Full text data of CUL5
CUL5
(VACM1)
[Confidence: high (present in two of the MS resources)]
Cullin-5; CUL-5 (Vasopressin-activated calcium-mobilizing receptor 1; VACM-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cullin-5; CUL-5 (Vasopressin-activated calcium-mobilizing receptor 1; VACM-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00216003
IPI00216003 Cullin homolog 5 Component of E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00216003 Cullin homolog 5 Component of E3 ubiquitin ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
Q93034
ID CUL5_HUMAN Reviewed; 780 AA.
AC Q93034; A8K960; O14766; Q9BZC6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Cullin-5;
DE Short=CUL-5;
DE AltName: Full=Vasopressin-activated calcium-mobilizing receptor 1;
DE Short=VACM-1;
GN Name=CUL5; Synonyms=VACM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9037604;
RA Byrd P.J., Stankovic T., McConville C.M., Smith A.D., Cooper P.R.,
RA Taylor A.M.R.;
RT "Identification and analysis of expression of human VACM-1, a cullin
RT gene family member located on chromosome 11q22-23.";
RL Genome Res. 7:71-75(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Longo K.A., North W.G., Du J., Fay M.J.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Kanaya K., Kamitani T.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH RBX1 AND RNF7.
RX PubMed=10230407; DOI=10.1016/S1097-2765(00)80482-7;
RA Ohta T., Michel J.J., Schottelius A.J., Xiong Y.;
RT "ROC1, a homolog of APC11, represents a family of cullin partners with
RT an associated ubiquitin ligase activity.";
RL Mol. Cell 3:535-541(1999).
RN [8]
RP NEDDYLATION.
RX PubMed=10597293; DOI=10.1038/sj.onc.1203093;
RA Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N.,
RA Kato S., Tanaka K.;
RT "Covalent modification of all members of human cullin family proteins
RT by NEDD8.";
RL Oncogene 18:6829-6834(1999).
RN [9]
RP IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH LRRC41,
RP IDENTIFICATION IN A COMPLEX WITH TCEB3, IDENTIFICATION IN A COMPLEX
RP WITH SOCS1, AND IDENTIFICATION IN A COMPLEX WITH WSB1.
RX PubMed=11384984; DOI=10.1074/jbc.M103093200;
RA Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E.,
RA Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.;
RT "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that
RT can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
RL J. Biol. Chem. 276:29748-29753(2001).
RN [10]
RP IDENTIFICATION IN COMPLEX WITH HUMAN ADENOVIRUS 5 PROTEINS, AND
RP NEDDYLATION.
RX PubMed=12186903; DOI=10.1128/JVI.76.18.9194-9206.2002;
RA Harada J.N., Shevchenko A., Shevchenko A., Pallas D.C., Berk A.J.;
RT "Analysis of the adenovirus E1B-55K-anchored proteome reveals its link
RT to ubiquitination machinery.";
RL J. Virol. 76:9194-9206(2002).
RN [11]
RP INTERACTION WITH HIV VIF.
RX PubMed=15574592; DOI=10.1101/gad.1249904;
RA Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.;
RT "Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1
RT Vif-Cul5 complex that promotes APOBEC3G degradation.";
RL Genes Dev. 18:2861-2866(2004).
RN [12]
RP IDENTIFICATION IN THE ECS(LRRC41) COMPLEX, IDENTIFICATION IN THE
RP ECS(SOCS3) COMPLEX, IDENTIFICATION IN THE ECS(SPSB1) COMPLEX,
RP IDENTIFICATION IN THE ECS(SPSB2) COMPLEX, IDENTIFICATION IN THE
RP ECS(SPSB4) COMPLEX, IDENTIFICATION IN THE ECS(RAB40C) COMPLEX,
RP IDENTIFICATION IN THE ECS(WSB1) COMPLEX, MASS SPECTROMETRY, AND
RP INTERACTION WITH LRRC41; SOCS3; SPSB1; SPSB2; SPSB4; WSB1 AND RAB40C.
RX PubMed=15601820; DOI=10.1101/gad.1252404;
RA Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D.,
RA Conaway R.C., Conaway J.W., Nakayama K.I.;
RT "VHL-box and SOCS-box domains determine binding specificity for Cul2-
RT Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases.";
RL Genes Dev. 18:3055-3065(2004).
RN [13]
RP INTERACTION WITH ASB1; ASB2; ASB6; ASB7 AND ASB12.
RX PubMed=16325183; DOI=10.1016/j.febslet.2005.11.016;
RA Kohroki J., Nishiyama T., Nakamura T., Masuho Y.;
RT "ASB proteins interact with cullin5 and Rbx2 to form E3 ubiquitin
RT ligase complexes.";
RL FEBS Lett. 579:6796-6802(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, AND MASS
RP SPECTROMETRY.
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 [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 401-780 IN COMPLEX WITH NEDD8
RP AND RBX1, AND NEDDYLATION AT LYS-724.
RX PubMed=18805092; DOI=10.1016/j.cell.2008.07.022;
RA Duda D.M., Borg L.A., Scott D.C., Hunt H.W., Hammel M., Schulman B.A.;
RT "Structural insights into NEDD8 activation of cullin-RING ligases:
RT conformational control of conjugation.";
RL Cell 134:995-1006(2008).
CC -!- FUNCTION: Core component of multiple SCF-like ECS (Elongin-Cullin
CC 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which
CC mediate the ubiquitination and subsequent proteasomal degradation
CC of target proteins. As a scaffold protein may contribute to
CC catalysis through positioning of the substrate and the ubiquitin-
CC conjugating enzyme. The functional specificity of the E3
CC ubiquitin-protein ligase complex depends on the variable substrate
CC recognition component. ECS(SOCS1) seems to direct ubiquitination
CC of JAK2. Seems to be involved in proteosomal degradation of
CC p53/TP53 stimulated by adenovirus E1B-55 kDa protein. May form a
CC cell surface vasopressin receptor.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of multiple ECS (Elongin BC-CUL2/5-SOCS-box
CC protein) E3 ubiquitin-protein ligase complexes formed of CUL5,
CC Elongin BC (TCEB1 and TCEB2), RBX2 and a variable SOCS box domain-
CC containing protein as substrate-specific recognition component.
CC Component of the probable ECS(LRRC41) complex with the substrate
CC recognition component LRRC41. Component of the probable ECS(SOCS1)
CC complex with the substrate recognition component SOCS1. Component
CC of the probable ECS(WSB1) complex with the substrate recognition
CC subunit WSB1. Component of the probable ECS(SOCS3) complex with
CC the substrate recognition component SOCS3. Component of the
CC probable ECS(SPSB1) complex with the substrate recognition
CC component SPSB1. Component of the probable ECS(SPSB2) complex with
CC the substrate recognition component SPSB2. Component of the
CC probable ECS(SPSB4) complex with the substrate recognition
CC component SPSB4. Component of the probable ECS(RAB40C) complex
CC with the substrate recognition subunit RAB40C. May also form
CC complexes containing CUL5, elongin BC complex (TCEB1 and TCEB2),
CC RBX1 and TCEB3. May also form complexes containing CUL5, Elongin
CC BC (TCEB1 and TCEB2), RBX1 and VHL. The substrate recognition
CC component can also be a viral protein such as HIV Vif, or human
CC adenovirus 5 E1B large T-antigen and E4-orf6. Interacts with
CC RNF7/RBX2, LRRC41, SOCS3, SPSB1, SPSB2, SPSB4 and RAB40C.
CC Interacts with ASB1, ASB2, ASB6, ASB7 and ASB12.
CC -!- INTERACTION:
CC Q96Q27:ASB2; NbExp=4; IntAct=EBI-1057139, EBI-2880677;
CC O41974:GAMMAHV.ORF73 (xeno); NbExp=2; IntAct=EBI-1057139, EBI-6933128;
CC P62877:RBX1; NbExp=3; IntAct=EBI-1057139, EBI-398523;
CC P12504:vif (xeno); NbExp=5; IntAct=EBI-1057139, EBI-779991;
CC -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF
CC and prevents binding of the inhibitor CAND1. Deneddylated via its
CC interaction with the COP9 signalosome (CSN).
CC -!- SIMILARITY: Belongs to the cullin family.
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DR EMBL; X81882; CAA57465.1; -; mRNA.
DR EMBL; AF017061; AAB70253.1; -; mRNA.
DR EMBL; AF327710; AAK07472.1; -; mRNA.
DR EMBL; AK292575; BAF85264.1; -; mRNA.
DR EMBL; CH471065; EAW67102.1; -; Genomic_DNA.
DR EMBL; BC063306; AAH63306.1; -; mRNA.
DR RefSeq; NP_003469.2; NM_003478.3.
DR UniGene; Hs.440320; -.
DR PDB; 3DPL; X-ray; 2.60 A; C=401-780.
DR PDB; 3DQV; X-ray; 3.00 A; C/D=401-780.
DR PDB; 4JGH; X-ray; 3.00 A; D=10-386.
DR PDBsum; 3DPL; -.
DR PDBsum; 3DQV; -.
DR PDBsum; 4JGH; -.
DR ProteinModelPortal; Q93034; -.
DR SMR; Q93034; 12-386, 401-780.
DR DIP; DIP-43696N; -.
DR IntAct; Q93034; 32.
DR MINT; MINT-1184052; -.
DR STRING; 9606.ENSP00000299351; -.
DR PhosphoSite; Q93034; -.
DR DMDM; 14917099; -.
DR PaxDb; Q93034; -.
DR PRIDE; Q93034; -.
DR Ensembl; ENST00000393094; ENSP00000376808; ENSG00000166266.
DR Ensembl; ENST00000531427; ENSP00000435376; ENSG00000166266.
DR GeneID; 8065; -.
DR KEGG; hsa:8065; -.
DR UCSC; uc001pjv.3; human.
DR CTD; 8065; -.
DR GeneCards; GC11P107913; -.
DR HGNC; HGNC:2556; CUL5.
DR HPA; CAB017787; -.
DR HPA; HPA002185; -.
DR MIM; 601741; gene.
DR neXtProt; NX_Q93034; -.
DR PharmGKB; PA27052; -.
DR eggNOG; COG5647; -.
DR HOGENOM; HOG000007610; -.
DR HOVERGEN; HBG099672; -.
DR InParanoid; Q93034; -.
DR KO; K10612; -.
DR OMA; VCLWDEK; -.
DR OrthoDB; EOG78D7JD; -.
DR PhylomeDB; Q93034; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q93034; -.
DR GeneWiki; CUL5; -.
DR GenomeRNAi; 8065; -.
DR NextBio; 30655; -.
DR PRO; PR:Q93034; -.
DR ArrayExpress; Q93034; -.
DR Bgee; Q93034; -.
DR CleanEx; HS_CUL5; -.
DR Genevestigator; Q93034; -.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005262; F:calcium channel activity; TAS:ProtInc.
DR GO; GO:0004872; F:receptor activity; TAS:ProtInc.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
DR GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0051480; P:cytosolic calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Host-virus interaction;
KW Isopeptide bond; Phosphoprotein; Receptor; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 780 Cullin-5.
FT /FTId=PRO_0000119797.
FT MOD_RES 210 210 Phosphothreonine.
FT CROSSLNK 724 724 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in NEDD8).
FT CONFLICT 9 9 N -> D (in Ref. 2; AAB70253).
FT CONFLICT 12 12 S -> F (in Ref. 2; AAB70253).
FT CONFLICT 16 16 E -> G (in Ref. 2; AAB70253).
FT CONFLICT 32 34 QES -> RDF (in Ref. 2; AAB70253).
FT CONFLICT 38 38 Q -> R (in Ref. 2; AAB70253).
FT CONFLICT 50 52 VCL -> FCF (in Ref. 2; AAB70253).
FT CONFLICT 68 68 D -> DF (in Ref. 2; AAB70253).
FT CONFLICT 224 224 Q -> P (in Ref. 1; CAA57465).
FT CONFLICT 648 648 L -> F (in Ref. 1; CAA57465).
FT CONFLICT 651 651 E -> D (in Ref. 1; CAA57465).
FT HELIX 15 30
FT HELIX 37 53
FT HELIX 57 81
FT HELIX 86 103
FT TURN 104 108
FT HELIX 109 111
FT HELIX 112 115
FT HELIX 134 146
FT HELIX 148 167
FT HELIX 175 186
FT HELIX 196 199
FT HELIX 202 224
FT HELIX 227 248
FT STRAND 252 254
FT HELIX 257 269
FT HELIX 271 273
FT HELIX 274 277
FT HELIX 278 280
FT HELIX 281 286
FT HELIX 290 300
FT HELIX 310 333
FT HELIX 337 357
FT TURN 358 361
FT HELIX 363 377
FT HELIX 405 416
FT STRAND 417 419
FT HELIX 420 423
FT HELIX 427 438
FT HELIX 439 443
FT HELIX 447 463
FT HELIX 470 482
FT HELIX 487 513
FT HELIX 523 525
FT STRAND 526 532
FT HELIX 533 536
FT HELIX 549 552
FT HELIX 555 563
FT STRAND 566 573
FT HELIX 575 577
FT STRAND 579 585
FT STRAND 590 596
FT HELIX 597 603
FT HELIX 604 606
FT HELIX 616 623
FT HELIX 627 638
FT STRAND 647 652
FT HELIX 657 659
FT STRAND 665 668
FT STRAND 674 687
FT TURN 690 693
FT HELIX 697 723
FT STRAND 726 729
FT HELIX 731 741
FT TURN 742 745
FT HELIX 750 762
FT STRAND 765 769
FT STRAND 772 778
SQ SEQUENCE 780 AA; 90955 MW; 57463CB4ED76E303 CRC64;
MATSNLLKNK GSLQFEDKWD FMRPIVLKLL RQESVTKQQW FDLFSDVHAV CLWDDKGPAK
IHQALKEDIL EFIKQAQARV LSHQDDTALL KAYIVEWRKF FTQCDILPKP FCQLEITLMG
KQGSNKKSNV EDSIVRKLML DTWNESIFSN IKNRLQDSAM KLVHAERLGE AFDSQLVIGV
RESYVNLCSN PEDKLQIYRD NFEKAYLDST ERFYRTQAPS YLQQNGVQNY MKYADAKLKE
EEKRALRYLE TRRECNSVEA LMECCVNALV TSFKETILAE CQGMIKRNET EKLHLMFSLM
DKVPNGIEPM LKDLEEHIIS AGLADMVAAA ETITTDSEKY VEQLLTLFNR FSKLVKEAFQ
DDPRFLTARD KAYKAVVNDA TIFKLELPLK QKGVGLKTQP ESKCPELLAN YCDMLLRKTP
LSKKLTSEEI EAKLKEVLLV LKYVQNKDVF MRYHKAHLTR RLILDISADS EIEENMVEWL
REVGMPADYV NKLARMFQDI KVSEDLNQAF KEMHKNNKLA LPADSVNIKI LNAGAWSRSS
EKVFVSLPTE LEDLIPEVEE FYKKNHSGRK LHWHHLMSNG IITFKNEVGQ YDLEVTTFQL
AVLFAWNQRP REKISFENLK LATELPDAEL RRTLWSLVAF PKLKRQVLLY EPQVNSPKDF
TEGTLFSVNQ EFSLIKNAKV QKRGKINLIG RLQLTTERMR EEENEGIVQL RILRTQEAII
QIMKMRKKIS NAQLQTELVE ILKNMFLPQK KMIKEQIEWL IEHKYIRRDE SDINTFIYMA
//
ID CUL5_HUMAN Reviewed; 780 AA.
AC Q93034; A8K960; O14766; Q9BZC6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Cullin-5;
DE Short=CUL-5;
DE AltName: Full=Vasopressin-activated calcium-mobilizing receptor 1;
DE Short=VACM-1;
GN Name=CUL5; Synonyms=VACM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9037604;
RA Byrd P.J., Stankovic T., McConville C.M., Smith A.D., Cooper P.R.,
RA Taylor A.M.R.;
RT "Identification and analysis of expression of human VACM-1, a cullin
RT gene family member located on chromosome 11q22-23.";
RL Genome Res. 7:71-75(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Longo K.A., North W.G., Du J., Fay M.J.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Kanaya K., Kamitani T.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH RBX1 AND RNF7.
RX PubMed=10230407; DOI=10.1016/S1097-2765(00)80482-7;
RA Ohta T., Michel J.J., Schottelius A.J., Xiong Y.;
RT "ROC1, a homolog of APC11, represents a family of cullin partners with
RT an associated ubiquitin ligase activity.";
RL Mol. Cell 3:535-541(1999).
RN [8]
RP NEDDYLATION.
RX PubMed=10597293; DOI=10.1038/sj.onc.1203093;
RA Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N.,
RA Kato S., Tanaka K.;
RT "Covalent modification of all members of human cullin family proteins
RT by NEDD8.";
RL Oncogene 18:6829-6834(1999).
RN [9]
RP IDENTIFICATION IN E3 UBIQUITIN-PROTEIN LIGASE COMPLEX WITH LRRC41,
RP IDENTIFICATION IN A COMPLEX WITH TCEB3, IDENTIFICATION IN A COMPLEX
RP WITH SOCS1, AND IDENTIFICATION IN A COMPLEX WITH WSB1.
RX PubMed=11384984; DOI=10.1074/jbc.M103093200;
RA Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E.,
RA Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.;
RT "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that
RT can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
RL J. Biol. Chem. 276:29748-29753(2001).
RN [10]
RP IDENTIFICATION IN COMPLEX WITH HUMAN ADENOVIRUS 5 PROTEINS, AND
RP NEDDYLATION.
RX PubMed=12186903; DOI=10.1128/JVI.76.18.9194-9206.2002;
RA Harada J.N., Shevchenko A., Shevchenko A., Pallas D.C., Berk A.J.;
RT "Analysis of the adenovirus E1B-55K-anchored proteome reveals its link
RT to ubiquitination machinery.";
RL J. Virol. 76:9194-9206(2002).
RN [11]
RP INTERACTION WITH HIV VIF.
RX PubMed=15574592; DOI=10.1101/gad.1249904;
RA Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D.;
RT "Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1
RT Vif-Cul5 complex that promotes APOBEC3G degradation.";
RL Genes Dev. 18:2861-2866(2004).
RN [12]
RP IDENTIFICATION IN THE ECS(LRRC41) COMPLEX, IDENTIFICATION IN THE
RP ECS(SOCS3) COMPLEX, IDENTIFICATION IN THE ECS(SPSB1) COMPLEX,
RP IDENTIFICATION IN THE ECS(SPSB2) COMPLEX, IDENTIFICATION IN THE
RP ECS(SPSB4) COMPLEX, IDENTIFICATION IN THE ECS(RAB40C) COMPLEX,
RP IDENTIFICATION IN THE ECS(WSB1) COMPLEX, MASS SPECTROMETRY, AND
RP INTERACTION WITH LRRC41; SOCS3; SPSB1; SPSB2; SPSB4; WSB1 AND RAB40C.
RX PubMed=15601820; DOI=10.1101/gad.1252404;
RA Kamura T., Maenaka K., Kotoshiba S., Matsumoto M., Kohda D.,
RA Conaway R.C., Conaway J.W., Nakayama K.I.;
RT "VHL-box and SOCS-box domains determine binding specificity for Cul2-
RT Rbx1 and Cul5-Rbx2 modules of ubiquitin ligases.";
RL Genes Dev. 18:3055-3065(2004).
RN [13]
RP INTERACTION WITH ASB1; ASB2; ASB6; ASB7 AND ASB12.
RX PubMed=16325183; DOI=10.1016/j.febslet.2005.11.016;
RA Kohroki J., Nishiyama T., Nakamura T., Masuho Y.;
RT "ASB proteins interact with cullin5 and Rbx2 to form E3 ubiquitin
RT ligase complexes.";
RL FEBS Lett. 579:6796-6802(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, AND MASS
RP SPECTROMETRY.
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 [15]
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.,
RA Buerckstuemmer T., 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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 401-780 IN COMPLEX WITH NEDD8
RP AND RBX1, AND NEDDYLATION AT LYS-724.
RX PubMed=18805092; DOI=10.1016/j.cell.2008.07.022;
RA Duda D.M., Borg L.A., Scott D.C., Hunt H.W., Hammel M., Schulman B.A.;
RT "Structural insights into NEDD8 activation of cullin-RING ligases:
RT conformational control of conjugation.";
RL Cell 134:995-1006(2008).
CC -!- FUNCTION: Core component of multiple SCF-like ECS (Elongin-Cullin
CC 2/5-SOCS-box protein) E3 ubiquitin-protein ligase complexes, which
CC mediate the ubiquitination and subsequent proteasomal degradation
CC of target proteins. As a scaffold protein may contribute to
CC catalysis through positioning of the substrate and the ubiquitin-
CC conjugating enzyme. The functional specificity of the E3
CC ubiquitin-protein ligase complex depends on the variable substrate
CC recognition component. ECS(SOCS1) seems to direct ubiquitination
CC of JAK2. Seems to be involved in proteosomal degradation of
CC p53/TP53 stimulated by adenovirus E1B-55 kDa protein. May form a
CC cell surface vasopressin receptor.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of multiple ECS (Elongin BC-CUL2/5-SOCS-box
CC protein) E3 ubiquitin-protein ligase complexes formed of CUL5,
CC Elongin BC (TCEB1 and TCEB2), RBX2 and a variable SOCS box domain-
CC containing protein as substrate-specific recognition component.
CC Component of the probable ECS(LRRC41) complex with the substrate
CC recognition component LRRC41. Component of the probable ECS(SOCS1)
CC complex with the substrate recognition component SOCS1. Component
CC of the probable ECS(WSB1) complex with the substrate recognition
CC subunit WSB1. Component of the probable ECS(SOCS3) complex with
CC the substrate recognition component SOCS3. Component of the
CC probable ECS(SPSB1) complex with the substrate recognition
CC component SPSB1. Component of the probable ECS(SPSB2) complex with
CC the substrate recognition component SPSB2. Component of the
CC probable ECS(SPSB4) complex with the substrate recognition
CC component SPSB4. Component of the probable ECS(RAB40C) complex
CC with the substrate recognition subunit RAB40C. May also form
CC complexes containing CUL5, elongin BC complex (TCEB1 and TCEB2),
CC RBX1 and TCEB3. May also form complexes containing CUL5, Elongin
CC BC (TCEB1 and TCEB2), RBX1 and VHL. The substrate recognition
CC component can also be a viral protein such as HIV Vif, or human
CC adenovirus 5 E1B large T-antigen and E4-orf6. Interacts with
CC RNF7/RBX2, LRRC41, SOCS3, SPSB1, SPSB2, SPSB4 and RAB40C.
CC Interacts with ASB1, ASB2, ASB6, ASB7 and ASB12.
CC -!- INTERACTION:
CC Q96Q27:ASB2; NbExp=4; IntAct=EBI-1057139, EBI-2880677;
CC O41974:GAMMAHV.ORF73 (xeno); NbExp=2; IntAct=EBI-1057139, EBI-6933128;
CC P62877:RBX1; NbExp=3; IntAct=EBI-1057139, EBI-398523;
CC P12504:vif (xeno); NbExp=5; IntAct=EBI-1057139, EBI-779991;
CC -!- PTM: Neddylated; which enhances the ubiquitination activity of SCF
CC and prevents binding of the inhibitor CAND1. Deneddylated via its
CC interaction with the COP9 signalosome (CSN).
CC -!- SIMILARITY: Belongs to the cullin family.
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DR EMBL; X81882; CAA57465.1; -; mRNA.
DR EMBL; AF017061; AAB70253.1; -; mRNA.
DR EMBL; AF327710; AAK07472.1; -; mRNA.
DR EMBL; AK292575; BAF85264.1; -; mRNA.
DR EMBL; CH471065; EAW67102.1; -; Genomic_DNA.
DR EMBL; BC063306; AAH63306.1; -; mRNA.
DR RefSeq; NP_003469.2; NM_003478.3.
DR UniGene; Hs.440320; -.
DR PDB; 3DPL; X-ray; 2.60 A; C=401-780.
DR PDB; 3DQV; X-ray; 3.00 A; C/D=401-780.
DR PDB; 4JGH; X-ray; 3.00 A; D=10-386.
DR PDBsum; 3DPL; -.
DR PDBsum; 3DQV; -.
DR PDBsum; 4JGH; -.
DR ProteinModelPortal; Q93034; -.
DR SMR; Q93034; 12-386, 401-780.
DR DIP; DIP-43696N; -.
DR IntAct; Q93034; 32.
DR MINT; MINT-1184052; -.
DR STRING; 9606.ENSP00000299351; -.
DR PhosphoSite; Q93034; -.
DR DMDM; 14917099; -.
DR PaxDb; Q93034; -.
DR PRIDE; Q93034; -.
DR Ensembl; ENST00000393094; ENSP00000376808; ENSG00000166266.
DR Ensembl; ENST00000531427; ENSP00000435376; ENSG00000166266.
DR GeneID; 8065; -.
DR KEGG; hsa:8065; -.
DR UCSC; uc001pjv.3; human.
DR CTD; 8065; -.
DR GeneCards; GC11P107913; -.
DR HGNC; HGNC:2556; CUL5.
DR HPA; CAB017787; -.
DR HPA; HPA002185; -.
DR MIM; 601741; gene.
DR neXtProt; NX_Q93034; -.
DR PharmGKB; PA27052; -.
DR eggNOG; COG5647; -.
DR HOGENOM; HOG000007610; -.
DR HOVERGEN; HBG099672; -.
DR InParanoid; Q93034; -.
DR KO; K10612; -.
DR OMA; VCLWDEK; -.
DR OrthoDB; EOG78D7JD; -.
DR PhylomeDB; Q93034; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_6900; Immune System.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q93034; -.
DR GeneWiki; CUL5; -.
DR GenomeRNAi; 8065; -.
DR NextBio; 30655; -.
DR PRO; PR:Q93034; -.
DR ArrayExpress; Q93034; -.
DR Bgee; Q93034; -.
DR CleanEx; HS_CUL5; -.
DR Genevestigator; Q93034; -.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005262; F:calcium channel activity; TAS:ProtInc.
DR GO; GO:0004872; F:receptor activity; TAS:ProtInc.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
DR GO; GO:0007050; P:cell cycle arrest; TAS:ProtInc.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0051480; P:cytosolic calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR Gene3D; 1.10.10.10; -; 2.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Host-virus interaction;
KW Isopeptide bond; Phosphoprotein; Receptor; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 780 Cullin-5.
FT /FTId=PRO_0000119797.
FT MOD_RES 210 210 Phosphothreonine.
FT CROSSLNK 724 724 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in NEDD8).
FT CONFLICT 9 9 N -> D (in Ref. 2; AAB70253).
FT CONFLICT 12 12 S -> F (in Ref. 2; AAB70253).
FT CONFLICT 16 16 E -> G (in Ref. 2; AAB70253).
FT CONFLICT 32 34 QES -> RDF (in Ref. 2; AAB70253).
FT CONFLICT 38 38 Q -> R (in Ref. 2; AAB70253).
FT CONFLICT 50 52 VCL -> FCF (in Ref. 2; AAB70253).
FT CONFLICT 68 68 D -> DF (in Ref. 2; AAB70253).
FT CONFLICT 224 224 Q -> P (in Ref. 1; CAA57465).
FT CONFLICT 648 648 L -> F (in Ref. 1; CAA57465).
FT CONFLICT 651 651 E -> D (in Ref. 1; CAA57465).
FT HELIX 15 30
FT HELIX 37 53
FT HELIX 57 81
FT HELIX 86 103
FT TURN 104 108
FT HELIX 109 111
FT HELIX 112 115
FT HELIX 134 146
FT HELIX 148 167
FT HELIX 175 186
FT HELIX 196 199
FT HELIX 202 224
FT HELIX 227 248
FT STRAND 252 254
FT HELIX 257 269
FT HELIX 271 273
FT HELIX 274 277
FT HELIX 278 280
FT HELIX 281 286
FT HELIX 290 300
FT HELIX 310 333
FT HELIX 337 357
FT TURN 358 361
FT HELIX 363 377
FT HELIX 405 416
FT STRAND 417 419
FT HELIX 420 423
FT HELIX 427 438
FT HELIX 439 443
FT HELIX 447 463
FT HELIX 470 482
FT HELIX 487 513
FT HELIX 523 525
FT STRAND 526 532
FT HELIX 533 536
FT HELIX 549 552
FT HELIX 555 563
FT STRAND 566 573
FT HELIX 575 577
FT STRAND 579 585
FT STRAND 590 596
FT HELIX 597 603
FT HELIX 604 606
FT HELIX 616 623
FT HELIX 627 638
FT STRAND 647 652
FT HELIX 657 659
FT STRAND 665 668
FT STRAND 674 687
FT TURN 690 693
FT HELIX 697 723
FT STRAND 726 729
FT HELIX 731 741
FT TURN 742 745
FT HELIX 750 762
FT STRAND 765 769
FT STRAND 772 778
SQ SEQUENCE 780 AA; 90955 MW; 57463CB4ED76E303 CRC64;
MATSNLLKNK GSLQFEDKWD FMRPIVLKLL RQESVTKQQW FDLFSDVHAV CLWDDKGPAK
IHQALKEDIL EFIKQAQARV LSHQDDTALL KAYIVEWRKF FTQCDILPKP FCQLEITLMG
KQGSNKKSNV EDSIVRKLML DTWNESIFSN IKNRLQDSAM KLVHAERLGE AFDSQLVIGV
RESYVNLCSN PEDKLQIYRD NFEKAYLDST ERFYRTQAPS YLQQNGVQNY MKYADAKLKE
EEKRALRYLE TRRECNSVEA LMECCVNALV TSFKETILAE CQGMIKRNET EKLHLMFSLM
DKVPNGIEPM LKDLEEHIIS AGLADMVAAA ETITTDSEKY VEQLLTLFNR FSKLVKEAFQ
DDPRFLTARD KAYKAVVNDA TIFKLELPLK QKGVGLKTQP ESKCPELLAN YCDMLLRKTP
LSKKLTSEEI EAKLKEVLLV LKYVQNKDVF MRYHKAHLTR RLILDISADS EIEENMVEWL
REVGMPADYV NKLARMFQDI KVSEDLNQAF KEMHKNNKLA LPADSVNIKI LNAGAWSRSS
EKVFVSLPTE LEDLIPEVEE FYKKNHSGRK LHWHHLMSNG IITFKNEVGQ YDLEVTTFQL
AVLFAWNQRP REKISFENLK LATELPDAEL RRTLWSLVAF PKLKRQVLLY EPQVNSPKDF
TEGTLFSVNQ EFSLIKNAKV QKRGKINLIG RLQLTTERMR EEENEGIVQL RILRTQEAII
QIMKMRKKIS NAQLQTELVE ILKNMFLPQK KMIKEQIEWL IEHKYIRRDE SDINTFIYMA
//
MIM
601741
*RECORD*
*FIELD* NO
601741
*FIELD* TI
*601741 CULLIN 5; CUL5
;;VASOPRESSIN-ACTIVATED CALCIUM-MOBILIZING RECEPTOR 1; VACM1
read more*FIELD* TX
CLONING
Arginine vasopressin (AVP)-activated calcium-mobilizing receptor-1
(VACM1) is a cell surface protein involved in intracellular signal
transduction. The gene encoding rabbit Vacm1 was isolated by
Burnatowska-Hledin et al. (1995) from a renal medullary cDNA library by
expression cloning in Xenopus laevis oocytes. While searching for
expressed genes in the ataxia-telangiectasia (208900) gene (ATM; 607585)
region on chromosome 11q22-q23, Byrd et al. (1997) identified the gene
encoding the human homolog of rabbit Vacm1 and determined the complete
amino acid sequence for the protein. The 780-amino acid predicted
polypeptide differs from the rabbit sequence by only 7 residues.
Northern hybridization analysis showed expression in a wide range of
human tissues. Byrd et al. (1997) noted that the human VACM1 gene shares
homology with the C. elegans gene Cul5, a member of the family of cullin
genes that are involved in cell cycle regulation.
GENE STRUCTURE
An et al. (2007) determined that the CUL5 gene contains 19 exons and
spans about 100 kb.
MAPPING
Byrd et al. (1997) mapped the CUL5 gene to chromosome 11q22-q23.
MOLECULAR GENETICS
Since human immunodeficiency virus (HIV)-1 viral infectivity factor
(Vif) interacts with CUL5 to mediate degradation of the anti-HIV-1
enzyme APOBEC3G (607113), An et al. (2007) investigated whether genetic
variation in CUL5 affects the course of HIV-1 infection. SNP analysis
showed that CUL5 genetic variation did not affect susceptibility to
HIV-1 infection. Some CUL5 haplotypes were associated with a rapid loss
of CD4 (186940)-positive T cells and increased viral loads after
infection, whereas other CUL5 haplotypes showed a delayed CD4-positive
T-cell depletion. Gel-shift analysis suggested that there may be
differential nuclear protein binding efficiencies between the CUL5
haplotypes. An et al. (2007) proposed that inhibitors that block
interaction between HIV-1 Vif and CUL5 may have potential as an
anti-HIV-1 therapeutic strategy.
*FIELD* RF
1. An, P.; Duggal, P.; Wang, L. H.; O'Brien, S. J.; Donfield, S.;
Goedert, J. J.; Phair, J.; Buchbinder, S.; Kirk, G. D.; Winkler, C.
A.: Polymorphisms of CUL5 are associated with CD4+ T cell loss in
HIV-1 infected individuals. PLoS Genet. 3: e19, 2007. Note: Electronic
Article.
2. Burnatowska-Hledin, M. A.; Spielman, W. S.; Smith, W. L.; Shi,
P.; Meyer, J. M.; Dewitt, D. L.: Expression cloning of an AVP-activated,
calcium-mobilizing receptor from rabbit kidney medulla. Am. J. Physiol. 268:
F1198-F1210, 1995.
3. Byrd, P. J.; Stankovic, T.; McConville, C. M.; Smith, A. D.; Cooper,
P. R.; Taylor, A. M. R.: Identification and analysis of expression
of human VACM-1, a cullin gene family member located on chromosome
11q22-23. Genome Res. 7: 71-75, 1997.
*FIELD* CN
Paul J. Converse - updated: 7/17/2007
*FIELD* CD
Victor A. McKusick: 4/9/1997
*FIELD* ED
mgross: 08/24/2007
mgross: 8/24/2007
terry: 7/17/2007
ckniffin: 3/11/2003
alopez: 1/7/1999
alopez: 5/16/1997
mark: 4/9/1997
*RECORD*
*FIELD* NO
601741
*FIELD* TI
*601741 CULLIN 5; CUL5
;;VASOPRESSIN-ACTIVATED CALCIUM-MOBILIZING RECEPTOR 1; VACM1
read more*FIELD* TX
CLONING
Arginine vasopressin (AVP)-activated calcium-mobilizing receptor-1
(VACM1) is a cell surface protein involved in intracellular signal
transduction. The gene encoding rabbit Vacm1 was isolated by
Burnatowska-Hledin et al. (1995) from a renal medullary cDNA library by
expression cloning in Xenopus laevis oocytes. While searching for
expressed genes in the ataxia-telangiectasia (208900) gene (ATM; 607585)
region on chromosome 11q22-q23, Byrd et al. (1997) identified the gene
encoding the human homolog of rabbit Vacm1 and determined the complete
amino acid sequence for the protein. The 780-amino acid predicted
polypeptide differs from the rabbit sequence by only 7 residues.
Northern hybridization analysis showed expression in a wide range of
human tissues. Byrd et al. (1997) noted that the human VACM1 gene shares
homology with the C. elegans gene Cul5, a member of the family of cullin
genes that are involved in cell cycle regulation.
GENE STRUCTURE
An et al. (2007) determined that the CUL5 gene contains 19 exons and
spans about 100 kb.
MAPPING
Byrd et al. (1997) mapped the CUL5 gene to chromosome 11q22-q23.
MOLECULAR GENETICS
Since human immunodeficiency virus (HIV)-1 viral infectivity factor
(Vif) interacts with CUL5 to mediate degradation of the anti-HIV-1
enzyme APOBEC3G (607113), An et al. (2007) investigated whether genetic
variation in CUL5 affects the course of HIV-1 infection. SNP analysis
showed that CUL5 genetic variation did not affect susceptibility to
HIV-1 infection. Some CUL5 haplotypes were associated with a rapid loss
of CD4 (186940)-positive T cells and increased viral loads after
infection, whereas other CUL5 haplotypes showed a delayed CD4-positive
T-cell depletion. Gel-shift analysis suggested that there may be
differential nuclear protein binding efficiencies between the CUL5
haplotypes. An et al. (2007) proposed that inhibitors that block
interaction between HIV-1 Vif and CUL5 may have potential as an
anti-HIV-1 therapeutic strategy.
*FIELD* RF
1. An, P.; Duggal, P.; Wang, L. H.; O'Brien, S. J.; Donfield, S.;
Goedert, J. J.; Phair, J.; Buchbinder, S.; Kirk, G. D.; Winkler, C.
A.: Polymorphisms of CUL5 are associated with CD4+ T cell loss in
HIV-1 infected individuals. PLoS Genet. 3: e19, 2007. Note: Electronic
Article.
2. Burnatowska-Hledin, M. A.; Spielman, W. S.; Smith, W. L.; Shi,
P.; Meyer, J. M.; Dewitt, D. L.: Expression cloning of an AVP-activated,
calcium-mobilizing receptor from rabbit kidney medulla. Am. J. Physiol. 268:
F1198-F1210, 1995.
3. Byrd, P. J.; Stankovic, T.; McConville, C. M.; Smith, A. D.; Cooper,
P. R.; Taylor, A. M. R.: Identification and analysis of expression
of human VACM-1, a cullin gene family member located on chromosome
11q22-23. Genome Res. 7: 71-75, 1997.
*FIELD* CN
Paul J. Converse - updated: 7/17/2007
*FIELD* CD
Victor A. McKusick: 4/9/1997
*FIELD* ED
mgross: 08/24/2007
mgross: 8/24/2007
terry: 7/17/2007
ckniffin: 3/11/2003
alopez: 1/7/1999
alopez: 5/16/1997
mark: 4/9/1997