Full text data of UFD1L
UFD1L
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin fusion degradation protein 1 homolog; UB fusion protein 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin fusion degradation protein 1 homolog; UB fusion protein 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q92890
ID UFD1_HUMAN Reviewed; 307 AA.
AC Q92890; A8MW31; Q9Y5N0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-NOV-2007, sequence version 3.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Ubiquitin fusion degradation protein 1 homolog;
DE Short=UB fusion protein 1;
GN Name=UFD1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND VARIANT
RP ALA-130.
RC TISSUE=Brain;
RX PubMed=9063746; DOI=10.1093/hmg/6.2.259;
RA Pizzuti A., Novelli G., Ratti A., Amati F., Mari A., Calabrese G.,
RA Nicolis S., Silani V., Marino B., Scarlato G., Ottolenghi S.,
RA Dallapiccola B.;
RT "UFD1L, a developmentally expressed ubiquitination gene, is deleted in
RT CATCH 22 syndrome.";
RL Hum. Mol. Genet. 6:259-265(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC TISSUE=Heart;
RA Gong L., Yeh E.T.H.;
RT "Characterization of human UFD1, a ubiquitin fusion-degradation
RT protein.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC TISSUE=Brain, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH NPLOC4.
RX PubMed=11574150; DOI=10.1016/S0378-1119(01)00649-7;
RA Botta A., Tandoi C., Fini G., Calabrese G., Dallapiccola B.,
RA Novelli G.;
RT "Cloning and characterization of the gene encoding human NPL4, a
RT protein interacting with the ubiquitin fusion-degradation protein
RT (UFD1L).";
RL Gene 275:39-46(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-245; SER-247
RP AND SER-299, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP INTERACTION WITH USP13.
RX PubMed=21571647; DOI=10.1073/pnas.1100028108;
RA Chen M., Gutierrez G.J., Ronai Z.A.;
RT "Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum
RT (ER) stress response to cell cycle control.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP STRUCTURE BY NMR OF 11-193.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of human ubiquitin fusion degradation protein 1
RT homolog UFD1.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Essential component of the ubiquitin-dependent
CC proteolytic pathway which degrades ubiquitin fusion proteins. The
CC ternary complex containing UFD1L, VCP and NPLOC4 binds
CC ubiquitinated proteins and is necessary for the export of
CC misfolded proteins from the ER to the cytoplasm, where they are
CC degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates
CC spindle disassembly at the end of mitosis and is necessary for the
CC formation of a closed nuclear envelope. It may be involved in the
CC development of some ectoderm-derived structures.
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent
CC pathway.
CC -!- SUBUNIT: Heterodimer with NPLOC4, this heterodimer binds VCP and
CC inhibits Golgi membrane fusion. Interacts with USP13.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm, cytosol
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Short;
CC IsoId=Q92890-2; Sequence=Displayed;
CC Note=Major isoform;
CC Name=Long;
CC IsoId=Q92890-1; Sequence=VSP_006707;
CC Name=3;
CC IsoId=Q92890-3; Sequence=VSP_045044;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Found in adult heart, skeletal muscle and
CC pancreas, and in fetal liver and kidney.
CC -!- SIMILARITY: Belongs to the UFD1 family.
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DR EMBL; U64444; AAD08720.1; -; mRNA.
DR EMBL; AF141201; AAD28788.1; -; mRNA.
DR EMBL; CR456607; CAG30493.1; -; mRNA.
DR EMBL; AK225877; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC000068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC000087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001049; AAH01049.1; -; mRNA.
DR EMBL; BC005087; AAH05087.1; -; mRNA.
DR RefSeq; NP_001030324.2; NM_001035247.2.
DR RefSeq; NP_005650.2; NM_005659.6.
DR UniGene; Hs.474213; -.
DR PDB; 2YUJ; NMR; -; A=11-193.
DR PDBsum; 2YUJ; -.
DR ProteinModelPortal; Q92890; -.
DR SMR; Q92890; 11-193.
DR DIP; DIP-45954N; -.
DR IntAct; Q92890; 26.
DR MINT; MINT-2837704; -.
DR STRING; 9606.ENSP00000263202; -.
DR PhosphoSite; Q92890; -.
DR DMDM; 160332310; -.
DR OGP; Q92890; -.
DR PaxDb; Q92890; -.
DR PRIDE; Q92890; -.
DR DNASU; 7353; -.
DR Ensembl; ENST00000263202; ENSP00000263202; ENSG00000070010.
DR Ensembl; ENST00000399523; ENSP00000382439; ENSG00000070010.
DR GeneID; 7353; -.
DR KEGG; hsa:7353; -.
DR UCSC; uc002zpm.2; human.
DR CTD; 7353; -.
DR GeneCards; GC22M019437; -.
DR HGNC; HGNC:12520; UFD1L.
DR HPA; HPA030287; -.
DR MIM; 601754; gene.
DR neXtProt; NX_Q92890; -.
DR Orphanet; 567; 22q11.2 deletion syndrome.
DR PharmGKB; PA37167; -.
DR eggNOG; COG5140; -.
DR HOGENOM; HOG000212737; -.
DR HOVERGEN; HBG001266; -.
DR KO; K14016; -.
DR OMA; STQYRCY; -.
DR OrthoDB; EOG70ZZNS; -.
DR UniPathway; UPA00144; -.
DR ChiTaRS; UFD1L; human.
DR EvolutionaryTrace; Q92890; -.
DR GeneWiki; UFD1L; -.
DR GenomeRNAi; 7353; -.
DR NextBio; 28788; -.
DR PRO; PR:Q92890; -.
DR ArrayExpress; Q92890; -.
DR Bgee; Q92890; -.
DR CleanEx; HS_UFD1L; -.
DR Genevestigator; Q92890; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:deubiquitinase activity; TAS:ProtInc.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
DR InterPro; IPR004854; UFD1.
DR PANTHER; PTHR12555; PTHR12555; 1.
DR Pfam; PF03152; UFD1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1 307 Ubiquitin fusion degradation protein 1
FT homolog.
FT /FTId=PRO_0000194984.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 231 231 Phosphoserine.
FT MOD_RES 245 245 Phosphoserine.
FT MOD_RES 247 247 Phosphoserine.
FT MOD_RES 299 299 Phosphoserine.
FT VAR_SEQ 106 106 E -> EDGLVQLETVNLQVATYSKSKFCYLPHWMMQNLLLE
FT E (in isoform Long).
FT /FTId=VSP_006707.
FT VAR_SEQ 267 307 Missing (in isoform 3).
FT /FTId=VSP_045044.
FT VARIANT 130 130 P -> A (in dbSNP:rs17744624).
FT /FTId=VAR_052436.
FT CONFLICT 25 25 C -> R (in Ref. 4; AK225877).
FT CONFLICT 33 33 G -> W (in Ref. 1; AAD08720).
FT CONFLICT 183 183 I -> H (in Ref. 1; AAD08720).
FT STRAND 16 18
FT STRAND 20 26
FT STRAND 31 35
FT TURN 39 44
FT STRAND 45 47
FT HELIX 50 58
FT STRAND 66 71
FT TURN 72 75
FT STRAND 76 84
FT STRAND 91 93
FT HELIX 97 102
FT STRAND 108 115
FT STRAND 121 129
FT HELIX 130 134
FT HELIX 138 146
FT STRAND 157 164
FT STRAND 166 181
FT STRAND 188 191
SQ SEQUENCE 307 AA; 34500 MW; FC69860002C042C6 CRC64;
MFSFNMFDHP IPRVFQNRFS TQYRCFSVSM LAGPNDRSDV EKGGKIIMPP SALDQLSRLN
ITYPMLFKLT NKNSDRMTHC GVLEFVADEG ICYLPHWMMQ NLLLEEGGLV QVESVNLQVA
TYSKFQPQSP DFLDITNPKA VLENALRNFA CLTTGDVIAI NYNEKIYELR VMETKPDKAV
SIIECDMNVD FDAPLGYKEP ERQVQHEEST EGEADHSGYA GELGFRAFSG SGNRLDGKKK
GVEPSPSPIK PGDIKRGIPN YEFKLGKITF IRNSRPLVKK VEEDEAGGRF VAFSGEGQSL
RKKGRKP
//
ID UFD1_HUMAN Reviewed; 307 AA.
AC Q92890; A8MW31; Q9Y5N0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 13-NOV-2007, sequence version 3.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Ubiquitin fusion degradation protein 1 homolog;
DE Short=UB fusion protein 1;
GN Name=UFD1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND VARIANT
RP ALA-130.
RC TISSUE=Brain;
RX PubMed=9063746; DOI=10.1093/hmg/6.2.259;
RA Pizzuti A., Novelli G., Ratti A., Amati F., Mari A., Calabrese G.,
RA Nicolis S., Silani V., Marino B., Scarlato G., Ottolenghi S.,
RA Dallapiccola B.;
RT "UFD1L, a developmentally expressed ubiquitination gene, is deleted in
RT CATCH 22 syndrome.";
RL Hum. Mol. Genet. 6:259-265(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC TISSUE=Heart;
RA Gong L., Yeh E.T.H.;
RT "Characterization of human UFD1, a ubiquitin fusion-degradation
RT protein.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC TISSUE=Brain, and 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH NPLOC4.
RX PubMed=11574150; DOI=10.1016/S0378-1119(01)00649-7;
RA Botta A., Tandoi C., Fini G., Calabrese G., Dallapiccola B.,
RA Novelli G.;
RT "Cloning and characterization of the gene encoding human NPL4, a
RT protein interacting with the ubiquitin fusion-degradation protein
RT (UFD1L).";
RL Gene 275:39-46(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP SPECTROMETRY.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP SPECTROMETRY.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-245; SER-247
RP AND SER-299, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP INTERACTION WITH USP13.
RX PubMed=21571647; DOI=10.1073/pnas.1100028108;
RA Chen M., Gutierrez G.J., Ronai Z.A.;
RT "Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum
RT (ER) stress response to cell cycle control.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9119-9124(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP STRUCTURE BY NMR OF 11-193.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of human ubiquitin fusion degradation protein 1
RT homolog UFD1.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Essential component of the ubiquitin-dependent
CC proteolytic pathway which degrades ubiquitin fusion proteins. The
CC ternary complex containing UFD1L, VCP and NPLOC4 binds
CC ubiquitinated proteins and is necessary for the export of
CC misfolded proteins from the ER to the cytoplasm, where they are
CC degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates
CC spindle disassembly at the end of mitosis and is necessary for the
CC formation of a closed nuclear envelope. It may be involved in the
CC development of some ectoderm-derived structures.
CC -!- PATHWAY: Protein degradation; proteasomal ubiquitin-dependent
CC pathway.
CC -!- SUBUNIT: Heterodimer with NPLOC4, this heterodimer binds VCP and
CC inhibits Golgi membrane fusion. Interacts with USP13.
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm, cytosol
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Short;
CC IsoId=Q92890-2; Sequence=Displayed;
CC Note=Major isoform;
CC Name=Long;
CC IsoId=Q92890-1; Sequence=VSP_006707;
CC Name=3;
CC IsoId=Q92890-3; Sequence=VSP_045044;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Found in adult heart, skeletal muscle and
CC pancreas, and in fetal liver and kidney.
CC -!- SIMILARITY: Belongs to the UFD1 family.
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DR EMBL; U64444; AAD08720.1; -; mRNA.
DR EMBL; AF141201; AAD28788.1; -; mRNA.
DR EMBL; CR456607; CAG30493.1; -; mRNA.
DR EMBL; AK225877; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC000068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC000087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001049; AAH01049.1; -; mRNA.
DR EMBL; BC005087; AAH05087.1; -; mRNA.
DR RefSeq; NP_001030324.2; NM_001035247.2.
DR RefSeq; NP_005650.2; NM_005659.6.
DR UniGene; Hs.474213; -.
DR PDB; 2YUJ; NMR; -; A=11-193.
DR PDBsum; 2YUJ; -.
DR ProteinModelPortal; Q92890; -.
DR SMR; Q92890; 11-193.
DR DIP; DIP-45954N; -.
DR IntAct; Q92890; 26.
DR MINT; MINT-2837704; -.
DR STRING; 9606.ENSP00000263202; -.
DR PhosphoSite; Q92890; -.
DR DMDM; 160332310; -.
DR OGP; Q92890; -.
DR PaxDb; Q92890; -.
DR PRIDE; Q92890; -.
DR DNASU; 7353; -.
DR Ensembl; ENST00000263202; ENSP00000263202; ENSG00000070010.
DR Ensembl; ENST00000399523; ENSP00000382439; ENSG00000070010.
DR GeneID; 7353; -.
DR KEGG; hsa:7353; -.
DR UCSC; uc002zpm.2; human.
DR CTD; 7353; -.
DR GeneCards; GC22M019437; -.
DR HGNC; HGNC:12520; UFD1L.
DR HPA; HPA030287; -.
DR MIM; 601754; gene.
DR neXtProt; NX_Q92890; -.
DR Orphanet; 567; 22q11.2 deletion syndrome.
DR PharmGKB; PA37167; -.
DR eggNOG; COG5140; -.
DR HOGENOM; HOG000212737; -.
DR HOVERGEN; HBG001266; -.
DR KO; K14016; -.
DR OMA; STQYRCY; -.
DR OrthoDB; EOG70ZZNS; -.
DR UniPathway; UPA00144; -.
DR ChiTaRS; UFD1L; human.
DR EvolutionaryTrace; Q92890; -.
DR GeneWiki; UFD1L; -.
DR GenomeRNAi; 7353; -.
DR NextBio; 28788; -.
DR PRO; PR:Q92890; -.
DR ArrayExpress; Q92890; -.
DR Bgee; Q92890; -.
DR CleanEx; HS_UFD1L; -.
DR Genevestigator; Q92890; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:deubiquitinase activity; TAS:ProtInc.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
DR InterPro; IPR004854; UFD1.
DR PANTHER; PTHR12555; PTHR12555; 1.
DR Pfam; PF03152; UFD1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1 307 Ubiquitin fusion degradation protein 1
FT homolog.
FT /FTId=PRO_0000194984.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 231 231 Phosphoserine.
FT MOD_RES 245 245 Phosphoserine.
FT MOD_RES 247 247 Phosphoserine.
FT MOD_RES 299 299 Phosphoserine.
FT VAR_SEQ 106 106 E -> EDGLVQLETVNLQVATYSKSKFCYLPHWMMQNLLLE
FT E (in isoform Long).
FT /FTId=VSP_006707.
FT VAR_SEQ 267 307 Missing (in isoform 3).
FT /FTId=VSP_045044.
FT VARIANT 130 130 P -> A (in dbSNP:rs17744624).
FT /FTId=VAR_052436.
FT CONFLICT 25 25 C -> R (in Ref. 4; AK225877).
FT CONFLICT 33 33 G -> W (in Ref. 1; AAD08720).
FT CONFLICT 183 183 I -> H (in Ref. 1; AAD08720).
FT STRAND 16 18
FT STRAND 20 26
FT STRAND 31 35
FT TURN 39 44
FT STRAND 45 47
FT HELIX 50 58
FT STRAND 66 71
FT TURN 72 75
FT STRAND 76 84
FT STRAND 91 93
FT HELIX 97 102
FT STRAND 108 115
FT STRAND 121 129
FT HELIX 130 134
FT HELIX 138 146
FT STRAND 157 164
FT STRAND 166 181
FT STRAND 188 191
SQ SEQUENCE 307 AA; 34500 MW; FC69860002C042C6 CRC64;
MFSFNMFDHP IPRVFQNRFS TQYRCFSVSM LAGPNDRSDV EKGGKIIMPP SALDQLSRLN
ITYPMLFKLT NKNSDRMTHC GVLEFVADEG ICYLPHWMMQ NLLLEEGGLV QVESVNLQVA
TYSKFQPQSP DFLDITNPKA VLENALRNFA CLTTGDVIAI NYNEKIYELR VMETKPDKAV
SIIECDMNVD FDAPLGYKEP ERQVQHEEST EGEADHSGYA GELGFRAFSG SGNRLDGKKK
GVEPSPSPIK PGDIKRGIPN YEFKLGKITF IRNSRPLVKK VEEDEAGGRF VAFSGEGQSL
RKKGRKP
//
MIM
601754
*RECORD*
*FIELD* NO
601754
*FIELD* TI
*601754 UBIQUITIN FUSION DEGRADATION 1-LIKE; UFD1L
*FIELD* TX
In a search for genes in the 22q11.2 region implicated in the DiGeorge
read moresyndrome (188400), Pizutti et al. (1997) identified a gene whose
functional features and tissue-specific expression suggested a distinct
role in embryogenesis. Symbolized UFD1L by them (for ubiquitin fusion
degradation 1-like), the gene encodes the human homolog of the yeast
ubiquitin fusion degradation 1 (UFD1) protein that is involved in the
degradation of ubiquitin fusion proteins (see 191339). Cloning and
characterization of the murine homolog (Ufd1l) showed it to be expressed
during embryogenesis in the eyes and in the inner ear primordia. These
findings suggested to Pizutti et al. (1997) that the proteolytic pathway
recognizing ubiquitin fusion proteins for degradation is conserved in
vertebrates and that UFD1L gene hemizygosity may be the cause of some of
the CATCH22-associated developmental defects.
The basic helix-loop-helix transcription factor dHAND (HAND2; 602407) is
required for survival of cells in the neural crest-derived branchial and
aortic arch arteries and the right ventricle. Mice lacking endothelin-1
(EDN1; 131240) have cardiac and cranial neural crest defects typical of
the 22q11 deletion syndrome and display downregulation of dHAND,
suggesting that a molecular pathway involving dHAND may be disrupted in
that syndrome. The HAND2, EDN1, and ET1 receptor (EDNRA; 131243) genes
do not map to 22q11, the DiGeorge syndrome critical region, in humans.
In a screen for mouse genes dependent on dHAND, Yamagishi et al. (1999)
identified Ufd1l. Mouse Ufd1l (Yamagishi et al., 1999) and chick Ufd1l
(Yamagishi et al., 2003) are specifically expressed in most tissues
affected in patients with the DiGeorge (22q11 deletion) syndrome.
Yamagishi et al. (2003) demonstrated that functional attenuation of
chick Ufd1l in cardiac neural crest cells resulted in an increased
incidence of conotruncal septation defects.
Yamagishi et al. (1999) found that the human UFD1L gene was deleted in
all 182 patients studied with the 22q11 deletion, and a smaller deletion
of approximately 20 kb that removed exons 1 to 3 of UFD1L was found in 1
individual with features typical of 22q11 deletion syndrome. In the
individual (J.F.) with the smaller deletion, Yamagishi et al. (1999)
showed that the CDC45L gene (603465), which is immediately telomeric of
UFD1L, was the site of the deletion in the region between exons 5 and 6
of the 5-prime breakpoint. They considered that the deletion in CDC45L
may act as a modifier of the phenotype in patient J.F. UFD1L and CDC45L
are transcribed in opposite directions. The deletion left exons 4 to 12
of UFD1L intact; the first 5 exons of CDC45L were deleted. Patient J.F.
had nearly all of the features commonly associated with the 2-Mb 22q11
deletion. Four days after birth the patient was diagnosed with
interrupted aortic arch, persistent truncus arteriosus, cleft palate,
small mouth, low-set ears, broad nasal bridge, neonatal hypocalcemia,
T-lymphocyte deficiency, and syndactyly of her toes. The deletion was
not present in her parents or in 100 control subjects.
*FIELD* RF
1. Pizutti, A.; Novelli, G.; Ratti, A.; Amati, F.; Mari, A.; Calabrese,
G.; Nicolis, S.; Silani, V.; Marino, B.; Scarlato, G.; Ottolenghi,
S.; Dallapiccola, B.: UFD1L, a developmentally expressed ubiquitination
gene, is deleted in CATCH 22 syndrome. Hum. Molec. Genet. 6: 259-265,
1997.
2. Yamagishi, C.; Hierck, B. P.; Gittenberger-De Groot, A. C.; Yamagishi,
H.; Srivastava, D.: Functional attenuation of Ufd1l, a 22q11.2 deletion
syndrome candidate gene, leads to cardiac outflow septation defects
in chicken embryos. Pediat. Res. 53: 546-553, 2003.
3. Yamagishi, H.; Garg, V.; Matsuoka, R.; Thomas, T.; Srivastava,
D.: A molecular pathway revealing a genetic basis for human cardiac
and craniofacial defects. Science 283: 1158-1161, 1999.
*FIELD* CN
Natalie E. Krasikov - updated: 2/10/2004
Victor A. McKusick - updated: 3/5/1999
*FIELD* CD
Victor A. McKusick: 4/15/1997
*FIELD* ED
carol: 05/13/2004
carol: 2/10/2004
mgross: 2/16/2000
terry: 1/12/2000
carol: 3/7/1999
terry: 3/5/1999
mark: 5/13/1997
mark: 4/18/1997
jenny: 4/15/1997
*RECORD*
*FIELD* NO
601754
*FIELD* TI
*601754 UBIQUITIN FUSION DEGRADATION 1-LIKE; UFD1L
*FIELD* TX
In a search for genes in the 22q11.2 region implicated in the DiGeorge
read moresyndrome (188400), Pizutti et al. (1997) identified a gene whose
functional features and tissue-specific expression suggested a distinct
role in embryogenesis. Symbolized UFD1L by them (for ubiquitin fusion
degradation 1-like), the gene encodes the human homolog of the yeast
ubiquitin fusion degradation 1 (UFD1) protein that is involved in the
degradation of ubiquitin fusion proteins (see 191339). Cloning and
characterization of the murine homolog (Ufd1l) showed it to be expressed
during embryogenesis in the eyes and in the inner ear primordia. These
findings suggested to Pizutti et al. (1997) that the proteolytic pathway
recognizing ubiquitin fusion proteins for degradation is conserved in
vertebrates and that UFD1L gene hemizygosity may be the cause of some of
the CATCH22-associated developmental defects.
The basic helix-loop-helix transcription factor dHAND (HAND2; 602407) is
required for survival of cells in the neural crest-derived branchial and
aortic arch arteries and the right ventricle. Mice lacking endothelin-1
(EDN1; 131240) have cardiac and cranial neural crest defects typical of
the 22q11 deletion syndrome and display downregulation of dHAND,
suggesting that a molecular pathway involving dHAND may be disrupted in
that syndrome. The HAND2, EDN1, and ET1 receptor (EDNRA; 131243) genes
do not map to 22q11, the DiGeorge syndrome critical region, in humans.
In a screen for mouse genes dependent on dHAND, Yamagishi et al. (1999)
identified Ufd1l. Mouse Ufd1l (Yamagishi et al., 1999) and chick Ufd1l
(Yamagishi et al., 2003) are specifically expressed in most tissues
affected in patients with the DiGeorge (22q11 deletion) syndrome.
Yamagishi et al. (2003) demonstrated that functional attenuation of
chick Ufd1l in cardiac neural crest cells resulted in an increased
incidence of conotruncal septation defects.
Yamagishi et al. (1999) found that the human UFD1L gene was deleted in
all 182 patients studied with the 22q11 deletion, and a smaller deletion
of approximately 20 kb that removed exons 1 to 3 of UFD1L was found in 1
individual with features typical of 22q11 deletion syndrome. In the
individual (J.F.) with the smaller deletion, Yamagishi et al. (1999)
showed that the CDC45L gene (603465), which is immediately telomeric of
UFD1L, was the site of the deletion in the region between exons 5 and 6
of the 5-prime breakpoint. They considered that the deletion in CDC45L
may act as a modifier of the phenotype in patient J.F. UFD1L and CDC45L
are transcribed in opposite directions. The deletion left exons 4 to 12
of UFD1L intact; the first 5 exons of CDC45L were deleted. Patient J.F.
had nearly all of the features commonly associated with the 2-Mb 22q11
deletion. Four days after birth the patient was diagnosed with
interrupted aortic arch, persistent truncus arteriosus, cleft palate,
small mouth, low-set ears, broad nasal bridge, neonatal hypocalcemia,
T-lymphocyte deficiency, and syndactyly of her toes. The deletion was
not present in her parents or in 100 control subjects.
*FIELD* RF
1. Pizutti, A.; Novelli, G.; Ratti, A.; Amati, F.; Mari, A.; Calabrese,
G.; Nicolis, S.; Silani, V.; Marino, B.; Scarlato, G.; Ottolenghi,
S.; Dallapiccola, B.: UFD1L, a developmentally expressed ubiquitination
gene, is deleted in CATCH 22 syndrome. Hum. Molec. Genet. 6: 259-265,
1997.
2. Yamagishi, C.; Hierck, B. P.; Gittenberger-De Groot, A. C.; Yamagishi,
H.; Srivastava, D.: Functional attenuation of Ufd1l, a 22q11.2 deletion
syndrome candidate gene, leads to cardiac outflow septation defects
in chicken embryos. Pediat. Res. 53: 546-553, 2003.
3. Yamagishi, H.; Garg, V.; Matsuoka, R.; Thomas, T.; Srivastava,
D.: A molecular pathway revealing a genetic basis for human cardiac
and craniofacial defects. Science 283: 1158-1161, 1999.
*FIELD* CN
Natalie E. Krasikov - updated: 2/10/2004
Victor A. McKusick - updated: 3/5/1999
*FIELD* CD
Victor A. McKusick: 4/15/1997
*FIELD* ED
carol: 05/13/2004
carol: 2/10/2004
mgross: 2/16/2000
terry: 1/12/2000
carol: 3/7/1999
terry: 3/5/1999
mark: 5/13/1997
mark: 4/18/1997
jenny: 4/15/1997