CCZ1B_HUMAN
ID CCZ1B_HUMAN Reviewed; 482 AA.
AC P86790; A2RU45; O95766; Q9UG65; Q9Y359;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Vacuolar fusion protein CCZ1 homolog B;
DE AltName: Full=Vacuolar fusion protein CCZ1 homolog-like;
GN Name=CCZ1B; Synonyms=C7orf28B;
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Placenta;
RX PubMed=17897319; DOI=10.1111/j.1600-0854.2007.00643.x;
RA Schroeder B., Wrocklage C., Pan C., Jaeger R., Koesters B., Schaefer H.,
RA Elsaesser H.-P., Mann M., Hasilik A.;
RT "Integral and associated lysosomal membrane proteins.";
RL Traffic 8:1676-1686(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP 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 [6]
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 [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).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-266, AND
RP IDENTIFICATION BY 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 [10]
RP INTERACTION OF MON1A/CCZ1B COMPLEX WITH RIMOC1 AND RAB7A.
RX PubMed=34432599; DOI=10.1080/15548627.2021.1960116;
RA Yan B.R., Li T., Coyaud E., Laurent E.M.N., St-Germain J., Zhou Y.,
RA Kim P.K., Raught B., Brumell J.H.;
RT "C5orf51 is a component of the MON1-CCZ1 complex and controls RAB7A
RT localization and stability during mitophagy.";
RL Autophagy 18:829-840(2022).
CC -!- SUBUNIT: The MON1A-CCZ1B complex interacts with RIMOC1
CC (PubMed:34432599). The MON1A-CCZ1B complex interacts with RAB7A and
CC this interaction is enhanced in the presence of RIMOC1
CC (PubMed:34432599). {ECO:0000269|PubMed:34432599}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:17897319}.
CC -!- SIMILARITY: Belongs to the CCZ1 family. {ECO:0000305}.
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DR EMBL; AC079882; AAQ93370.1; -; Genomic_DNA.
DR EMBL; BC010130; AAH10130.1; -; mRNA.
DR CCDS; CCDS5354.1; -.
DR PIR; T08806; T08806.
DR RefSeq; NP_056437.4; NM_015622.5.
DR RefSeq; NP_932765.1; NM_198097.3.
DR AlphaFoldDB; P86790; -.
DR SMR; P86790; -.
DR BioGRID; 119643; 81.
DR BioGRID; 128773; 7.
DR IntAct; P86790; 9.
DR STRING; 9606.ENSP00000314544; -.
DR iPTMnet; P86790; -.
DR PhosphoSitePlus; P86790; -.
DR BioMuta; CCZ1B; -.
DR DMDM; 310943081; -.
DR EPD; P86790; -.
DR jPOST; P86790; -.
DR MassIVE; P86790; -.
DR PaxDb; P86790; -.
DR PeptideAtlas; P86790; -.
DR PRIDE; P86790; -.
DR Antibodypedia; 69715; 42 antibodies from 11 providers.
DR DNASU; 51622; -.
DR Ensembl; ENST00000316731.13; ENSP00000314544.8; ENSG00000146574.16.
DR GeneID; 221960; -.
DR GeneID; 51622; -.
DR KEGG; hsa:221960; -.
DR KEGG; hsa:51622; -.
DR MANE-Select; ENST00000316731.13; ENSP00000314544.8; NM_198097.5; NP_932765.1.
DR MANE-Select; ENST00000325974.9; ENSP00000325681.6; NM_015622.6; NP_056437.4.
DR CTD; 221960; -.
DR CTD; 51622; -.
DR DisGeNET; 221960; -.
DR DisGeNET; 51622; -.
DR GeneCards; CCZ1B; -.
DR HGNC; HGNC:21717; CCZ1B.
DR HPA; ENSG00000146574; Low tissue specificity.
DR neXtProt; NX_P86790; -.
DR OpenTargets; ENSG00000122674; -.
DR VEuPathDB; HostDB:ENSG00000146574; -.
DR eggNOG; KOG2622; Eukaryota.
DR HOGENOM; CLU_037828_2_0_1; -.
DR InParanoid; P86790; -.
DR OMA; WVIARLN; -.
DR OrthoDB; 448107at2759; -.
DR PhylomeDB; P86790; -.
DR TreeFam; TF314962; -.
DR PathwayCommons; P86790; -.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P86790; -.
DR BioGRID-ORCS; 221960; 41 hits in 960 CRISPR screens.
DR BioGRID-ORCS; 51622; 20 hits in 313 CRISPR screens.
DR ChiTaRS; CCZ1B; human.
DR Pharos; P86790; Tdark.
DR PRO; PR:P86790; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P86790; protein.
DR Bgee; ENSG00000146574; Expressed in calcaneal tendon and 94 other tissues.
DR ExpressionAtlas; P86790; baseline and differential.
DR Genevisible; P86790; HS.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035658; C:Mon1-Ccz1 complex; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR InterPro; IPR013176; Ccz1.
DR InterPro; IPR043987; CCZ1/INTU/HSP4_longin_1.
DR InterPro; IPR043989; CCZ1/INTU/HSP4_longin_3.
DR InterPro; IPR043988; CCZ1/INTU_longin_2.
DR PANTHER; PTHR13056; PTHR13056; 1.
DR Pfam; PF19031; Intu_longin_1; 1.
DR Pfam; PF19032; Intu_longin_2; 1.
DR Pfam; PF19033; Intu_longin_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Lysosome; Membrane; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..482
FT /note="Vacuolar fusion protein CCZ1 homolog B"
FT /id="PRO_0000089584"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
SQ SEQUENCE 482 AA; 55866 MW; EE10E55EEC918C18 CRC64;
MAAAAAGAGS GPWAAQEKQF PPALLSFFIY NPRFGPREGQ EENKILFYHP NEVEKNEKIR
NVGLCEAIVQ FTRTFSPSKP AKSLHTQKNR QFFNEPEENF WMVMVVRNPI IEKQSKDGKP
VIEYQEEELL DKVYSSVLRQ CYSMYKLFNG TFLKAMEDGG VKLLKERLEK FFHRYLQTLH
LQSCDLLDIF GGISFFPLDK MTYLKIQSFI NRMEESLNIV KYTAFLYNDQ LIWSGLEQDD
MRILYKYLTT SLFPRHIEPE LAGRDSPIRA EMPGNLQHYG RFLTGPLNLN DPDAKCRFPK
IFVNTDDTYE ELHLIVYKAM SAAVCFMIDA SVHPTLDFCR RLDSIVGPQL TVLASDICEQ
FNINKRMSGS EKEPQFKFIY FNHMNLAEKS TVHMRKTPSV SLTSVHPDLM KILGDINSDF
TRVDEDEEII VKAMSDYWVV GKKSDRRELY VILNQKNANL IEVNEEVKKL CATQFNNIFF
LD
