stress via modulating the G2/M DNA damage checkpoint.";
J. Biol. Chem. 280:20651-20659(2005).
[12]
FUNCTION, INTERACTION WITH CDKN2A/ARF AND MDM2, AND SUBCELLULAR
LOCATION.
PubMed=16173922; DOI=10.1042/BJ20050960;
Wang J., He X., Luo Y., Yarbrough W.G.;
"A novel ARF-binding protein (LZAP) alters ARF regulation of HDM2.";
Biochem. J. 393:489-501(2006).
[13]
FUNCTION, AND INTERACTION WITH RELA.
PubMed=17785205; DOI=10.1016/j.ccr.2007.07.002;
Wang J., An H., Mayo M.W., Baldwin A.S., Yarbrough W.G.;
"LZAP, a putative tumor suppressor, selectively inhibits NF-kappaB.";
Cancer Cell 12:239-251(2007).
[14]
FUNCTION, INTERACTION WITH CHEK1, REGION, AND SUBCELLULAR LOCATION.
PubMed=19223857; DOI=10.1038/cr.2009.14;
Jiang H., Wu J., He C., Yang W., Li H.;
"Tumor suppressor protein C53 antagonizes checkpoint kinases to
promote cyclin-dependent kinase 1 activation.";
Cell Res. 19:458-468(2009).
[15]
INTERACTION WITH UFL1.
PubMed=20164180; DOI=10.1074/jbc.M109.065920;
Kwon J., Cho H.J., Han S.H., No J.G., Kwon J.Y., Kim H.;
"A novel LZAP-binding protein, NLBP, inhibits cell invasion.";
J. Biol. Chem. 285:12232-12240(2010).
[16]
FUNCTION, INTERACTION WITH DDRGK1 AND UFL1, REGION, AND
UBIQUITINATION.
PubMed=20228063; DOI=10.1074/jbc.M110.110619;
Wu J., Lei G., Mei M., Tang Y., Li H.;
"A novel C53/LZAP-interacting protein regulates stability of C53/LZAP
and DDRGK domain-containing Protein 1 (DDRGK1) and modulates NF-kappaB
signaling.";
J. Biol. Chem. 285:15126-15136(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
FUNCTION, AND INTERACTION WITH MAPK14.
PubMed=21283629; DOI=10.1371/journal.pone.0016427;
An H., Lu X., Liu D., Yarbrough W.G.;
"LZAP inhibits p38 MAPK (p38) phosphorylation and activity by
facilitating p38 association with the wild-type p53 induced
phosphatase 1 (WIP1).";
PLoS ONE 6:E16427-E16427(2011).
[19]
INTERACTION WITH TUBG1.
PubMed=21465471; DOI=10.1002/jcp.22772;
Horejsi B., Vinopal S., Sladkova V., Draberova E., Sulimenko V.,
Sulimenko T., Vosecka V., Philimonenko A., Hozak P., Katsetos C.D.,
Draber P.;
"Nuclear gamma-tubulin associates with nucleoli and interacts with
tumor suppressor protein C53.";
J. Cell. Physiol. 227:367-382(2012).
[20]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HEPATITIS B VIRUS
LARGE ENVELOPE PROTEIN.
PubMed=21971960; DOI=10.3892/or.2011.1489;
Lei Y., Liu H., Yang Y., Wang X., Ren N., Li B., Liu S., Cheng J.,
Fu X., Zhang J.;
"Interaction of LHBs with C53 promotes hepatocyte mitotic entry: A
novel mechanism for HBV-induced hepatocellular carcinoma.";
Oncol. Rep. 27:151-159(2012).
[21]
FUNCTION.
PubMed=23152784; DOI=10.1371/journal.pone.0048587;
Zhang Y., Zhang M., Wu J., Lei G., Li H.;
"Transcriptional regulation of the Ufm1 conjugation system in response
to disturbance of the endoplasmic reticulum homeostasis and inhibition
of vesicle trafficking.";
PLoS ONE 7:E48587-E48587(2012).
[22]
FUNCTION, CLEAVAGE BY CASPASES, MUTAGENESIS OF ASP-268; ASP-282 AND
ASP-311, AND SUBCELLULAR LOCATION.
PubMed=23478299; DOI=10.1038/cr.2013.36;
Wu J., Jiang H., Luo S., Zhang M., Zhang Y., Sun F., Huang S., Li H.;
"Caspase-mediated cleavage of C53/LZAP protein causes abnormal
microtubule bundling and rupture of the nuclear envelope.";
Cell Res. 23:691-704(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-450, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Probable tumor suppressor initially identified as a
CDK5R1 interactor controlling cell proliferation (PubMed:12054757,
PubMed:12737517). Negatively regulates NF-kappa-B-mediated gene
transcription through the control of RELA phosphorylation
(PubMed:17785205, PubMed:20228063). Also regulates mitotic G2/M
transition checkpoint and mitotic G2 DNA damage checkpoint
(PubMed:15790566, PubMed:19223857). 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 (PubMed:16173922). May play a role in the unfolded
protein response, mediating the ufmylation of multiple proteins in
response to endoplasmic reticulum stress (PubMed:23152784). May
also play a role in the rupture of the nuclear envelope during
apoptosis (PubMed:23478299). May regulate MAPK14 activity by
regulating its dephosphorylation by PPM1D/WIP1 (PubMed:21283629).
{ECO:0000269|PubMed:12054757, ECO:0000269|PubMed:12737517,
ECO:0000269|PubMed:15790566, ECO:0000269|PubMed:16173922,
ECO:0000269|PubMed:17785205, ECO:0000269|PubMed:19223857,
ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:21283629,
ECO:0000269|PubMed:23152784, ECO:0000269|PubMed:23478299}.
-!- FUNCTION: (Microbial infection) May be negatively regulated by
hepatitis B virus large envelope protein mutant pre-s2 to promote
mitotic entry.
-!- SUBUNIT: Interacts with CDK5R1; competes with CDK5RAP1 and
CDK5RAP2 (PubMed:12737517). Interacts with RELA (PubMed:17785205).
Interacts with CHEK1; may negatively regulate CHEK1 and thereby
stimulate entry into mitosis (PubMed:19223857). Interacts with
CDKN2A/ARF and MDM2; forms a ternary complex involved in
regulation of p53/TP53 (PubMed:16173922). Interacts with UFL1; the
interaction is direct (PubMed:20164180, PubMed:20228063).
Interacts with DDRGK1 (PubMed:20228063). Interacts with MAPK14
(PubMed:21283629). Interacts with CCNB1 (PubMed:15790566).
Interacts with TUBG1; may regulate CDK5RAP3 in mitotic G2/M
transition checkpoint (PubMed:21465471).
{ECO:0000269|PubMed:12737517, ECO:0000269|PubMed:15790566,
ECO:0000269|PubMed:16173922, ECO:0000269|PubMed:17785205,
ECO:0000269|PubMed:19223857, ECO:0000269|PubMed:20164180,
ECO:0000269|PubMed:20228063, ECO:0000269|PubMed:21283629,
ECO:0000269|PubMed:21465471}.
-!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus
large envelope protein mutant pre-s2; promotes mitotic entry.
{ECO:0000269|PubMed:21971960}.
-!- INTERACTION:
O75344:FKBP6; NbExp=8; IntAct=EBI-718818, EBI-744771;
Q04206:RELA; NbExp=4; IntAct=EBI-718818, EBI-73886;
Q9UJ04:TSPYL4; NbExp=5; IntAct=EBI-718818, EBI-308511;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16173922}.
Cytoplasm {ECO:0000269|PubMed:15790566,
ECO:0000269|PubMed:16173922, ECO:0000269|PubMed:19223857}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:19223857}. Note=Colocalizes and associates
with microtubules. {ECO:0000269|PubMed:23478299}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q96JB5-1; Sequence=Displayed;
Name=2; Synonyms=IC53;
IsoId=Q96JB5-2; Sequence=VSP_007566, VSP_007567;
Note=Due to an intron retention.;
Name=3; Synonyms=IC53-2;
IsoId=Q96JB5-3; Sequence=VSP_007568;
Note=Due to intron retention. No experimental confirmation
available.;
Name=4;
IsoId=Q96JB5-4; Sequence=VSP_055646;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:12054757,
PubMed:10721722). Expressed in heart, brain, placenta, lung,
liver, skeletal muscle, kidney and pancreas. Isoform 3 is
expressed in kidney, liver, skeletal muscle and placenta
(PubMed:12737517). {ECO:0000269|PubMed:10721722,
ECO:0000269|PubMed:12054757, ECO:0000269|PubMed:12737517}.
-!- PTM: May be phosphorylated by CDK5.
{ECO:0000250|UniProtKB:Q9JLH7}.
-!- PTM: Ubiquitinated. Probably triggers proteasomal degradation and
is negatively regulated by UFL1. {ECO:0000269|PubMed:20228063}.
-!- PTM: May be ufmylated. {ECO:0000250|UniProtKB:Q99LM2}.
-!- PTM: Cleaved by caspases early during apoptosis, the resulting
peptides may play a role in rupture of the nuclear envelope.
{ECO:0000269|PubMed:23478299}.
-!- SIMILARITY: Belongs to the CDK5RAP3 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK69655.1; Type=Frameshift; Positions=410; Evidence={ECO:0000305};
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EMBL; AF110322; AAG39277.1; -; mRNA.
EMBL; AF217982; AAG17225.1; -; mRNA.
EMBL; AF343090; AAK69655.1; ALT_FRAME; mRNA.
EMBL; AB062433; BAB93496.1; -; mRNA.
EMBL; AK023722; BAB14657.1; -; mRNA.
EMBL; AK300643; BAH13320.1; -; mRNA.
EMBL; AK223387; BAD97107.1; -; mRNA.
EMBL; AC018521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94772.1; -; Genomic_DNA.
EMBL; CH471109; EAW94774.1; -; Genomic_DNA.
EMBL; CH471109; EAW94775.1; -; Genomic_DNA.
EMBL; CH471109; EAW94778.1; -; Genomic_DNA.
EMBL; BC009957; AAH09957.1; -; mRNA.
EMBL; BC072435; AAH72435.1; -; mRNA.
CCDS; CCDS42356.1; -. [Q96JB5-1]
CCDS; CCDS62232.1; -. [Q96JB5-4]
PIR; JC7863; JC7863.
RefSeq; NP_001265126.1; NM_001278197.1. [Q96JB5-4]
RefSeq; NP_001265127.1; NM_001278198.1.
RefSeq; NP_001265145.1; NM_001278216.1. [Q96JB5-3]
RefSeq; NP_001265146.1; NM_001278217.1. [Q96JB5-2]
RefSeq; NP_788276.1; NM_176096.2. [Q96JB5-1]
RefSeq; XP_011523599.1; XM_011525297.1. [Q96JB5-4]
RefSeq; XP_016880653.1; XM_017025164.1. [Q96JB5-2]
RefSeq; XP_016880654.1; XM_017025165.1. [Q96JB5-2]
UniGene; Hs.20157; -.
ProteinModelPortal; Q96JB5; -.
SMR; Q96JB5; -.
BioGrid; 123213; 53.
IntAct; Q96JB5; 23.
MINT; MINT-1410069; -.
STRING; 9606.ENSP00000344683; -.
iPTMnet; Q96JB5; -.
PhosphoSitePlus; Q96JB5; -.
SwissPalm; Q96JB5; -.
DMDM; 32129444; -.
EPD; Q96JB5; -.
MaxQB; Q96JB5; -.
PaxDb; Q96JB5; -.
PeptideAtlas; Q96JB5; -.
PRIDE; Q96JB5; -.
DNASU; 80279; -.
Ensembl; ENST00000338399; ENSP00000344683; ENSG00000108465. [Q96JB5-1]
Ensembl; ENST00000536708; ENSP00000438886; ENSG00000108465. [Q96JB5-4]
GeneID; 80279; -.
KEGG; hsa:80279; -.
UCSC; uc002imr.5; human. [Q96JB5-1]
CTD; 80279; -.
DisGeNET; 80279; -.
EuPathDB; HostDB:ENSG00000108465.14; -.
GeneCards; CDK5RAP3; -.
H-InvDB; HIX0013932; -.
HGNC; HGNC:18673; CDK5RAP3.
HPA; HPA022141; -.
HPA; HPA022882; -.
HPA; HPA027883; -.
MIM; 608202; gene.
neXtProt; NX_Q96JB5; -.
OpenTargets; ENSG00000108465; -.
PharmGKB; PA38633; -.
eggNOG; KOG2607; Eukaryota.
eggNOG; ENOG410XSWB; LUCA.
GeneTree; ENSGT00390000000713; -.
HOGENOM; HOG000231047; -.
HOVERGEN; HBG050978; -.
InParanoid; Q96JB5; -.
OMA; PGVRKQM; -.
OrthoDB; EOG091G11PB; -.
PhylomeDB; Q96JB5; -.
ChiTaRS; CDK5RAP3; human.
GeneWiki; CDK5RAP3; -.
GenomeRNAi; 80279; -.
PRO; PR:Q96JB5; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108465; -.
CleanEx; HS_CDK5RAP3; -.
ExpressionAtlas; Q96JB5; baseline and differential.
Genevisible; Q96JB5; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:UniProtKB.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB.
GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0044389; F:ubiquitin-like protein ligase binding; IDA:MGI.
GO; GO:0030262; P:apoptotic nuclear changes; IMP:UniProtKB.
GO; GO:0007420; P:brain development; NAS:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IMP:UniProtKB.
GO; GO:0044818; P:mitotic G2/M transition checkpoint; IMP:UniProtKB.
GO; GO:1903363; P:negative regulation of cellular protein catabolic process; IDA:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0071569; P:protein ufmylation; IDA:MGI.
GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
GO; GO:0045664; P:regulation of neuron differentiation; NAS:UniProtKB.
GO; GO:0010921; P:regulation of phosphatase activity; IMP:UniProtKB.
InterPro; IPR008491; CDK5RAP3.
PANTHER; PTHR14894; PTHR14894; 1.
Pfam; PF05600; DUF773; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 506 CDK5 regulatory subunit-associated
protein 3.
/FTId=PRO_0000220516.
REGION 269 506 Required for interaction with UFL1 and
mediates interaction with CHEK1.
{ECO:0000269|PubMed:19223857,
ECO:0000269|PubMed:20228063}.
CROSSLNK 450 450 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364}.
VAR_SEQ 1 225 Missing (in isoform 3).
{ECO:0000303|PubMed:12737517}.
/FTId=VSP_007568.
VAR_SEQ 1 87 Missing (in isoform 2).
{ECO:0000303|PubMed:12054757}.
/FTId=VSP_007566.
VAR_SEQ 1 2 ME -> MRRQSMTSATRDLHTALDGKATQGGKK (in
isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055646.
VAR_SEQ 88 111 RYSSQRMKDWQEIIALYEKDNTYL -> MCVHPGACLPHVG
VSWAEFPGHFS (in isoform 2).
{ECO:0000303|PubMed:12054757}.
/FTId=VSP_007567.
VARIANT 324 324 L -> V (in dbSNP:rs35054799).
/FTId=VAR_048688.
MUTAGEN 268 268 D->E: Alters cleavage by CASP3 in vitro.
Prevents apoptosis-induced cleavage in
vivo; when associated with E-282 and E-
311. {ECO:0000269|PubMed:23478299}.
MUTAGEN 282 282 D->E: Alters cleavage by CASP3 in vitro.
Prevents apoptosis-induced cleavage in
vivo; when associated with E-268 and E-
311. {ECO:0000269|PubMed:23478299}.
MUTAGEN 311 311 D->E: Alters cleavage by CASP3 in vitro.
Prevents apoptosis-induced cleavage in
vivo; when associated with E-268 and E-
282. {ECO:0000269|PubMed:23478299}.
CONFLICT 98 98 Q -> R (in Ref. 5; BAH13320).
{ECO:0000305}.
CONFLICT 113 113 E -> V (in Ref. 6; BAD97107).
{ECO:0000305}.
CONFLICT 406 406 E -> K (in Ref. 3; AAK69655).
{ECO:0000305}.
CONFLICT 443 443 Q -> E (in Ref. 6; BAD97107).
{ECO:0000305}.
CONFLICT 479 479 T -> A (in Ref. 5; BAH13320).
{ECO:0000305}.
SEQUENCE 506 AA; 56921 MW; A21E59A79E1F87E0 CRC64;
MEDHQHVPID IQTSKLLDWL VDRRHCSLKW QSLVLTIREK INAAIQDMPE SEEIAQLLSG
SYIHYFHCLR ILDLLKGTEA STKNIFGRYS SQRMKDWQEI IALYEKDNTY LVELSSLLVR
NVNYEIPSLK KQIAKCQQLQ QEYSRKEEEC QAGAAEMREQ FYHSCKQYGI TGENVRGELL
ALVKDLPSQL AEIGAAAQQS LGEAIDVYQA SVGFVCESPT EQVLPMLRFV QKRGNSTVYE
WRTGTEPSVV ERPHLEELPE QVAEDAIDWG DFGVEAVSEG TDSGISAEAA GIDWGIFPES
DSKDPGGDGI DWGDDAVALQ ITVLEAGTQA PEGVARGPDA LTLLEYTETR NQFLDELMEL
EIFLAQRAVE LSEEADVLSV SQFQLAPAIL QGQTKEKMVT MVSVLEDLIG KLTSLQLQHL
FMILASPRYV DRVTEFLQQK LKQSQLLALK KELMVQKQQE ALEEQAALEP KLDLLLEKTK
ELQKLIEADI SKRYSGRPVN LMGTSL


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