CLUA1_HUMAN
ID CLUA1_HUMAN Reviewed; 413 AA.
AC Q96AJ1; O75138; Q65ZA3; Q9H8R4; Q9H8T1;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 4.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Clusterin-associated protein 1;
DE AltName: Full=Qilin {ECO:0000303|PubMed:15530380};
GN Name=CLUAP1; Synonyms=KIAA0643;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CLU, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Colon tumor;
RX PubMed=15480429; DOI=10.1038/sj.onc.1208100;
RA Takahashi M., Lin Y.-M., Nakamura Y., Furukawa Y.;
RT "Isolation and characterization of a novel gene CLUAP1 whose expression is
RT frequently upregulated in colon cancer.";
RL Oncogene 23:9289-9294(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 222-413 (ISOFORMS 1/2).
RC TISSUE=Ovary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TRP-401.
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 [5]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=15530380; DOI=10.1016/j.cub.2004.10.011;
RA Marshall W.F.;
RT "Human cilia proteome contains homolog of zebrafish polycystic kidney
RT disease gene qilin.";
RL Curr. Biol. 14:R913-R914(2004).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=17203229;
RA Ishikura H., Ikeda H., Abe H., Ohkuri T., Hiraga H., Isu K., Tsukahara T.,
RA Sato N., Kitamura H., Iwasaki N., Takeda N., Minami A., Nishimura T.;
RT "Identification of CLUAP1 as a human osteosarcoma tumor-associated antigen
RT recognized by the humoral immune system.";
RL Int. J. Oncol. 30:461-467(2007).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND IDENTIFICATION BY
RP 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 [9]
RP INTERACTION WITH UBXN10.
RX PubMed=26389662; DOI=10.1038/ncb3238;
RA Raman M., Sergeev M., Garnaas M., Lydeard J.R., Huttlin E.L., Goessling W.,
RA Shah J.V., Harper J.W.;
RT "Systematic proteomics of the VCP-UBXD adaptor network identifies a role
RT for UBXN10 in regulating ciliogenesis.";
RL Nat. Cell Biol. 17:1356-1369(2015).
CC -!- FUNCTION: Required for cilia biogenesis. Appears to function within the
CC multiple intraflagellar transport complex B (IFT-B). Key regulator of
CC hedgehog signaling. {ECO:0000250|UniProtKB:Q8R3P7}.
CC -!- SUBUNIT: Interacts with CLU/clusterin (PubMed:15480429). Interacts with
CC UBXN10; the interaction is direct (PubMed:26389662).
CC {ECO:0000269|PubMed:15480429, ECO:0000269|PubMed:26389662}.
CC -!- INTERACTION:
CC Q96AJ1; Q9BW66: CINP; NbExp=5; IntAct=EBI-739780, EBI-739784;
CC Q96AJ1; P43364: MAGEA11; NbExp=5; IntAct=EBI-739780, EBI-739552;
CC Q96AJ1; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-739780, EBI-10178634;
CC Q96AJ1; P15173: MYOG; NbExp=7; IntAct=EBI-739780, EBI-3906629;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:15530380}. Nucleus {ECO:0000269|PubMed:15480429}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96AJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AJ1-2; Sequence=VSP_019229;
CC -!- TISSUE SPECIFICITY: Expressed in testis, thyroid and trachea and to a
CC lower extent in spinal cord and adrenal gland. Highly expressed in
CC colon cancer and osteosarcoma cell lines. {ECO:0000269|PubMed:15480429,
CC ECO:0000269|PubMed:17203229}.
CC -!- MISCELLANEOUS: Associated with a number of cancers such as colon
CC (PubMed:15480429) and bone cancer (PubMed:17203229). Possibly involved
CC in polycystic kidney diseases (PubMed:15530380).
CC {ECO:0000305|PubMed:15480429, ECO:0000305|PubMed:15530380,
CC ECO:0000305|PubMed:17203229}.
CC -!- SIMILARITY: Belongs to the CLUAP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31618.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAB14523.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB089691; BAD44779.1; -; mRNA.
DR EMBL; AB014543; BAA31618.1; ALT_SEQ; mRNA.
DR EMBL; AK023319; BAB14523.1; ALT_INIT; mRNA.
DR EMBL; AK023359; BAB14542.1; -; mRNA.
DR EMBL; BC017070; AAH17070.3; -; mRNA.
DR CCDS; CCDS32381.1; -. [Q96AJ1-1]
DR CCDS; CCDS45398.1; -. [Q96AJ1-2]
DR RefSeq; NP_055856.1; NM_015041.2. [Q96AJ1-1]
DR RefSeq; NP_079069.1; NM_024793.2. [Q96AJ1-2]
DR AlphaFoldDB; Q96AJ1; -.
DR SMR; Q96AJ1; -.
DR BioGRID; 116694; 227.
DR ComplexPortal; CPX-5022; IFT-B complex.
DR IntAct; Q96AJ1; 20.
DR STRING; 9606.ENSP00000460850; -.
DR iPTMnet; Q96AJ1; -.
DR PhosphoSitePlus; Q96AJ1; -.
DR BioMuta; CLUAP1; -.
DR DMDM; 108935970; -.
DR EPD; Q96AJ1; -.
DR jPOST; Q96AJ1; -.
DR MassIVE; Q96AJ1; -.
DR MaxQB; Q96AJ1; -.
DR PaxDb; Q96AJ1; -.
DR PeptideAtlas; Q96AJ1; -.
DR PRIDE; Q96AJ1; -.
DR ProteomicsDB; 75967; -. [Q96AJ1-1]
DR ProteomicsDB; 75968; -. [Q96AJ1-2]
DR Antibodypedia; 24143; 149 antibodies from 26 providers.
DR DNASU; 23059; -.
DR Ensembl; ENST00000572600.5; ENSP00000460889.1; ENSG00000103351.13. [Q96AJ1-2]
DR Ensembl; ENST00000576634.6; ENSP00000460850.1; ENSG00000103351.13. [Q96AJ1-1]
DR GeneID; 23059; -.
DR KEGG; hsa:23059; -.
DR MANE-Select; ENST00000576634.6; ENSP00000460850.1; NM_015041.3; NP_055856.1.
DR UCSC; uc002cvk.3; human. [Q96AJ1-1]
DR CTD; 23059; -.
DR DisGeNET; 23059; -.
DR GeneCards; CLUAP1; -.
DR HGNC; HGNC:19009; CLUAP1.
DR HPA; ENSG00000103351; Low tissue specificity.
DR MalaCards; CLUAP1; -.
DR neXtProt; NX_Q96AJ1; -.
DR OpenTargets; ENSG00000103351; -.
DR PharmGKB; PA128394600; -.
DR VEuPathDB; HostDB:ENSG00000103351; -.
DR eggNOG; KOG3647; Eukaryota.
DR GeneTree; ENSGT00390000008957; -.
DR HOGENOM; CLU_098325_0_0_1; -.
DR InParanoid; Q96AJ1; -.
DR OMA; DHHRLEQ; -.
DR PhylomeDB; Q96AJ1; -.
DR TreeFam; TF314639; -.
DR PathwayCommons; Q96AJ1; -.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR SignaLink; Q96AJ1; -.
DR BioGRID-ORCS; 23059; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; CLUAP1; human.
DR GeneWiki; CLUAP1; -.
DR GenomeRNAi; 23059; -.
DR Pharos; Q96AJ1; Tbio.
DR PRO; PR:Q96AJ1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96AJ1; protein.
DR Bgee; ENSG00000103351; Expressed in bronchial epithelial cell and 198 other tissues.
DR ExpressionAtlas; Q96AJ1; baseline and differential.
DR Genevisible; Q96AJ1; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0097546; C:ciliary base; IEA:Ensembl.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030991; C:intraciliary transport particle A; IEA:Ensembl.
DR GO; GO:0030992; C:intraciliary transport particle B; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0035082; P:axoneme assembly; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0021508; P:floor plate formation; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0060972; P:left/right pattern formation; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR InterPro; IPR019366; Clusterin-associated_protein-1.
DR PANTHER; PTHR21547; PTHR21547; 1.
DR Pfam; PF10234; Cluap1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..413
FT /note="Clusterin-associated protein 1"
FT /id="PRO_0000239451"
FT REGION 305..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 198..291
FT /evidence="ECO:0000255"
FT COMPBIAS 361..387
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3P7"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3P7"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3P7"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..166
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019229"
FT VARIANT 68
FT /note="A -> S (in dbSNP:rs34115694)"
FT /id="VAR_050869"
FT VARIANT 401
FT /note="R -> W (in dbSNP:rs9790)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_050870"
SQ SEQUENCE 413 AA; 48125 MW; 7A23D4FA2EBE5A9F CRC64;
MSFRDLRNFT EMMRALGYPR HISMENFRTP NFGLVSEVLL WLVKRYEPQT DIPPDVDTEQ
DRVFFIKAIA QFMATKAHIK LNTKKLYQAD GYAVKELLKI TSVLYNAMKT KGMEGSEIVE
EDVNKFKFDL GSKIADLKAA RQLASEITSK GASLYDLLGM EVELREMRTE AIARPLEINE
TEKVMRIAIK EILTQVQKTK DLLNNVASDE ANLEAKIEKR KLELERNRKR LETLQSVRPC
FMDEYEKTEE ELQKQYDTYL EKFQNLTYLE QQLEDHHRME QERFEEAKNT LCLIQNKLKE
EEKRLLKSGS NDDSDIDIQE DDESDSELEE RRLPKPQTAM EMLMQGRPGK RIVGTMQGGD
SDDNEDSEES EIDMEDDDDE DDDLEDESIS LSPTKPNRRV RKSEPLDESD NDF
