CLU_HUMAN
ID CLU_HUMAN Reviewed; 1309 AA.
AC O75153; Q6AHY2; Q6P3X7; Q6ZUG8; Q8N4U7; Q9BTA3; Q9H979;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Clustered mitochondria protein homolog {ECO:0000255|HAMAP-Rule:MF_03013};
GN Name=CLUH; Synonyms=KIAA0664;
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].
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., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-1309.
RC TISSUE=Salivary gland;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 176-1309.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 280-1309, AND VARIANT VAL-633.
RC TISSUE=Blood, PNS, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279; SER-281 AND SER-664, AND
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654 AND SER-664, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, 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 [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=25349259; DOI=10.1083/jcb.201403129;
RA Gao J., Schatton D., Martinelli P., Hansen H., Pla-Martin D., Barth E.,
RA Becker C., Altmueller J., Frommolt P., Sardiello M., Rugarli E.I.;
RT "CLUH regulates mitochondrial biogenesis by binding mRNAs of nuclear-
RT encoded mitochondrial proteins.";
RL J. Cell Biol. 207:213-223(2014).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: mRNA-binding protein involved in proper cytoplasmic
CC distribution of mitochondria. Specifically binds mRNAs of nuclear-
CC encoded mitochondrial proteins in the cytoplasm and regulates transport
CC or translation of these transcripts close to mitochondria, playing a
CC role in mitochondrial biogenesis. {ECO:0000255|HAMAP-Rule:MF_03013,
CC ECO:0000269|PubMed:25349259}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03013}.
CC Cytoplasmic granule {ECO:0000269|PubMed:25349259}. Note=A fraction
CC colocalizes with tyrosinated tubulin and can be detected close to
CC mitochondria. {ECO:0000269|PubMed:25349259}.
CC -!- SIMILARITY: Belongs to the CLU family. {ECO:0000255|HAMAP-
CC Rule:MF_03013}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK023003; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AK125717; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAH10532.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK125717; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK023003; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CR627449; CAH10532.1; ALT_INIT; mRNA.
DR EMBL; AB014564; BAA31639.1; -; mRNA.
DR EMBL; BC004266; AAH04266.1; -; mRNA.
DR EMBL; BC033614; AAH33614.1; -; mRNA.
DR EMBL; BC063786; AAH63786.1; -; mRNA.
DR RefSeq; NP_056044.3; NM_015229.3.
DR AlphaFoldDB; O75153; -.
DR SMR; O75153; -.
DR BioGRID; 116878; 115.
DR IntAct; O75153; 32.
DR MINT; O75153; -.
DR STRING; 9606.ENSP00000458986; -.
DR ChEMBL; CHEMBL4295673; -.
DR GlyGen; O75153; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75153; -.
DR MetOSite; O75153; -.
DR PhosphoSitePlus; O75153; -.
DR SwissPalm; O75153; -.
DR BioMuta; CLUH; -.
DR EPD; O75153; -.
DR jPOST; O75153; -.
DR MassIVE; O75153; -.
DR MaxQB; O75153; -.
DR PaxDb; O75153; -.
DR PeptideAtlas; O75153; -.
DR PRIDE; O75153; -.
DR ProteomicsDB; 49819; -.
DR Antibodypedia; 22958; 77 antibodies from 16 providers.
DR DNASU; 23277; -.
DR Ensembl; ENST00000435359.5; ENSP00000388872.1; ENSG00000132361.18.
DR Ensembl; ENST00000570628.6; ENSP00000458986.1; ENSG00000132361.18.
DR GeneID; 23277; -.
DR KEGG; hsa:23277; -.
DR UCSC; uc002fuy.1; human.
DR CTD; 23277; -.
DR DisGeNET; 23277; -.
DR GeneCards; CLUH; -.
DR HGNC; HGNC:29094; CLUH.
DR HPA; ENSG00000132361; Low tissue specificity.
DR MIM; 616184; gene.
DR neXtProt; NX_O75153; -.
DR OpenTargets; ENSG00000132361; -.
DR PharmGKB; PA142671614; -.
DR VEuPathDB; HostDB:ENSG00000132361; -.
DR eggNOG; KOG1839; Eukaryota.
DR GeneTree; ENSGT00390000012485; -.
DR InParanoid; O75153; -.
DR OrthoDB; 60958at2759; -.
DR PhylomeDB; O75153; -.
DR TreeFam; TF300565; -.
DR PathwayCommons; O75153; -.
DR SignaLink; O75153; -.
DR BioGRID-ORCS; 23277; 74 hits in 1072 CRISPR screens.
DR GenomeRNAi; 23277; -.
DR Pharos; O75153; Tbio.
DR PRO; PR:O75153; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O75153; protein.
DR Bgee; ENSG00000132361; Expressed in gingival epithelium and 191 other tissues.
DR ExpressionAtlas; O75153; baseline and differential.
DR Genevisible; O75153; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR CDD; cd15466; CLU-central; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.30.2280.10; -; 1.
DR HAMAP; MF_03013; CLU; 1.
DR InterPro; IPR033646; CLU-central.
DR InterPro; IPR025697; CLU_dom.
DR InterPro; IPR028275; CLU_N.
DR InterPro; IPR027523; CLU_prot.
DR InterPro; IPR023231; GSKIP_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR12601; PTHR12601; 1.
DR Pfam; PF13236; CLU; 1.
DR Pfam; PF15044; CLU_N; 1.
DR Pfam; PF12807; eIF3_p135; 1.
DR SUPFAM; SSF103107; SSF103107; 1.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS51823; CLU; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW TPR repeat.
FT CHAIN 1..1309
FT /note="Clustered mitochondria protein homolog"
FT /id="PRO_0000123553"
FT DOMAIN 335..577
FT /note="Clu"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01167"
FT REPEAT 978..1011
FT /note="TPR 1"
FT REPEAT 1020..1053
FT /note="TPR 2"
FT REPEAT 1104..1137
FT /note="TPR 3"
FT REPEAT 1146..1179
FT /note="TPR 4"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1264..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 633
FT /note="A -> V (in dbSNP:rs11078312)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034008"
FT CONFLICT 220
FT /note="M -> T (in Ref. 1; AK125717)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="V -> A (in Ref. 4; AAH63786)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="D -> G (in Ref. 1; AK125717)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="T -> TA (in Ref. 1; AK023003, 2; CAH10532 and 4;
FT AAH63786)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="K -> E (in Ref. 1; AK125717)"
FT /evidence="ECO:0000305"
FT CONFLICT 1104
FT /note="A -> G (in Ref. 1; AK023003)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="S -> N (in Ref. 2; CAH10532)"
FT /evidence="ECO:0000305"
FT CONFLICT 1209
FT /note="N -> S (in Ref. 1; AK125717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1309 AA; 146670 MW; 715A7BA3A9874D2E CRC64;
MLLNGDCPES LKKEAAAAEP PRENGLDEAG PGDETTGQEV IVIQDTGFSV KILAPGIEPF
SLQVSPQEMV QEIHQVLMDR EDTCHRTCFS LHLDGNVLDH FSELRSVEGL QEGSVLRVVE
EPYTVREARI HVRHVRDLLK SLDPSDAFNG VDCNSLSFLS VFTDGDLGDS GKRKKGLEMD
PIDCTPPEYI LPGSRERPLC PLQPQNRDWK PLQCLKVLTM SGWNPPPGNR KMHGDLMYLF
VITAEDRQVS ITASTRGFYL NQSTAYHFNP KPASPRFLSH SLVELLNQIS PTFKKNFAVL
QKKRVQRHPF ERIATPFQVY SWTAPQAEHA MDCVRAEDAY TSRLGYEEHI PGQTRDWNEE
LQTTRELPRK NLPERLLRER AIFKVHSDFT AAATRGAMAV IDGNVMAINP SEETKMQMFI
WNNIFFSLGF DVRDHYKDFG GDVAAYVAPT NDLNGVRTYN AVDVEGLYTL GTVVVDYRGY
RVTAQSIIPG ILERDQEQSV IYGSIDFGKT VVSHPRYLEL LERTSRPLKI LRHQVLNDRD
EEVELCSSVE CKGIIGNDGR HYILDLLRTF PPDLNFLPVP GEELPEECAR AGFPRAHRHK
LCCLRQELVD AFVEHRYLLF MKLAALQLMQ QNASQLETPS SLENGGPSSL ESKSEDPPGQ
EAGSEEEGSS ASGLAKVKEL AETIAADDGT DPRSREVIRN ACKAVGSISS TAFDIRFNPD
IFSPGVRFPE SCQDEVRDQK QLLKDAAAFL LSCQIPGLVK DCMEHAVLPV DGATLAEVMR
QRGINMRYLG KVLELVLRSP ARHQLDHVFK IGIGELITRS AKHIFKTYLQ GVELSGLSAA
ISHFLNCFLS SYPNPVAHLP ADELVSKKRN KRRKNRPPGA ADNTAWAVMT PQELWKNICQ
EAKNYFDFDL ECETVDQAVE TYGLQKITLL REISLKTGIQ VLLKEYSFDS RHKPAFTEED
VLNIFPVVKH VNPKASDAFH FFQSGQAKVQ QGFLKEGCEL INEALNLFNN VYGAMHVETC
ACLRLLARLH YIMGDYAEAL SNQQKAVLMS ERVMGTEHPN TIQEYMHLAL YCFASSQLST
ALSLLYRARY LMLLVFGEDH PEMALLDNNI GLVLHGVMEY DLSLRFLENA LAVSTKYHGP
KALKVALSHH LVARVYESKA EFRSALQHEK EGYTIYKTQL GEDHEKTKES SEYLKCLTQQ
AVALQRTMNE IYRNGSSANI PPLKFTAPSM ASVLEQLNVI NGILFIPLSQ KDLENLKAEV
ARRHQLQEAS RNRDRAEEPM ATEPAPAGAP GDLGSQPPAA KDPSPSVQG
