CAND2_HUMAN
ID CAND2_HUMAN Reviewed; 1236 AA.
AC O75155; B9EGM9; E9KL24;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cullin-associated NEDD8-dissociated protein 2;
DE AltName: Full=Cullin-associated and neddylation-dissociated protein 2;
DE AltName: Full=Epididymis tissue protein Li 169;
DE AltName: Full=TBP-interacting protein of 120 kDa B;
DE Short=TBP-interacting protein 120B;
DE AltName: Full=p120 CAND2;
GN Name=CAND2; Synonyms=KIAA0667, TIP120B;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Epididymis;
RX PubMed=20736409; DOI=10.1074/mcp.m110.001719;
RA Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C.,
RA Jin S., Liu J., Zhu P., Liu Y.;
RT "Systematic mapping and functional analysis of a family of human epididymal
RT secretory sperm-located proteins.";
RL Mol. Cell. Proteomics 9:2517-2528(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP PROTEIN SEQUENCE OF 2-14 AND 864-878, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Ramsay A., Leung H.Y.;
RL Submitted (MAR-2009) to UniProtKB.
RN [4]
RP PROTEIN SEQUENCE OF 2-14 AND 606-620, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1236 (ISOFORM 1), AND VARIANTS
RP PRO-858 AND THR-1225.
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-1236 (ISOFORM 2), AND VARIANTS
RP ARG-408 AND PRO-858.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [7]
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).
CC -!- FUNCTION: Probable assembly factor of SCF (SKP1-CUL1-F-box protein) E3
CC ubiquitin ligase complexes that promotes the exchange of the substrate-
CC recognition F-box subunit in SCF complexes, thereby playing a key role
CC in the cellular repertoire of SCF complexes. {ECO:0000250}.
CC -!- SUBUNIT: Binds TBP, CNOT3 and UBE3C. {ECO:0000250}.
CC -!- INTERACTION:
CC O75155; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-5656182, EBI-7062247;
CC O75155; Q14192: FHL2; NbExp=3; IntAct=EBI-5656182, EBI-701903;
CC O75155; P08247: SYP; NbExp=3; IntAct=EBI-5656182, EBI-9071725;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75155-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75155-2; Sequence=VSP_037240, VSP_037241, VSP_037242;
CC -!- TISSUE SPECIFICITY: Expressed in epididymis (at protein level).
CC {ECO:0000269|PubMed:20736409}.
CC -!- PTM: Ubiquitinated and targeted for proteasomal degradation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI36593.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; GU727621; ADU87623.1; -; mRNA.
DR EMBL; AC034198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136592; AAI36593.1; ALT_INIT; mRNA.
DR EMBL; AB014567; BAA31642.1; -; mRNA.
DR CCDS; CCDS43053.1; -. [O75155-2]
DR CCDS; CCDS54554.1; -. [O75155-1]
DR PIR; T01239; T01239.
DR RefSeq; NP_001155971.1; NM_001162499.1. [O75155-1]
DR RefSeq; NP_036430.1; NM_012298.2. [O75155-2]
DR AlphaFoldDB; O75155; -.
DR SMR; O75155; -.
DR BioGRID; 116701; 79.
DR IntAct; O75155; 36.
DR MINT; O75155; -.
DR STRING; 9606.ENSP00000387641; -.
DR GlyGen; O75155; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; O75155; -.
DR PhosphoSitePlus; O75155; -.
DR BioMuta; CAND2; -.
DR EPD; O75155; -.
DR jPOST; O75155; -.
DR MassIVE; O75155; -.
DR MaxQB; O75155; -.
DR PaxDb; O75155; -.
DR PeptideAtlas; O75155; -.
DR PRIDE; O75155; -.
DR ProteomicsDB; 49823; -. [O75155-1]
DR ProteomicsDB; 49824; -. [O75155-2]
DR Antibodypedia; 5869; 68 antibodies from 21 providers.
DR DNASU; 23066; -.
DR Ensembl; ENST00000295989.9; ENSP00000295989.5; ENSG00000144712.12. [O75155-2]
DR Ensembl; ENST00000456430.6; ENSP00000387641.2; ENSG00000144712.12. [O75155-1]
DR GeneID; 23066; -.
DR KEGG; hsa:23066; -.
DR MANE-Select; ENST00000456430.6; ENSP00000387641.2; NM_001162499.2; NP_001155971.1.
DR UCSC; uc003bxj.3; human. [O75155-1]
DR CTD; 23066; -.
DR DisGeNET; 23066; -.
DR GeneCards; CAND2; -.
DR HGNC; HGNC:30689; CAND2.
DR HPA; ENSG00000144712; Tissue enhanced (skeletal).
DR MIM; 610403; gene.
DR neXtProt; NX_O75155; -.
DR OpenTargets; ENSG00000144712; -.
DR PharmGKB; PA142672208; -.
DR VEuPathDB; HostDB:ENSG00000144712; -.
DR eggNOG; KOG1824; Eukaryota.
DR GeneTree; ENSGT00390000017740; -.
DR HOGENOM; CLU_007157_1_0_1; -.
DR InParanoid; O75155; -.
DR OMA; TNMRSDK; -.
DR OrthoDB; 194023at2759; -.
DR PhylomeDB; O75155; -.
DR TreeFam; TF300355; -.
DR PathwayCommons; O75155; -.
DR SignaLink; O75155; -.
DR SIGNOR; O75155; -.
DR BioGRID-ORCS; 23066; 15 hits in 1084 CRISPR screens.
DR ChiTaRS; CAND2; human.
DR GenomeRNAi; 23066; -.
DR Pharos; O75155; Tbio.
DR PRO; PR:O75155; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O75155; protein.
DR Bgee; ENSG00000144712; Expressed in skeletal muscle tissue of rectus abdominis and 181 other tissues.
DR ExpressionAtlas; O75155; baseline and differential.
DR Genevisible; O75155; HS.
DR GO; GO:0005829; C:cytosol; IDA:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010265; P:SCF complex assembly; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039852; CAND1/CAND2.
DR InterPro; IPR013932; TATA-bd_TIP120.
DR PANTHER; PTHR12696; PTHR12696; 1.
DR Pfam; PF08623; TIP120; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing; Nucleus;
KW Reference proteome; Repeat; Transcription; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT CHAIN 2..1236
FT /note="Cullin-associated NEDD8-dissociated protein 2"
FT /id="PRO_0000089297"
FT REPEAT 2..39
FT /note="HEAT 1"
FT REPEAT 44..81
FT /note="HEAT 2"
FT REPEAT 83..119
FT /note="HEAT 3"
FT REPEAT 129..167
FT /note="HEAT 4"
FT REPEAT 171..208
FT /note="HEAT 5"
FT REPEAT 210..246
FT /note="HEAT 6"
FT REPEAT 254..291
FT /note="HEAT 7"
FT REPEAT 327..368
FT /note="HEAT 8"
FT REPEAT 372..409
FT /note="HEAT 9"
FT REPEAT 432..469
FT /note="HEAT 10"
FT REPEAT 517..554
FT /note="HEAT 11"
FT REPEAT 565..604
FT /note="HEAT 12"
FT REPEAT 608..645
FT /note="HEAT 13"
FT REPEAT 648..685
FT /note="HEAT 14"
FT REPEAT 690..727
FT /note="HEAT 15"
FT REPEAT 731..770
FT /note="HEAT 16"
FT REPEAT 772..813
FT /note="HEAT 17"
FT REPEAT 857..894
FT /note="HEAT 18"
FT REPEAT 896..931
FT /note="HEAT 19"
FT REPEAT 933..966
FT /note="HEAT 20"
FT REPEAT 967..1003
FT /note="HEAT 21"
FT REPEAT 1007..1044
FT /note="HEAT 22"
FT REPEAT 1048..1084
FT /note="HEAT 23"
FT REPEAT 1105..1141
FT /note="HEAT 24"
FT REPEAT 1157..1194
FT /note="HEAT 25"
FT REPEAT 1204..1236
FT /note="HEAT 26"
FT REGION 315..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..344
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.3, ECO:0000269|Ref.4"
FT VAR_SEQ 71
FT /note="C -> W (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_037240"
FT VAR_SEQ 72..164
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_037241"
FT VAR_SEQ 1014..1037
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_037242"
FT VARIANT 408
FT /note="Q -> R (in dbSNP:rs2305398)"
FT /evidence="ECO:0000269|PubMed:9734811"
FT /id="VAR_055023"
FT VARIANT 476
FT /note="P -> L (in dbSNP:rs2305397)"
FT /id="VAR_055024"
FT VARIANT 533
FT /note="S -> P (in dbSNP:rs3732675)"
FT /id="VAR_055025"
FT VARIANT 655
FT /note="H -> R (in dbSNP:rs9838943)"
FT /id="VAR_055026"
FT VARIANT 845
FT /note="L -> F (in dbSNP:rs17037287)"
FT /id="VAR_055027"
FT VARIANT 858
FT /note="H -> P (in dbSNP:rs3732678)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_055028"
FT VARIANT 990
FT /note="V -> I (in dbSNP:rs3817121)"
FT /id="VAR_055029"
FT VARIANT 1225
FT /note="A -> T (in dbSNP:rs12629133)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055030"
FT CONFLICT 204
FT /note="A -> T (in Ref. 6; BAA31642)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1236 AA; 135256 MW; 38F43A7C1B8322A8 CRC64;
MSTAAFHISS LLEKMTSSDK DFRFMATSDL MSELQKDSIQ LDEDSERKVV KMLLRLLEDK
NGEVQNLAVK CLGPLVVKVK EYQVETIVDT LCTNMRSDKE QLRDIAGIGL KTVLSELPPA
ATGSGLATNV CRKITGQLTS AIAQQEDVAV QLEALDILSD MLSRLGVPLG AFHASLLHCL
LPQLSSPRLA VRKRAVGALG HLAAACSTDL FVELADHLLD RLPGPRVPTS PTAIRTLIQC
LGSVGRQAGH RLGAHLDRLV PLVEDFCNLD DDELRESCLQ AFEAFLRKCP KEMGPHVPNV
TSLCLQYIKH DPNYNYDSDE DEEQMETEDS EFSEQESEDE YSDDDDMSWK VRRAAAKCIA
ALISSRPDLL PDFHCTLAPV LIRRFKEREE NVKADVFTAY IVLLRQTQPP KGWLEAMEEP
TQTGSNLHML RGQVPLVVKA LQRQLKDRSV RARQGCFSLL TELAGVLPGS LAEHMPVLVS
GIIFSLADRS SSSTIRMDAL AFLQGLLGTE PAEAFHPHLP ILLPPVMACV ADSFYKIAAE
ALVVLQELVR ALWPLHRPRM LDPEPYVGEM SAVTLARLRA TDLDQEVKER AISCMGHLVG
HLGDRLGDDL EPTLLLLLDR LRNEITRLPA IKALTLVAVS PLQLDLQPIL AEALHILASF
LRKNQRALRL ATLAALDALA QSQGLSLPPS AVQAVLAELP ALVNESDMHV AQLAVDFLAT
VTQAQPASLV EVSGPVLSEL LRLLRSPLLP AGVLAAAEGF LQALVGTRPP CVDYAKLISL
LTAPVYEQAV DGGPGLHKQV FHSLARCVAA LSAACPQEAA STASRLVCDA RSPHSSTGVK
VLAFLSLAEV GQVAGPGHQR ELKAVLLEAL GSPSEDVRAA ASYALGRVGA GSLPDFLPFL
LEQIEAEPRR QYLLLHSLRE ALGAAQPDSL KPYAEDIWAL LFQRCEGAEE GTRGVVAECI
GKLVLVNPSF LLPRLRKQLA AGRPHTRSTV ITAVKFLISD QPHPIDPLLK SFIGEFMESL
QDPDLNVRRA TLAFFNSAVH NKPSLVRDLL DDILPLLYQE TKIRRDLIRE VEMGPFKHTV
DDGLDVRKAA FECMYSLLES CLGQLDICEF LNHVEDGLKD HYDIRMLTFI MVARLATLCP
APVLQRVDRL IEPLRATCTA KVKAGSVKQE FEKQDELKRS AMRAVAALLT IPEVGKSPIM
ADFSSQIRSN PELAALFESI QKDSASAPST DSMELS
