CK054_HUMAN
ID CK054_HUMAN Reviewed; 315 AA.
AC Q9H0W9; A8K850; Q6FI88; Q6XYB0; Q96EI3; Q96IX1; Q9Y6B4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ester hydrolase C11orf54;
DE EC=3.1.-.-;
GN Name=C11orf54; ORFNames=LP4947, PTD012;
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] (ISOFORM 4).
RC TISSUE=Pituitary tumor;
RA Mao Y., Song H., Peng Y., Huang Q., Dai M., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RT "Human PTD012 mRNA, complete cds.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Esophagus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Colon, and Skeletal muscle;
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 [8]
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 [9]
RP IDENTIFICATION BY 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).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-315, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=16522806; DOI=10.1110/ps.052037006;
RA Manjasetty B.A., Buessow K., Fieber-Erdmann M., Roske Y., Gobom J.,
RA Scheich C., Goetz F., Niesen F.H., Heinemann U.;
RT "Crystal structure of Homo sapiens PTD012 reveals a zinc-containing
RT hydrolase fold.";
RL Protein Sci. 15:914-920(2006).
CC -!- FUNCTION: Exhibits ester hydrolase activity on the substrate p-
CC nitrophenyl acetate. {ECO:0000269|PubMed:16522806}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16522806}.
CC -!- INTERACTION:
CC Q9H0W9; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-740204, EBI-2212028;
CC Q9H0W9; Q15645: TRIP13; NbExp=3; IntAct=EBI-740204, EBI-358993;
CC Q9H0W9; Q08AM6: VAC14; NbExp=4; IntAct=EBI-740204, EBI-2107455;
CC Q9H0W9-3; Q86V38: ATN1; NbExp=3; IntAct=EBI-12108466, EBI-11954292;
CC Q9H0W9-3; P55212: CASP6; NbExp=3; IntAct=EBI-12108466, EBI-718729;
CC Q9H0W9-3; P02489: CRYAA; NbExp=3; IntAct=EBI-12108466, EBI-6875961;
CC Q9H0W9-3; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-12108466, EBI-12593112;
CC Q9H0W9-3; O14901: KLF11; NbExp=3; IntAct=EBI-12108466, EBI-948266;
CC Q9H0W9-3; Q92876: KLK6; NbExp=3; IntAct=EBI-12108466, EBI-2432309;
CC Q9H0W9-3; P13473-2: LAMP2; NbExp=3; IntAct=EBI-12108466, EBI-21591415;
CC Q9H0W9-3; Q13153: PAK1; NbExp=3; IntAct=EBI-12108466, EBI-1307;
CC Q9H0W9-3; P62826: RAN; NbExp=3; IntAct=EBI-12108466, EBI-286642;
CC Q9H0W9-3; Q15645: TRIP13; NbExp=3; IntAct=EBI-12108466, EBI-358993;
CC Q9H0W9-3; Q08AM6: VAC14; NbExp=3; IntAct=EBI-12108466, EBI-2107455;
CC Q9H0W9-4; P04792: HSPB1; NbExp=3; IntAct=EBI-25849710, EBI-352682;
CC Q9H0W9-4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-25849710, EBI-10975473;
CC Q9H0W9-4; O76024: WFS1; NbExp=3; IntAct=EBI-25849710, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16522806}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9H0W9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0W9-2; Sequence=VSP_019818;
CC Name=3;
CC IsoId=Q9H0W9-3; Sequence=VSP_019821;
CC Name=4;
CC IsoId=Q9H0W9-4; Sequence=VSP_019817;
CC -!- MISCELLANEOUS: [Isoform 3]: Probably non-functional. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07110.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAP34483.1; Type=Frameshift; 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; AF092133; AAD40375.1; -; mRNA.
DR EMBL; AL136605; CAB66540.1; -; mRNA.
DR EMBL; CR533538; CAG38569.1; -; mRNA.
DR EMBL; AY203960; AAP34483.1; ALT_FRAME; mRNA.
DR EMBL; AK292215; BAF84904.1; -; mRNA.
DR EMBL; CH471065; EAW66915.1; -; Genomic_DNA.
DR EMBL; BC007110; AAH07110.2; ALT_INIT; mRNA.
DR EMBL; BC012298; AAH12298.1; -; mRNA.
DR CCDS; CCDS66204.1; -. [Q9H0W9-1]
DR CCDS; CCDS73366.1; -. [Q9H0W9-2]
DR CCDS; CCDS8294.1; -. [Q9H0W9-3]
DR RefSeq; NP_001272996.1; NM_001286067.1. [Q9H0W9-1]
DR RefSeq; NP_001272997.1; NM_001286068.1. [Q9H0W9-1]
DR RefSeq; NP_001272998.1; NM_001286069.1. [Q9H0W9-1]
DR RefSeq; NP_001272999.1; NM_001286070.1. [Q9H0W9-2]
DR RefSeq; NP_001273000.1; NM_001286071.1.
DR RefSeq; NP_054758.2; NM_014039.3. [Q9H0W9-3]
DR RefSeq; XP_006718887.1; XM_006718824.1.
DR RefSeq; XP_011541083.1; XM_011542781.2. [Q9H0W9-1]
DR RefSeq; XP_011541084.1; XM_011542782.2. [Q9H0W9-1]
DR RefSeq; XP_016873102.1; XM_017017613.1.
DR RefSeq; XP_016873103.1; XM_017017614.1.
DR RefSeq; XP_016873104.1; XM_017017615.1.
DR RefSeq; XP_016873105.1; XM_017017616.1.
DR PDB; 1XCR; X-ray; 1.70 A; A/B=2-315.
DR PDBsum; 1XCR; -.
DR AlphaFoldDB; Q9H0W9; -.
DR SMR; Q9H0W9; -.
DR BioGRID; 118794; 50.
DR IntAct; Q9H0W9; 17.
DR STRING; 9606.ENSP00000331209; -.
DR GlyGen; Q9H0W9; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q9H0W9; -.
DR PhosphoSitePlus; Q9H0W9; -.
DR BioMuta; C11orf54; -.
DR DMDM; 74718025; -.
DR EPD; Q9H0W9; -.
DR jPOST; Q9H0W9; -.
DR MassIVE; Q9H0W9; -.
DR MaxQB; Q9H0W9; -.
DR PeptideAtlas; Q9H0W9; -.
DR PRIDE; Q9H0W9; -.
DR ProteomicsDB; 80335; -. [Q9H0W9-1]
DR ProteomicsDB; 80336; -. [Q9H0W9-2]
DR ProteomicsDB; 80337; -. [Q9H0W9-3]
DR ProteomicsDB; 80338; -. [Q9H0W9-4]
DR Antibodypedia; 31588; 59 antibodies from 16 providers.
DR DNASU; 28970; -.
DR Ensembl; ENST00000331239.8; ENSP00000331209.4; ENSG00000182919.15. [Q9H0W9-1]
DR Ensembl; ENST00000354421.8; ENSP00000346403.3; ENSG00000182919.15. [Q9H0W9-1]
DR Ensembl; ENST00000528099.5; ENSP00000435113.1; ENSG00000182919.15. [Q9H0W9-1]
DR Ensembl; ENST00000528288.5; ENSP00000433721.1; ENSG00000182919.15. [Q9H0W9-3]
DR Ensembl; ENST00000540113.5; ENSP00000442094.1; ENSG00000182919.15. [Q9H0W9-2]
DR GeneID; 28970; -.
DR KEGG; hsa:28970; -.
DR MANE-Select; ENST00000354421.8; ENSP00000346403.3; NM_001286069.2; NP_001272998.1.
DR UCSC; uc001pef.5; human. [Q9H0W9-1]
DR CTD; 28970; -.
DR DisGeNET; 28970; -.
DR GeneCards; C11orf54; -.
DR HGNC; HGNC:30204; C11orf54.
DR HPA; ENSG00000182919; Group enriched (kidney, liver).
DR MIM; 615810; gene.
DR neXtProt; NX_Q9H0W9; -.
DR OpenTargets; ENSG00000182919; -.
DR PharmGKB; PA143485349; -.
DR VEuPathDB; HostDB:ENSG00000182919; -.
DR eggNOG; KOG4048; Eukaryota.
DR GeneTree; ENSGT00390000017214; -.
DR InParanoid; Q9H0W9; -.
DR OMA; HIMPDFS; -.
DR OrthoDB; 877242at2759; -.
DR PhylomeDB; Q9H0W9; -.
DR TreeFam; TF313169; -.
DR PathwayCommons; Q9H0W9; -.
DR SignaLink; Q9H0W9; -.
DR BioGRID-ORCS; 28970; 17 hits in 1051 CRISPR screens.
DR ChiTaRS; C11orf54; human.
DR EvolutionaryTrace; Q9H0W9; -.
DR GeneWiki; C11orf54; -.
DR GenomeRNAi; 28970; -.
DR Pharos; Q9H0W9; Tbio.
DR PRO; PR:Q9H0W9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9H0W9; protein.
DR Bgee; ENSG00000182919; Expressed in kidney epithelium and 191 other tissues.
DR ExpressionAtlas; Q9H0W9; baseline and differential.
DR Genevisible; Q9H0W9; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IDA:FlyBase.
DR InterPro; IPR015021; DUF1907.
DR PANTHER; PTHR13204; PTHR13204; 1.
DR Pfam; PF08925; DUF1907; 1.
DR SMART; SM01168; DUF1907; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..315
FT /note="Ester hydrolase C11orf54"
FT /id="PRO_0000246029"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT VAR_SEQ 1..111
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019817"
FT VAR_SEQ 1..19
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019818"
FT VAR_SEQ 170..219
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019821"
FT CONFLICT 10
FT /note="V -> A (in Ref. 3; CAG38569)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="F -> L (in Ref. 3; CAG38569)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="D -> G (in Ref. 1; AAD40375)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1XCR"
FT HELIX 13..27
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:1XCR"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:1XCR"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1XCR"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1XCR"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 129..133
FT /evidence="ECO:0007829|PDB:1XCR"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:1XCR"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 153..163
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 169..178
FT /evidence="ECO:0007829|PDB:1XCR"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 202..218
FT /evidence="ECO:0007829|PDB:1XCR"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:1XCR"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 289..296
FT /evidence="ECO:0007829|PDB:1XCR"
FT STRAND 298..304
FT /evidence="ECO:0007829|PDB:1XCR"
SQ SEQUENCE 315 AA; 35117 MW; F084671CC1E3F72A CRC64;
MACAEFSFHV PSLEELAGVM QKGLKDNFAD VQVSVVDCPD LTKEPFTFPV KGICGKTRIA
EVGGVPYLLP LVNQKKVYDL NKIAKEIKLP GAFILGAGAG PFQTLGFNSE FMPVIQTESE
HKPPVNGSYF AHVNPADGGC LLEKYSEKCH DFQCALLANL FASEGQPGKV IEVKAKRRTG
PLNFVTCMRE TLEKHYGNKP IGMGGTFIIQ KGKVKSHIMP AEFSSCPLNS DEEVNKWLHF
YEMKAPLVCL PVFVSRDPGF DLRLEHTHFF SRHGEGGHYH YDTTPDIVEY LGYFLPAEFL
YRIDQPKETH SIGRD
