CK5P3_HUMAN
ID CK5P3_HUMAN Reviewed; 506 AA.
AC Q96JB5; B7Z6N4; D3DTU1; D3DTU2; F5H3I5; Q53FA2; Q9H3F8; Q9H8G0; Q9HBR9;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=CDK5 regulatory subunit-associated protein 3 {ECO:0000305};
DE AltName: Full=CDK5 activator-binding protein C53 {ECO:0000305|PubMed:10721722};
DE AltName: Full=LXXLL/leucine-zipper-containing ARF-binding protein {ECO:0000303|PubMed:20164180};
DE AltName: Full=Protein HSF-27 {ECO:0000312|EMBL:AAK69655.1};
GN Name=CDK5RAP3 {ECO:0000312|HGNC:HGNC:18673};
GN Synonyms=IC53 {ECO:0000303|PubMed:20164180},
GN LZAP {ECO:0000303|PubMed:20164180}; ORFNames=MSTP016, OK/SW-cl.114, PP1553;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Aorta;
RX PubMed=12054757; DOI=10.1016/s0006-291x(02)00446-1;
RA Chen J., Liu B., Liu Y.Q., Han Y., Yu H., Zhang Y., Lu L., Zhen Y.,
RA Hui R.T.;
RT "A novel gene IC53 stimulates ECV304 cell proliferation and is upregulated
RT in failing heart.";
RL Biochem. Biophys. Res. Commun. 294:161-166(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH CDK5R1,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=12737517; DOI=10.1038/sj.cr.7290153;
RA Xie Y.H., He X.H., Tang Y.T., Li J.J., Pan Z.M., Qin W.X., Wan da F.,
RA Gu J.R.;
RT "Cloning and characterization of human IC53-2, a novel CDK5 activator
RT binding protein.";
RL Cell Res. 13:83-91(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Favier A.-L., Harsi C., Chrobozcek J.;
RT "Protein interacting with the receptor binding domain of enteric adenovirus
RT serotype 41 fiber protein.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Placenta, and Rectum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Synovial cell;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP TISSUE SPECIFICITY.
RX PubMed=10721722; DOI=10.1016/s0378-1119(99)00499-0;
RA Ching Y.-P., Qi Z., Wang J.H.;
RT "Cloning of three novel neuronal Cdk5 activator binding proteins.";
RL Gene 242:285-294(2000).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CCNB1.
RX PubMed=15790566; DOI=10.1074/jbc.m413431200;
RA Jiang H., Luo S., Li H.;
RT "Cdk5 activator-binding protein C53 regulates apoptosis induced by
RT genotoxic stress via modulating the G2/M DNA damage checkpoint.";
RL J. Biol. Chem. 280:20651-20659(2005).
RN [12]
RP FUNCTION, INTERACTION WITH CDKN2A/ARF AND MDM2, AND SUBCELLULAR LOCATION.
RX PubMed=16173922; DOI=10.1042/bj20050960;
RA Wang J., He X., Luo Y., Yarbrough W.G.;
RT "A novel ARF-binding protein (LZAP) alters ARF regulation of HDM2.";
RL Biochem. J. 393:489-501(2006).
RN [13]
RP FUNCTION, AND INTERACTION WITH RELA.
RX PubMed=17785205; DOI=10.1016/j.ccr.2007.07.002;
RA Wang J., An H., Mayo M.W., Baldwin A.S., Yarbrough W.G.;
RT "LZAP, a putative tumor suppressor, selectively inhibits NF-kappaB.";
RL Cancer Cell 12:239-251(2007).
RN [14]
RP FUNCTION, INTERACTION WITH CHEK1, REGION, AND SUBCELLULAR LOCATION.
RX PubMed=19223857; DOI=10.1038/cr.2009.14;
RA Jiang H., Wu J., He C., Yang W., Li H.;
RT "Tumor suppressor protein C53 antagonizes checkpoint kinases to promote
RT cyclin-dependent kinase 1 activation.";
RL Cell Res. 19:458-468(2009).
RN [15]
RP INTERACTION WITH UFL1.
RX PubMed=20164180; DOI=10.1074/jbc.m109.065920;
RA Kwon J., Cho H.J., Han S.H., No J.G., Kwon J.Y., Kim H.;
RT "A novel LZAP-binding protein, NLBP, inhibits cell invasion.";
RL J. Biol. Chem. 285:12232-12240(2010).
RN [16]
RP FUNCTION, INTERACTION WITH DDRGK1 AND UFL1, REGION, AND UBIQUITINATION.
RX PubMed=20228063; DOI=10.1074/jbc.m110.110619;
RA Wu J., Lei G., Mei M., Tang Y., Li H.;
RT "A novel C53/LZAP-interacting protein regulates stability of C53/LZAP and
RT DDRGK domain-containing Protein 1 (DDRGK1) and modulates NF-kappaB
RT signaling.";
RL J. Biol. Chem. 285:15126-15136(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP FUNCTION, AND INTERACTION WITH MAPK14.
RX PubMed=21283629; DOI=10.1371/journal.pone.0016427;
RA An H., Lu X., Liu D., Yarbrough W.G.;
RT "LZAP inhibits p38 MAPK (p38) phosphorylation and activity by facilitating
RT p38 association with the wild-type p53 induced phosphatase 1 (WIP1).";
RL PLoS ONE 6:E16427-E16427(2011).
RN [19]
RP INTERACTION WITH TUBG1.
RX PubMed=21465471; DOI=10.1002/jcp.22772;
RA Horejsi B., Vinopal S., Sladkova V., Draberova E., Sulimenko V.,
RA Sulimenko T., Vosecka V., Philimonenko A., Hozak P., Katsetos C.D.,
RA Draber P.;
RT "Nuclear gamma-tubulin associates with nucleoli and interacts with tumor
RT suppressor protein C53.";
RL J. Cell. Physiol. 227:367-382(2012).
RN [20]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HEPATITIS B VIRUS
RP LARGE ENVELOPE PROTEIN.
RX PubMed=21971960; DOI=10.3892/or.2011.1489;
RA Lei Y., Liu H., Yang Y., Wang X., Ren N., Li B., Liu S., Cheng J., Fu X.,
RA Zhang J.;
RT "Interaction of LHBs with C53 promotes hepatocyte mitotic entry: A novel
RT mechanism for HBV-induced hepatocellular carcinoma.";
RL Oncol. Rep. 27:151-159(2012).
RN [21]
RP FUNCTION.
RX PubMed=23152784; DOI=10.1371/journal.pone.0048587;
RA Zhang Y., Zhang M., Wu J., Lei G., Li H.;
RT "Transcriptional regulation of the Ufm1 conjugation system in response to
RT disturbance of the endoplasmic reticulum homeostasis and inhibition of
RT vesicle trafficking.";
RL PLoS ONE 7:E48587-E48587(2012).
RN [22]
RP FUNCTION, CLEAVAGE BY CASPASES, MUTAGENESIS OF ASP-268; ASP-282 AND
RP ASP-311, AND SUBCELLULAR LOCATION.
RX PubMed=23478299; DOI=10.1038/cr.2013.36;
RA Wu J., Jiang H., Luo S., Zhang M., Zhang Y., Sun F., Huang S., Li H.;
RT "Caspase-mediated cleavage of C53/LZAP protein causes abnormal microtubule
RT bundling and rupture of the nuclear envelope.";
RL Cell Res. 23:691-704(2013).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-450, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [26]
RP FUNCTION.
RX PubMed=30635284; DOI=10.1242/dev.169235;
RA Yang R., Wang H., Kang B., Chen B., Shi Y., Yang S., Sun L., Liu Y.,
RA Xiao W., Zhang T., Yang J., Zhang Y., Zhu M., Xu P., Chang Y., Jia Y.,
RA Huang Y.;
RT "CDK5RAP3, a UFL1 substrate adaptor, is crucial for liver development.";
RL Development 146:0-0(2019).
CC -!- FUNCTION: Substrate adapter for ufmylation, the covalent attachment of
CC the ubiquitin-like modifier UFM1 to substrate proteins, in response to
CC endoplasmic reticulum stress (PubMed:23152784, PubMed:30635284).
CC Negatively regulates NF-kappa-B-mediated gene transcription through the
CC control of RELA phosphorylation (PubMed:17785205, PubMed:20228063).
CC Probable tumor suppressor initially identified as a CDK5R1 interactor
CC controlling cell proliferation (PubMed:12054757, PubMed:12737517). Also
CC regulates mitotic G2/M transition checkpoint and mitotic G2 DNA damage
CC checkpoint (PubMed:15790566, PubMed:19223857). Through its interaction
CC with CDKN2A/ARF and MDM2 may induce MDM2-dependent p53/TP53
CC ubiquitination, stabilization and activation in the nucleus, thereby
CC promoting G1 cell cycle arrest and inhibition of cell proliferation
CC (PubMed:16173922). May also play a role in the rupture of the nuclear
CC envelope during apoptosis (PubMed:23478299). May regulate MAPK14
CC activity by regulating its dephosphorylation by PPM1D/WIP1
CC (PubMed:21283629). Required for liver development (By similarity).
CC {ECO:0000250|UniProtKB:Q99LM2, ECO:0000269|PubMed:12054757,
CC ECO:0000269|PubMed:12737517, ECO:0000269|PubMed:15790566,
CC ECO:0000269|PubMed:16173922, ECO:0000269|PubMed:17785205,
CC ECO:0000269|PubMed:19223857, ECO:0000269|PubMed:20228063,
CC ECO:0000269|PubMed:21283629, ECO:0000269|PubMed:23152784,
CC ECO:0000269|PubMed:23478299, ECO:0000269|PubMed:30635284}.
CC -!- FUNCTION: (Microbial infection) May be negatively regulated by
CC hepatitis B virus large envelope protein mutant pre-s2 to promote
CC mitotic entry. {ECO:0000269|PubMed:21971960}.
CC -!- SUBUNIT: Interacts with CDK5R1; competes with CDK5RAP1 and CDK5RAP2
CC (PubMed:12737517). Interacts with RELA (PubMed:17785205). Interacts
CC with CHEK1; may negatively regulate CHEK1 and thereby stimulate entry
CC into mitosis (PubMed:19223857). Interacts with CDKN2A/ARF and MDM2;
CC forms a ternary complex involved in regulation of p53/TP53
CC (PubMed:16173922). Interacts with UFL1; the interaction is direct
CC (PubMed:20164180, PubMed:20228063). Interaction with UFL1 anchors
CC CDK5RAP3 in the cytoplasm, preventing its translocation to the nucleus
CC which allows expression of the CCND1 cyclin and progression of cells
CC through the G1/S transition (By similarity). Interacts with DDRGK1
CC (PubMed:20228063). Interacts with MAPK14 (PubMed:21283629). Interacts
CC with CCNB1 (PubMed:15790566). Interacts with TUBG1; may regulate
CC CDK5RAP3 in mitotic G2/M transition checkpoint (PubMed:21465471).
CC {ECO:0000250|UniProtKB:Q9JLH7, ECO:0000269|PubMed:12737517,
CC ECO:0000269|PubMed:15790566, ECO:0000269|PubMed:16173922,
CC ECO:0000269|PubMed:17785205, ECO:0000269|PubMed:19223857,
CC ECO:0000269|PubMed:20164180, ECO:0000269|PubMed:20228063,
CC ECO:0000269|PubMed:21283629, ECO:0000269|PubMed:21465471}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus large
CC envelope protein mutant pre-s2; promotes mitotic entry.
CC {ECO:0000269|PubMed:21971960}.
CC -!- INTERACTION:
CC Q96JB5; O75344: FKBP6; NbExp=12; IntAct=EBI-718818, EBI-744771;
CC Q96JB5; Q04206: RELA; NbExp=4; IntAct=EBI-718818, EBI-73886;
CC Q96JB5; Q9UJ04: TSPYL4; NbExp=6; IntAct=EBI-718818, EBI-308511;
CC Q96JB5; O94874: UFL1; NbExp=3; IntAct=EBI-718818, EBI-1048088;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16173922}. Cytoplasm
CC {ECO:0000269|PubMed:15790566, ECO:0000269|PubMed:16173922,
CC ECO:0000269|PubMed:19223857}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:19223857}.
CC Note=Colocalizes and associates with microtubules.
CC {ECO:0000269|PubMed:23478299}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96JB5-1; Sequence=Displayed;
CC Name=2; Synonyms=IC53;
CC IsoId=Q96JB5-2; Sequence=VSP_007566, VSP_007567;
CC Name=3; Synonyms=IC53-2;
CC IsoId=Q96JB5-3; Sequence=VSP_007568;
CC Name=4;
CC IsoId=Q96JB5-4; Sequence=VSP_055646;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:12054757,
CC PubMed:10721722). Expressed in heart, brain, placenta, lung, liver,
CC skeletal muscle, kidney and pancreas. Isoform 3 is expressed in kidney,
CC liver, skeletal muscle and placenta (PubMed:12737517).
CC {ECO:0000269|PubMed:10721722, ECO:0000269|PubMed:12054757,
CC ECO:0000269|PubMed:12737517}.
CC -!- PTM: May be phosphorylated by CDK5. {ECO:0000250|UniProtKB:Q9JLH7}.
CC -!- PTM: Ubiquitinated. Probably triggers proteasomal degradation and is
CC negatively regulated by UFL1. {ECO:0000269|PubMed:20228063}.
CC -!- PTM: May be ufmylated. {ECO:0000250|UniProtKB:Q99LM2}.
CC -!- PTM: Cleaved by caspases early during apoptosis, the resulting peptides
CC may play a role in rupture of the nuclear envelope.
CC {ECO:0000269|PubMed:23478299}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to an intron retention. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CDK5RAP3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK69655.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF110322; AAG39277.1; -; mRNA.
DR EMBL; AF217982; AAG17225.1; -; mRNA.
DR EMBL; AF343090; AAK69655.1; ALT_FRAME; mRNA.
DR EMBL; AB062433; BAB93496.1; -; mRNA.
DR EMBL; AK023722; BAB14657.1; -; mRNA.
DR EMBL; AK300643; BAH13320.1; -; mRNA.
DR EMBL; AK223387; BAD97107.1; -; mRNA.
DR EMBL; AC018521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94772.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94774.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94775.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94778.1; -; Genomic_DNA.
DR EMBL; BC009957; AAH09957.1; -; mRNA.
DR EMBL; BC072435; AAH72435.1; -; mRNA.
DR CCDS; CCDS42356.1; -. [Q96JB5-1]
DR CCDS; CCDS62232.1; -. [Q96JB5-4]
DR PIR; JC7863; JC7863.
DR RefSeq; NP_001265126.1; NM_001278197.1. [Q96JB5-4]
DR RefSeq; NP_001265127.1; NM_001278198.1.
DR RefSeq; NP_001265145.1; NM_001278216.1. [Q96JB5-3]
DR RefSeq; NP_001265146.1; NM_001278217.1. [Q96JB5-2]
DR RefSeq; NP_788276.1; NM_176096.2. [Q96JB5-1]
DR RefSeq; XP_011523599.1; XM_011525297.1. [Q96JB5-4]
DR RefSeq; XP_016880653.1; XM_017025164.1. [Q96JB5-2]
DR RefSeq; XP_016880654.1; XM_017025165.1. [Q96JB5-2]
DR AlphaFoldDB; Q96JB5; -.
DR SMR; Q96JB5; -.
DR BioGRID; 123213; 155.
DR IntAct; Q96JB5; 45.
DR MINT; Q96JB5; -.
DR STRING; 9606.ENSP00000438886; -.
DR iPTMnet; Q96JB5; -.
DR PhosphoSitePlus; Q96JB5; -.
DR SwissPalm; Q96JB5; -.
DR BioMuta; CDK5RAP3; -.
DR DMDM; 32129444; -.
DR EPD; Q96JB5; -.
DR jPOST; Q96JB5; -.
DR MassIVE; Q96JB5; -.
DR MaxQB; Q96JB5; -.
DR PaxDb; Q96JB5; -.
DR PeptideAtlas; Q96JB5; -.
DR PRIDE; Q96JB5; -.
DR ProteomicsDB; 26284; -.
DR ProteomicsDB; 76930; -. [Q96JB5-1]
DR ProteomicsDB; 76931; -. [Q96JB5-2]
DR ProteomicsDB; 76932; -. [Q96JB5-3]
DR Antibodypedia; 8591; 237 antibodies from 31 providers.
DR DNASU; 80279; -.
DR Ensembl; ENST00000338399.9; ENSP00000344683.4; ENSG00000108465.15. [Q96JB5-1]
DR Ensembl; ENST00000536708.6; ENSP00000438886.2; ENSG00000108465.15. [Q96JB5-4]
DR GeneID; 80279; -.
DR KEGG; hsa:80279; -.
DR MANE-Select; ENST00000338399.9; ENSP00000344683.4; NM_176096.3; NP_788276.1.
DR UCSC; uc002imr.5; human. [Q96JB5-1]
DR CTD; 80279; -.
DR DisGeNET; 80279; -.
DR GeneCards; CDK5RAP3; -.
DR HGNC; HGNC:18673; CDK5RAP3.
DR HPA; ENSG00000108465; Low tissue specificity.
DR MIM; 608202; gene.
DR neXtProt; NX_Q96JB5; -.
DR OpenTargets; ENSG00000108465; -.
DR PharmGKB; PA38633; -.
DR VEuPathDB; HostDB:ENSG00000108465; -.
DR eggNOG; KOG2607; Eukaryota.
DR GeneTree; ENSGT00390000000713; -.
DR HOGENOM; CLU_025645_1_0_1; -.
DR InParanoid; Q96JB5; -.
DR OMA; PGVRKQM; -.
DR OrthoDB; 619606at2759; -.
DR PhylomeDB; Q96JB5; -.
DR PathwayCommons; Q96JB5; -.
DR SignaLink; Q96JB5; -.
DR BioGRID-ORCS; 80279; 56 hits in 1091 CRISPR screens.
DR ChiTaRS; CDK5RAP3; human.
DR GeneWiki; CDK5RAP3; -.
DR GenomeRNAi; 80279; -.
DR Pharos; Q96JB5; Tbio.
DR PRO; PR:Q96JB5; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96JB5; protein.
DR Bgee; ENSG00000108465; Expressed in pituitary gland and 91 other tissues.
DR ExpressionAtlas; Q96JB5; baseline and differential.
DR Genevisible; Q96JB5; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:UniProtKB.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IDA:MGI.
DR GO; GO:0030262; P:apoptotic nuclear changes; IMP:UniProtKB.
DR GO; GO:0007420; P:brain development; NAS:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB.
DR GO; GO:0060318; P:definitive erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
DR GO; GO:0001889; P:liver development; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; IMP:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0044387; P:negative regulation of protein kinase activity by regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0071569; P:protein ufmylation; IDA:MGI.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045664; P:regulation of neuron differentiation; NAS:UniProtKB.
DR GO; GO:0010921; P:regulation of phosphatase activity; IMP:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR InterPro; IPR008491; CDK5RAP3.
DR PANTHER; PTHR14894; PTHR14894; 1.
DR Pfam; PF05600; DUF773; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Host-virus interaction;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..506
FT /note="CDK5 regulatory subunit-associated protein 3"
FT /id="PRO_0000220516"
FT REGION 269..506
FT /note="Required for interaction with UFL1 and mediates
FT interaction with CHEK1"
FT /evidence="ECO:0000269|PubMed:19223857,
FT ECO:0000269|PubMed:20228063"
FT CROSSLNK 450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364"
FT VAR_SEQ 1..225
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12737517"
FT /id="VSP_007568"
FT VAR_SEQ 1..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12054757"
FT /id="VSP_007566"
FT VAR_SEQ 1..2
FT /note="ME -> MRRQSMTSATRDLHTALDGKATQGGKK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055646"
FT VAR_SEQ 88..111
FT /note="RYSSQRMKDWQEIIALYEKDNTYL -> MCVHPGACLPHVGVSWAEFPGHFS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12054757"
FT /id="VSP_007567"
FT VARIANT 324
FT /note="L -> V (in dbSNP:rs35054799)"
FT /id="VAR_048688"
FT MUTAGEN 268
FT /note="D->E: Alters cleavage by CASP3 in vitro. Prevents
FT apoptosis-induced cleavage in vivo; when associated with E-
FT 282 and E-311."
FT /evidence="ECO:0000269|PubMed:23478299"
FT MUTAGEN 282
FT /note="D->E: Alters cleavage by CASP3 in vitro. Prevents
FT apoptosis-induced cleavage in vivo; when associated with E-
FT 268 and E-311."
FT /evidence="ECO:0000269|PubMed:23478299"
FT MUTAGEN 311
FT /note="D->E: Alters cleavage by CASP3 in vitro. Prevents
FT apoptosis-induced cleavage in vivo; when associated with E-
FT 268 and E-282."
FT /evidence="ECO:0000269|PubMed:23478299"
FT CONFLICT 98
FT /note="Q -> R (in Ref. 5; BAH13320)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="E -> V (in Ref. 6; BAD97107)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="E -> K (in Ref. 3; AAK69655)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="Q -> E (in Ref. 6; BAD97107)"
FT /evidence="ECO:0000305"
FT CONFLICT 479
FT /note="T -> A (in Ref. 5; BAH13320)"
FT /evidence="ECO:0000305"
SQ 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
