ID CAND1_HUMAN Reviewed; 1230 AA. AC Q86VP6; B2RAU3; O94918; Q6PIY4; Q8NDJ4; Q96JZ9; Q96T19; Q9BTC4; Q9H0G2; AC Q9P0H7; Q9UF85; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 27-MAR-2024, entry version 193. DE RecName: Full=Cullin-associated NEDD8-dissociated protein 1; DE AltName: Full=Cullin-associated and neddylation-dissociated protein 1; DE AltName: Full=TBP-interacting protein of 120 kDa A; DE Short=TBP-interacting protein 120A; DE AltName: Full=p120 CAND1; GN Name=CAND1; Synonyms=KIAA0829, TIP120, TIP120A; 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 [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [2] RP SEQUENCE REVISION. RA Ohara O., Nagase T., Kikuno R., Ishikawa K., Suyama M.; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Adrenal gland; RX PubMed=10931946; DOI=10.1073/pnas.160270997; RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J., RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., RA Chen M.-D., Chen J.-L.; RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis RT and full-length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-952. RC TISSUE=Cervix, Testis, and Uterus; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Placenta; 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 [8] RP PROTEIN SEQUENCE OF 2-14 AND 374-382, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT ALA-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 [9] RP PROTEIN SEQUENCE OF 2-14; 535-548; 668-679; 730-743; 859-873; 958-969 AND RP 983-990, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [10] RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH RP CUL1 AND RBX1. RX PubMed=12504026; DOI=10.1016/s1097-2765(02)00784-0; RA Zheng J., Yang X., Harrell J.M., Ryzhikov S., Shim E.-H., RA Lykke-Andersen K., Wei N., Sun H., Kobayashi R., Zhang H.; RT "CAND1 binds to unneddylated CUL1 and regulates the formation of SCF RT ubiquitin E3 ligase complex."; RL Mol. Cell 10:1519-1526(2002). RN [11] RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH CUL1 AND RBX1, AND INTERACTION RP WITH UNNEDDYLATED CUL1; CUL4A AND CUL5. RX PubMed=12504025; DOI=10.1016/s1097-2765(02)00783-9; RA Liu J., Furukawa M., Matsumoto T., Xiong Y.; RT "NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1- RT SKP1 binding and SCF ligases."; RL Mol. Cell 10:1511-1518(2002). RN [12] RP FUNCTION, INTERACTION WITH CUL1; CUL2; CUL3; CUL4A; CUL4B AND RBX1, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12609982; DOI=10.1074/jbc.m213070200; RA Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.; RT "TIP120A associates with cullins and modulates ubiquitin ligase activity."; RL J. Biol. Chem. 278:15905-15910(2003). RN [13] RP FUNCTION, AND INTERACTION WITH CUL3. RX PubMed=16449638; DOI=10.1128/mcb.26.4.1235-1244.2006; RA Lo S.C., Hannink M.; RT "CAND1-mediated substrate adaptor recycling is required for efficient RT repression of Nrf2 by Keap1."; RL Mol. Cell. Biol. 26:1235-1244(2006). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55 AND LYS-971, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [18] RP INDUCTION. RX PubMed=20820187; DOI=10.1038/pcan.2010.32; RA Murata T., Takayama K., Katayama S., Urano T., Horie-Inoue K., Ikeda K., RA Takahashi S., Kawazu C., Hasegawa A., Ouchi Y., Homma Y., Hayashizaki Y., RA Inoue S.; RT "miR-148a is an androgen-responsive microRNA that promotes LNCaP prostate RT cell growth by repressing its target CAND1 expression."; RL Prostate Cancer Prostatic Dis. 13:356-361(2010). RN [19] 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 [20] RP INTERACTION WITH CUL2. RX PubMed=21778237; DOI=10.1074/jbc.m111.278408; RA Mao X., Gluck N., Chen B., Starokadomskyy P., Li H., Maine G.N., RA Burstein E.; RT "COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates RT Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8- RT dissociated protein 1) binding."; RL J. Biol. Chem. 286:32355-32365(2011). RN [21] RP FUNCTION, INTERACTION WITH CUL2; CUL3; CUL4A AND CUL5, AND SUBCELLULAR RP LOCATION. RX PubMed=21249194; DOI=10.1371/journal.pone.0016071; RA Chua Y.S., Boh B.K., Ponyeam W., Hagen T.; RT "Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo."; RL PLoS ONE 6:E16071-E16071(2011). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [24] RP FUNCTION, AND REACTION MECHANISM. RX PubMed=23453757; DOI=10.1016/j.cell.2013.02.024; RA Pierce N.W., Lee J.E., Liu X., Sweredoski M.J., Graham R.L., Larimore E.A., RA Rome M., Zheng N., Clurman B.E., Hess S., Shan S.O., Deshaies R.J.; RT "Cand1 promotes assembly of new SCF complexes through dynamic exchange of F RT box proteins."; RL Cell 153:206-215(2013). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [26] RP INTERACTION WITH DCUN1D5. RX PubMed=24192928; DOI=10.1158/1078-0432.ccr-13-1252; RA Bommelje C.C., Weeda V.B., Huang G., Shah K., Bains S., Buss E., Shaha M., RA Goenen M., Ghossein R., Ramanathan S.Y., Singh B.; RT "Oncogenic function of SCCRO5/DCUN1D5 requires its Neddylation E3 activity RT and nuclear localization."; RL Clin. Cancer Res. 20:372-381(2014). RN [27] RP INTERACTION WITH DCUN1D3. RX PubMed=25349211; DOI=10.1074/jbc.m114.585505; RA Huang G., Stock C., Bommelje C.C., Weeda V.B., Shah K., Bains S., Buss E., RA Shaha M., Rechler W., Ramanathan S.Y., Singh B.; RT "SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of RT SCCRO (DCUN1D1)."; RL J. Biol. Chem. 289:34728-34742(2014). RN [28] 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 [29] RP INTERACTION WITH ERCC6. RX PubMed=26030138; DOI=10.1371/journal.pone.0128558; RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G., RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.; RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin RT Dynamics."; RL PLoS ONE 10:E0128558-E0128558(2015). RN [30] 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 [31] RP INTERACTION WITH DCUN1D1; DCUN1D2; DCUN1D3; DCUN1D4 AND DCUN1D5. RX PubMed=26906416; DOI=10.1242/jcs.181784; RA Keuss M.J., Thomas Y., Mcarthur R., Wood N.T., Knebel A., Kurz T.; RT "Characterization of the mammalian family of DCN-type NEDD8 E3 ligases."; RL J. Cell Sci. 129:1441-1454(2016). RN [32] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH CUL1 AND RBX1. RX PubMed=15537541; DOI=10.1016/j.cell.2004.10.019; RA Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J., Xiong Y., RA Zheng N.; RT "Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for RT the assembly of the multisubunit cullin-dependent ubiquitin ligases."; RL Cell 119:517-528(2004). RN [33] RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) IN COMPLEX WITH CUL4B AND RBX1. RX PubMed=22118460; DOI=10.1016/j.cell.2011.10.035; RA Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M., Faty M., RA Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S., Gut H., RA Sugasawa K., Thoma N.H.; RT "The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, RT targeting, and activation."; RL Cell 147:1024-1039(2011). CC -!- FUNCTION: Key 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. Acts as a F-box protein CC exchange factor. The exchange activity of CAND1 is coupled with cycles CC of neddylation conjugation: in the deneddylated state, cullin-binding CC CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and CC promoting exchange of the F-box protein. Probably plays a similar role CC in other cullin-RING E3 ubiquitin ligase complexes. CC {ECO:0000269|PubMed:12504025, ECO:0000269|PubMed:12504026, CC ECO:0000269|PubMed:12609982, ECO:0000269|PubMed:16449638, CC ECO:0000269|PubMed:21249194, ECO:0000269|PubMed:23453757}. CC -!- SUBUNIT: Interacts with TBP (By similarity). Part of a complex that CC contains CUL1 and RBX1. Interacts with unneddylated cullins: interacts CC with CUL1, CUL2, CUL3, CUL4A, CUL4B and CUL5. Does not bind neddylated CC CUL1. Interaction with cullins is abolished in presence of COMMD1, CC which antagonizes with CAND1 for interacting with cullins. Interacts CC with ERCC6 (PubMed:26030138). Interacts with DCUN1D1, DCUN1D2, DCUN1D3, CC DCUN1D4 and DCUN1D5; these interactions are bridged by cullins and CC strongly inhibits the neddylation of cullins (PubMed:24192928, CC PubMed:26906416, PubMed:25349211). {ECO:0000250|UniProtKB:P97536, CC ECO:0000269|PubMed:12504025, ECO:0000269|PubMed:12504026, CC ECO:0000269|PubMed:12609982, ECO:0000269|PubMed:15537541, CC ECO:0000269|PubMed:16449638, ECO:0000269|PubMed:21249194, CC ECO:0000269|PubMed:21778237, ECO:0000269|PubMed:22118460, CC ECO:0000269|PubMed:24192928, ECO:0000269|PubMed:25349211, CC ECO:0000269|PubMed:26030138, ECO:0000269|PubMed:26906416}. CC -!- INTERACTION: CC Q86VP6; Q13616: CUL1; NbExp=33; IntAct=EBI-456077, EBI-359390; CC Q86VP6; Q13617: CUL2; NbExp=3; IntAct=EBI-456077, EBI-456179; CC Q86VP6; Q13618: CUL3; NbExp=8; IntAct=EBI-456077, EBI-456129; CC Q86VP6; Q13619: CUL4A; NbExp=6; IntAct=EBI-456077, EBI-456106; CC Q86VP6; Q13620: CUL4B; NbExp=13; IntAct=EBI-456077, EBI-456067; CC Q86VP6; P46776: RPL27A; NbExp=2; IntAct=EBI-456077, EBI-350581; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21249194}. Nucleus CC {ECO:0000269|PubMed:21249194}. Note=Predominantly cytoplasmic. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q86VP6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86VP6-2; Sequence=VSP_013948; CC Name=3; CC IsoId=Q86VP6-3; Sequence=VSP_013947, VSP_013949, VSP_013950; CC -!- INDUCTION: Repressed by miR-148a. {ECO:0000269|PubMed:20820187}. CC -!- MISCELLANEOUS: A model has been proposed to explain the mechanisms of CC cullin-RING E3 ubiquitin ligase complexes assembly. According to this CC hypothesis, cullin-RING E3 ubiquitin ligase complexes exist in a CC 'stable' active state when saturated with substrate, occluding access CC to deneddylation by the COP9 signalosome (CSN) complex. The CC neddylation-conjugated cullin-RING E3 ubiquitin ligase complexes CC mediate ubiquitination of substrates and can recruit downstream factors CC involved in substrate degradation. Depletion of the substrate promotes CC the ability of CSN to bind the cullin-RING E3 ubiquitin ligase complex CC and mediate deneddylation. In this 'intermediate' deneddylated state, CC the complex can bind CAND1 and enter the 'exchange' state, resulting in CC high increase in dissociation rate of the substrate-recognition CC subunit. The resulting CAND1-cullin-RING complex rapidly assembles with CC another available substrate-recognition subunit to form an unstable CC ternary intermediate and yield a new cullin-RING E3 ubiquitin ligase CC complex. Subsequent neddylation of the cullin, which is stabilized by CC substrate, completes the cycle (PubMed:23453757). CC {ECO:0000305|PubMed:23453757}. CC -!- SIMILARITY: Belongs to the CAND family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA74852.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB55090.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB020636; BAA74852.2; ALT_INIT; mRNA. DR EMBL; AF157326; AAF67492.1; -; mRNA. DR EMBL; AL133560; CAB63714.1; -; mRNA. DR EMBL; AL136810; CAB66744.1; -; mRNA. DR EMBL; AL833880; CAD38737.1; -; mRNA. DR EMBL; CH471054; EAW97172.1; -; Genomic_DNA. DR EMBL; BC004232; AAH04232.1; -; mRNA. DR EMBL; BC026220; AAH26220.1; -; mRNA. DR EMBL; BC050341; AAH50341.1; -; mRNA. DR EMBL; AK027404; BAB55090.1; ALT_INIT; mRNA. DR EMBL; AK027783; BAB55365.1; -; mRNA. DR EMBL; AK314358; BAG36990.1; -; mRNA. DR CCDS; CCDS8977.1; -. [Q86VP6-1] DR PIR; T43441; T43441. DR RefSeq; NP_060918.2; NM_018448.4. [Q86VP6-1] DR PDB; 1U6G; X-ray; 3.10 A; C=1-1230. DR PDB; 4A0C; X-ray; 3.80 A; A/B=1-1230. DR PDB; 7Z8R; EM; 2.70 A; D=1-1230. DR PDB; 7Z8T; EM; 3.00 A; D=1-1230. DR PDB; 7Z8V; EM; 2.70 A; D=1-1230. DR PDB; 7ZBW; EM; 3.50 A; D=1-1230. DR PDB; 7ZBZ; EM; 3.10 A; D=1-1230. DR PDB; 8CDJ; EM; 3.40 A; D=1-1230. DR PDB; 8CDK; EM; 3.32 A; D=1-1230. DR PDB; 8H3Q; EM; 3.76 A; A=1-1230. DR PDB; 8OR0; EM; 3.10 A; C=1-1230. DR PDB; 8OR2; EM; 3.20 A; C=1-1230. DR PDB; 8OR3; EM; 2.90 A; C=1-1230. DR PDB; 8OR4; EM; 3.80 A; C=1-1230. DR PDBsum; 1U6G; -. DR PDBsum; 4A0C; -. DR PDBsum; 7Z8R; -. DR PDBsum; 7Z8T; -. DR PDBsum; 7Z8V; -. DR PDBsum; 7ZBW; -. DR PDBsum; 7ZBZ; -. DR PDBsum; 8CDJ; -. DR PDBsum; 8CDK; -. DR PDBsum; 8H3Q; -. DR PDBsum; 8OR0; -. DR PDBsum; 8OR2; -. DR PDBsum; 8OR3; -. DR PDBsum; 8OR4; -. DR AlphaFoldDB; Q86VP6; -. DR EMDB; EMD-17114; -. DR EMDB; EMD-17115; -. DR EMDB; EMD-17116; -. DR EMDB; EMD-17117; -. DR EMDB; EMD-34473; -. DR SMR; Q86VP6; -. DR BioGRID; 120937; 907. DR CORUM; Q86VP6; -. DR DIP; DIP-31608N; -. DR IntAct; Q86VP6; 617. DR MINT; Q86VP6; -. DR STRING; 9606.ENSP00000442318; -. DR GlyGen; Q86VP6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q86VP6; -. DR MetOSite; Q86VP6; -. DR PhosphoSitePlus; Q86VP6; -. DR SwissPalm; Q86VP6; -. DR BioMuta; CAND1; -. DR DMDM; 67460541; -. DR EPD; Q86VP6; -. DR jPOST; Q86VP6; -. DR MassIVE; Q86VP6; -. DR MaxQB; Q86VP6; -. DR PaxDb; 9606-ENSP00000442318; -. DR PeptideAtlas; Q86VP6; -. DR ProteomicsDB; 70051; -. [Q86VP6-1] DR ProteomicsDB; 70052; -. [Q86VP6-2] DR ProteomicsDB; 70053; -. [Q86VP6-3] DR Pumba; Q86VP6; -. DR Antibodypedia; 16667; 242 antibodies from 27 providers. DR DNASU; 55832; -. DR Ensembl; ENST00000545606.6; ENSP00000442318.1; ENSG00000111530.13. [Q86VP6-1] DR GeneID; 55832; -. DR KEGG; hsa:55832; -. DR MANE-Select; ENST00000545606.6; ENSP00000442318.1; NM_018448.5; NP_060918.2. DR UCSC; uc001stn.3; human. [Q86VP6-1] DR AGR; HGNC:30688; -. DR CTD; 55832; -. DR DisGeNET; 55832; -. DR GeneCards; CAND1; -. DR HGNC; HGNC:30688; CAND1. DR HPA; ENSG00000111530; Low tissue specificity. DR MIM; 607727; gene. DR neXtProt; NX_Q86VP6; -. DR OpenTargets; ENSG00000111530; -. DR PharmGKB; PA142672207; -. DR VEuPathDB; HostDB:ENSG00000111530; -. DR eggNOG; KOG1824; Eukaryota. DR GeneTree; ENSGT00390000017740; -. DR HOGENOM; CLU_007157_0_0_1; -. DR InParanoid; Q86VP6; -. DR OMA; AYIPHFQ; -. DR OrthoDB; 68829at2759; -. DR PhylomeDB; Q86VP6; -. DR TreeFam; TF300355; -. DR PathwayCommons; Q86VP6; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-917937; Iron uptake and transport. DR SignaLink; Q86VP6; -. DR BioGRID-ORCS; 55832; 276 hits in 1180 CRISPR screens. DR ChiTaRS; CAND1; human. DR EvolutionaryTrace; Q86VP6; -. DR GeneWiki; CAND1; -. DR GenomeRNAi; 55832; -. DR Pharos; Q86VP6; Tbio. DR PRO; PR:Q86VP6; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q86VP6; Protein. DR Bgee; ENSG00000111530; Expressed in adrenal tissue and 210 other cell types or tissues. DR ExpressionAtlas; Q86VP6; baseline and differential. DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0017025; F:TBP-class protein binding; IEA:Ensembl. DR GO; GO:0030154; P:cell differentiation; IDA:UniProtKB. DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:UniProtKB. DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:Ensembl. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0010265; P:SCF complex assembly; IDA:UniProtKB. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR IDEAL; IID00089; -. 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:SF1; CULLIN-ASSOCIATED NEDD8-DISSOCIATED PROTEIN 1; 1. DR PANTHER; PTHR12696; TIP120; 1. DR Pfam; PF13513; HEAT_EZ; 1. DR Pfam; PF08623; TIP120; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; Q86VP6; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Ubl conjugation pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8, ECO:0000269|Ref.9, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895" FT CHAIN 2..1230 FT /note="Cullin-associated NEDD8-dissociated protein 1" FT /id="PRO_0000089293" 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 131..165 FT /note="HEAT 4" FT REPEAT 171..208 FT /note="HEAT 5" FT REPEAT 210..247 FT /note="HEAT 6" FT REPEAT 248..282 FT /note="HEAT 7" FT REPEAT 289..366 FT /note="HEAT 8" FT REPEAT 370..407 FT /note="HEAT 9" FT REPEAT 424..467 FT /note="HEAT 10" FT REPEAT 471..510 FT /note="HEAT 11" FT REPEAT 515..552 FT /note="HEAT 12" FT REPEAT 563..602 FT /note="HEAT 13" FT REPEAT 606..643 FT /note="HEAT 14" FT REPEAT 646..683 FT /note="HEAT 15" FT REPEAT 688..725 FT /note="HEAT 16" FT REPEAT 729..768 FT /note="HEAT 17" FT REPEAT 770..808 FT /note="HEAT 18" FT REPEAT 809..845 FT /note="HEAT 19" FT REPEAT 852..889 FT /note="HEAT 20" FT REPEAT 890..927 FT /note="HEAT 21" FT REPEAT 928..960 FT /note="HEAT 22" FT REPEAT 961..998 FT /note="HEAT 23" FT REPEAT 1002..1039 FT /note="HEAT 24" FT REPEAT 1043..1097 FT /note="HEAT 25" FT REPEAT 1099..1133 FT /note="HEAT 26" FT REPEAT 1140..1189 FT /note="HEAT 27" FT REGION 315..344 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 315..342 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.8, ECO:0000269|Ref.9, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895" FT MOD_RES 55 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 335 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 558 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 971 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT VAR_SEQ 1..157 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013947" FT VAR_SEQ 458..625 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11230166" FT /id="VSP_013948" FT VAR_SEQ 549..560 FT /note="VIRPLDQPSSFD -> AHHMPEAQWLRL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013949" FT VAR_SEQ 561..1230 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013950" FT VARIANT 803 FT /note="V -> A (in dbSNP:rs12580996)" FT /id="VAR_054041" FT VARIANT 952 FT /note="A -> V (in dbSNP:rs17854618)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_025327" FT CONFLICT 272 FT /note="R -> K (in Ref. 7; BAB55365)" FT /evidence="ECO:0000305" FT CONFLICT 457 FT /note="M -> I (in Ref. 7; BAB55090)" FT /evidence="ECO:0000305" FT CONFLICT 606 FT /note="S -> P (in Ref. 3; AAF67492)" FT /evidence="ECO:0000305" FT CONFLICT 609 FT /note="P -> S (in Ref. 3; AAF67492)" FT /evidence="ECO:0000305" FT CONFLICT 1047 FT /note="T -> S (in Ref. 3; AAF67492)" FT /evidence="ECO:0000305" FT CONFLICT 1177 FT /note="M -> T (in Ref. 7; BAB55090)" FT /evidence="ECO:0000305" FT HELIX 7..14 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:7Z8V" FT HELIX 20..33 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:1U6G" FT HELIX 46..56 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 62..76 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 81..95 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 100..116 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 128..143 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 148..164 FT /evidence="ECO:0007829|PDB:7Z8R" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:7Z8V" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:7Z8V" FT HELIX 173..180 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 181..185 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 189..204 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 208..224 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 228..244 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:1U6G" FT HELIX 250..252 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 253..263 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 269..285 FT /evidence="ECO:0007829|PDB:7Z8R" FT TURN 287..290 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 291..293 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 294..305 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 347..362 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 365..367 FT /evidence="ECO:0007829|PDB:8CDK" FT HELIX 368..381 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 382..384 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 388..405 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 424..442 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 448..464 FT /evidence="ECO:0007829|PDB:7Z8R" FT TURN 466..469 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 470..472 FT /evidence="ECO:0007829|PDB:8OR3" FT HELIX 473..484 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:1U6G" FT HELIX 491..506 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 510..516 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 517..528 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 533..550 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 553..555 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 562..576 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 579..581 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 583..600 FT /evidence="ECO:0007829|PDB:7Z8R" FT TURN 601..603 FT /evidence="ECO:0007829|PDB:8OR3" FT HELIX 607..618 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 621..623 FT /evidence="ECO:0007829|PDB:1U6G" FT HELIX 625..636 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 637..640 FT /evidence="ECO:0007829|PDB:8OR3" FT HELIX 645..657 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 658..660 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 664..680 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 682..684 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 687..694 FT /evidence="ECO:0007829|PDB:7Z8R" FT TURN 698..700 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 701..704 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 706..722 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 724..729 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 733..742 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 750..765 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 772..785 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 793..809 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 811..813 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 814..826 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 828..830 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 832..848 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 853..856 FT /evidence="ECO:0007829|PDB:8OR0" FT HELIX 857..865 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 870..886 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 888..901 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 903..905 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 909..918 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 922..925 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 926..928 FT /evidence="ECO:0007829|PDB:8CDK" FT HELIX 929..939 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 943..946 FT /evidence="ECO:0007829|PDB:8CDK" FT HELIX 947..960 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 963..972 FT /evidence="ECO:0007829|PDB:7Z8R" FT TURN 973..975 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 979..989 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 990..992 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1001..1012 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1013..1015 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 1016..1019 FT /evidence="ECO:0007829|PDB:8OR3" FT HELIX 1020..1036 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1038..1040 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1042..1044 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1045..1054 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1060..1062 FT /evidence="ECO:0007829|PDB:7Z8V" FT STRAND 1064..1068 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 1071..1075 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1079..1095 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 1098..1100 FT /evidence="ECO:0007829|PDB:8OR3" FT HELIX 1104..1112 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1117..1130 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1135..1140 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1142..1153 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 1159..1161 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1163..1184 FT /evidence="ECO:0007829|PDB:7Z8R" FT STRAND 1186..1188 FT /evidence="ECO:0007829|PDB:7ZBZ" FT HELIX 1193..1204 FT /evidence="ECO:0007829|PDB:7Z8R" FT HELIX 1206..1214 FT /evidence="ECO:0007829|PDB:7Z8R" SQ SEQUENCE 1230 AA; 136376 MW; FE344558F72D79D8 CRC64; MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILKLLEDK NGEVQNLAVK CLGPLVSKVK EYQVETIVDT LCTNMLSDKE QLRDISSIGL KTVIGELPPA SSGSALAANV CKKITGRLTS AIAKQEDVSV QLEALDIMAD MLSRQGGLLV NFHPSILTCL LPQLTSPRLA VRKRTIIALG HLVMSCGNIV FVDLIEHLLS ELSKNDSMST TRTYIQCIAA ISRQAGHRIG EYLEKIIPLV VKFCNVDDDE LREYCIQAFE SFVRRCPKEV YPHVSTIINI CLKYLTYDPN YNYDDEDEDE NAMDADGGDD DDQGSDDEYS DDDDMSWKVR RAAAKCLDAV VSTRHEMLPE FYKTVSPALI SRFKEREENV KADVFHAYLS LLKQTRPVQS WLCDPDAMEQ GETPLTMLQS QVPNIVKALH KQMKEKSVKT RQCCFNMLTE LVNVLPGALT QHIPVLVPGI IFSLNDKSSS SNLKIDALSC LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL LVTQQLVKVI RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL GDNLGSDLPN TLQIFLERLK NEITRLTTVK ALTLIAGSPL KIDLRPVLGE GVPILASFLR KNQRALKLGT LSALDILIKN YSDSLTAAMI DAVLDELPPL ISESDMHVSQ MAISFLTTLA KVYPSSLSKI SGSILNELIG LVRSPLLQGG ALSAMLDFFQ ALVVTGTNNL GYMDLLRMLT GPVYSQSTAL THKQSYYSIA KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL SLGEVGHHID LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLPE YLPFVLQEIT SQPKRQYLLL HSLKEIISSA SVVGLKPYVE NIWALLLKHC ECAEEGTRNV VAECLGKLTL IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI DPLLKNCIGD FLKTLEDPDL NVRRVALVTF NSAAHNKPSL IRDLLDTVLP HLYNETKVRK ELIREVEMGP FKHTVDDGLD IRKAAFECMY TLLDSCLDRL DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ RLDRLVEPLR ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS QISSNPELAA IFESIQKDSS STNLESMDTS //