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 27-MAR-2024, entry version 157. 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}; 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; 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; Intraflagellar transport complex B. DR IntAct; Q96AJ1; 20. DR STRING; 9606.ENSP00000344392; -. 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; 9606-ENSP00000460850; -. DR PeptideAtlas; Q96AJ1; -. DR ProteomicsDB; 75967; -. [Q96AJ1-1] DR ProteomicsDB; 75968; -. [Q96AJ1-2] DR Pumba; Q96AJ1; -. DR Antibodypedia; 24143; 159 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 AGR; HGNC:19009; -. 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; KPAYQSE; -. DR OrthoDB; 5489815at2759; -. DR PhylomeDB; Q96AJ1; -. DR TreeFam; TF314639; -. DR PathwayCommons; Q96AJ1; -. DR Reactome; R-HSA-5620924; Intraflagellar transport. DR SignaLink; Q96AJ1; -. DR BioGRID-ORCS; 23059; 14 hits in 1155 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 200 other cell types or tissues. DR ExpressionAtlas; Q96AJ1; baseline and differential. 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; NAS:ComplexPortal. 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; CLUSTERIN ASSOCIATED PROTEIN 1; 1. DR PANTHER; PTHR21547:SF0; CLUSTERIN-ASSOCIATED PROTEIN 1; 1. DR Pfam; PF10234; Cluap1; 1. DR Genevisible; Q96AJ1; HS. 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 //