Full text data of UFM1
UFM1
(C13orf20)
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin-fold modifier 1; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-fold modifier 1; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P61960
ID UFM1_HUMAN Reviewed; 85 AA.
AC P61960; Q14346; Q5VXS0; Q6IAG6; Q9CPX2; Q9NZF2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Ubiquitin-fold modifier 1;
DE Flags: Precursor;
GN Name=UFM1; Synonyms=C13orf20; ORFNames=BM-002;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLY-83.
RX PubMed=15071506; DOI=10.1038/sj.emboj.7600205;
RA Komatsu M., Chiba T., Tatsumi K., Iemura S., Tanida I., Okazaki N.,
RA Ueno T., Kominami E., Natsume T., Tanaka K.;
RT "A novel protein-conjugating system for Ufm1, a ubiquitin-fold
RT modifier.";
RL EMBO J. 23:1977-1986(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
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 2).
RC TISSUE=Neuroblastoma;
RX PubMed=16344560; DOI=10.1101/gr.4039406;
RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T.,
RA Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H.,
RA Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N.,
RA Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M.,
RA Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T.,
RA Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.;
RT "Diversification of transcriptional modulation: large-scale
RT identification and characterization of putative alternative promoters
RT of human genes.";
RL Genome Res. 16:55-65(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-80 (ISOFORM 1).
RC TISSUE=Brain;
RA Dmitrenko V.V., Garifulin O.M., Kavsan V.M.;
RT "Characterization of different mRNA types expressed in human brain.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=20018847; DOI=10.1074/jbc.M109.036814;
RA Tatsumi K., Sou Y.S., Tada N., Nakamura E., Iemura S., Natsume T.,
RA Kang S.H., Chung C.H., Kasahara M., Kominami E., Yamamoto M.,
RA Tanaka K., Komatsu M.;
RT "A novel type of E3 ligase for the Ufm1 conjugation system.";
RL J. Biol. Chem. 285:5417-5427(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.,
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 [10]
RP STRUCTURE BY NMR.
RX PubMed=16527251; DOI=10.1016/j.bbrc.2006.02.107;
RA Sasakawa H., Sakata E., Yamaguchi Y., Komatsu M., Tatsumi K.,
RA Kominami E., Tanaka K., Kato K.;
RT "Solution structure and dynamics of Ufm1, a ubiquitin-fold modifier
RT 1.";
RL Biochem. Biophys. Res. Commun. 343:21-26(2006).
CC -!- FUNCTION: Ubiquitin-like modifier protein which binds to a number
CC of target proteins, such as DDRGK1.
CC -!- INTERACTION:
CC Q96JB5:CDK5RAP3; NbExp=1; IntAct=EBI-1045061, EBI-718818;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly
CC nuclear. Also expressed diffusely in the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61960-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61960-2; Sequence=VSP_041186;
CC -!- SIMILARITY: Belongs to the UFM1 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB154404; BAD15373.1; -; mRNA.
DR EMBL; AF208844; AAF64258.1; -; mRNA.
DR EMBL; CR457189; CAG33470.1; -; mRNA.
DR EMBL; DA664581; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL356863; CAH70411.1; -; Genomic_DNA.
DR EMBL; AL356863; CAH70414.1; -; Genomic_DNA.
DR EMBL; BC005193; AAH05193.1; -; mRNA.
DR EMBL; Z70222; CAA94181.1; -; mRNA.
DR RefSeq; NP_057701.1; NM_016617.3.
DR UniGene; Hs.643655; -.
DR PDB; 1WXS; NMR; -; A=1-85.
DR PDBsum; 1WXS; -.
DR ProteinModelPortal; P61960; -.
DR SMR; P61960; 1-85.
DR IntAct; P61960; 6.
DR MINT; MINT-7005139; -.
DR STRING; 9606.ENSP00000239878; -.
DR PhosphoSite; P61960; -.
DR DMDM; 48428799; -.
DR PaxDb; P61960; -.
DR PRIDE; P61960; -.
DR DNASU; 51569; -.
DR Ensembl; ENST00000239878; ENSP00000239878; ENSG00000120686.
DR Ensembl; ENST00000379641; ENSP00000368962; ENSG00000120686.
DR Ensembl; ENST00000379649; ENSP00000368970; ENSG00000120686.
DR GeneID; 51569; -.
DR KEGG; hsa:51569; -.
DR UCSC; uc001uwu.3; human.
DR CTD; 51569; -.
DR GeneCards; GC13P038923; -.
DR HGNC; HGNC:20597; UFM1.
DR HPA; HPA039758; -.
DR MIM; 610553; gene.
DR neXtProt; NX_P61960; -.
DR PharmGKB; PA134863405; -.
DR eggNOG; NOG249065; -.
DR HOGENOM; HOG000238677; -.
DR HOVERGEN; HBG094129; -.
DR KO; K12162; -.
DR OMA; VTFKIIL; -.
DR OrthoDB; EOG7Q8CQW; -.
DR PhylomeDB; P61960; -.
DR ChiTaRS; UFM1; human.
DR EvolutionaryTrace; P61960; -.
DR GeneWiki; UFM1; -.
DR GenomeRNAi; 51569; -.
DR NextBio; 55392; -.
DR PRO; PR:P61960; -.
DR Bgee; P61960; -.
DR CleanEx; HS_UFM1; -.
DR Genevestigator; P61960; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071569; P:protein ufmylation; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:MGI.
DR InterPro; IPR005375; UFM1.
DR Pfam; PF03671; Ufm1; 1.
DR PIRSF; PIRSF038027; Ubiquitin-like_Ufm1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1 83 Ubiquitin-fold modifier 1.
FT /FTId=PRO_0000042122.
FT PROPEP 84 85 Removed in mature form.
FT /FTId=PRO_0000042123.
FT CROSSLNK 83 83 Glycyl lysine isopeptide (Gly-Lys)
FT (interchain with K-? in acceptor
FT proteins) (Potential).
FT VAR_SEQ 1 20 MSKVSFKITLTSDPRLPYKV -> MIRAFPTTTPRSLHLFT
FT SSTFLARALPGAFPTGACEER (in isoform 2).
FT /FTId=VSP_041186.
FT MUTAGEN 83 83 G->A: Confers resistance to cleavage.
FT CONFLICT 12 12 S -> W (in Ref. 7; CAA94181).
FT CONFLICT 78 80 PRD -> LEI (in Ref. 7; CAA94181).
FT STRAND 4 11
FT STRAND 14 16
FT STRAND 20 23
FT STRAND 25 28
FT HELIX 29 39
FT STRAND 44 53
FT HELIX 63 69
FT STRAND 72 79
SQ SEQUENCE 85 AA; 9118 MW; EDB2412E5E5836D8 CRC64;
MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA
QTAGNVFLKH GSELRIIPRD RVGSC
//
ID UFM1_HUMAN Reviewed; 85 AA.
AC P61960; Q14346; Q5VXS0; Q6IAG6; Q9CPX2; Q9NZF2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 07-JUN-2004, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=Ubiquitin-fold modifier 1;
DE Flags: Precursor;
GN Name=UFM1; Synonyms=C13orf20; ORFNames=BM-002;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLY-83.
RX PubMed=15071506; DOI=10.1038/sj.emboj.7600205;
RA Komatsu M., Chiba T., Tatsumi K., Iemura S., Tanida I., Okazaki N.,
RA Ueno T., Kominami E., Natsume T., Tanaka K.;
RT "A novel protein-conjugating system for Ufm1, a ubiquitin-fold
RT modifier.";
RL EMBO J. 23:1977-1986(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
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 2).
RC TISSUE=Neuroblastoma;
RX PubMed=16344560; DOI=10.1101/gr.4039406;
RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T.,
RA Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H.,
RA Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N.,
RA Yoneyama T., Otsuka R., Kanda K., Yokoi T., Kondo H., Wagatsuma M.,
RA Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T.,
RA Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.;
RT "Diversification of transcriptional modulation: large-scale
RT identification and characterization of putative alternative promoters
RT of human genes.";
RL Genome Res. 16:55-65(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-80 (ISOFORM 1).
RC TISSUE=Brain;
RA Dmitrenko V.V., Garifulin O.M., Kavsan V.M.;
RT "Characterization of different mRNA types expressed in human brain.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=20018847; DOI=10.1074/jbc.M109.036814;
RA Tatsumi K., Sou Y.S., Tada N., Nakamura E., Iemura S., Natsume T.,
RA Kang S.H., Chung C.H., Kasahara M., Kominami E., Yamamoto M.,
RA Tanaka K., Komatsu M.;
RT "A novel type of E3 ligase for the Ufm1 conjugation system.";
RL J. Biol. Chem. 285:5417-5427(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.,
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 [10]
RP STRUCTURE BY NMR.
RX PubMed=16527251; DOI=10.1016/j.bbrc.2006.02.107;
RA Sasakawa H., Sakata E., Yamaguchi Y., Komatsu M., Tatsumi K.,
RA Kominami E., Tanaka K., Kato K.;
RT "Solution structure and dynamics of Ufm1, a ubiquitin-fold modifier
RT 1.";
RL Biochem. Biophys. Res. Commun. 343:21-26(2006).
CC -!- FUNCTION: Ubiquitin-like modifier protein which binds to a number
CC of target proteins, such as DDRGK1.
CC -!- INTERACTION:
CC Q96JB5:CDK5RAP3; NbExp=1; IntAct=EBI-1045061, EBI-718818;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly
CC nuclear. Also expressed diffusely in the cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61960-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61960-2; Sequence=VSP_041186;
CC -!- SIMILARITY: Belongs to the UFM1 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB154404; BAD15373.1; -; mRNA.
DR EMBL; AF208844; AAF64258.1; -; mRNA.
DR EMBL; CR457189; CAG33470.1; -; mRNA.
DR EMBL; DA664581; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL356863; CAH70411.1; -; Genomic_DNA.
DR EMBL; AL356863; CAH70414.1; -; Genomic_DNA.
DR EMBL; BC005193; AAH05193.1; -; mRNA.
DR EMBL; Z70222; CAA94181.1; -; mRNA.
DR RefSeq; NP_057701.1; NM_016617.3.
DR UniGene; Hs.643655; -.
DR PDB; 1WXS; NMR; -; A=1-85.
DR PDBsum; 1WXS; -.
DR ProteinModelPortal; P61960; -.
DR SMR; P61960; 1-85.
DR IntAct; P61960; 6.
DR MINT; MINT-7005139; -.
DR STRING; 9606.ENSP00000239878; -.
DR PhosphoSite; P61960; -.
DR DMDM; 48428799; -.
DR PaxDb; P61960; -.
DR PRIDE; P61960; -.
DR DNASU; 51569; -.
DR Ensembl; ENST00000239878; ENSP00000239878; ENSG00000120686.
DR Ensembl; ENST00000379641; ENSP00000368962; ENSG00000120686.
DR Ensembl; ENST00000379649; ENSP00000368970; ENSG00000120686.
DR GeneID; 51569; -.
DR KEGG; hsa:51569; -.
DR UCSC; uc001uwu.3; human.
DR CTD; 51569; -.
DR GeneCards; GC13P038923; -.
DR HGNC; HGNC:20597; UFM1.
DR HPA; HPA039758; -.
DR MIM; 610553; gene.
DR neXtProt; NX_P61960; -.
DR PharmGKB; PA134863405; -.
DR eggNOG; NOG249065; -.
DR HOGENOM; HOG000238677; -.
DR HOVERGEN; HBG094129; -.
DR KO; K12162; -.
DR OMA; VTFKIIL; -.
DR OrthoDB; EOG7Q8CQW; -.
DR PhylomeDB; P61960; -.
DR ChiTaRS; UFM1; human.
DR EvolutionaryTrace; P61960; -.
DR GeneWiki; UFM1; -.
DR GenomeRNAi; 51569; -.
DR NextBio; 55392; -.
DR PRO; PR:P61960; -.
DR Bgee; P61960; -.
DR CleanEx; HS_UFM1; -.
DR Genevestigator; P61960; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071569; P:protein ufmylation; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:MGI.
DR InterPro; IPR005375; UFM1.
DR Pfam; PF03671; Ufm1; 1.
DR PIRSF; PIRSF038027; Ubiquitin-like_Ufm1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1 83 Ubiquitin-fold modifier 1.
FT /FTId=PRO_0000042122.
FT PROPEP 84 85 Removed in mature form.
FT /FTId=PRO_0000042123.
FT CROSSLNK 83 83 Glycyl lysine isopeptide (Gly-Lys)
FT (interchain with K-? in acceptor
FT proteins) (Potential).
FT VAR_SEQ 1 20 MSKVSFKITLTSDPRLPYKV -> MIRAFPTTTPRSLHLFT
FT SSTFLARALPGAFPTGACEER (in isoform 2).
FT /FTId=VSP_041186.
FT MUTAGEN 83 83 G->A: Confers resistance to cleavage.
FT CONFLICT 12 12 S -> W (in Ref. 7; CAA94181).
FT CONFLICT 78 80 PRD -> LEI (in Ref. 7; CAA94181).
FT STRAND 4 11
FT STRAND 14 16
FT STRAND 20 23
FT STRAND 25 28
FT HELIX 29 39
FT STRAND 44 53
FT HELIX 63 69
FT STRAND 72 79
SQ SEQUENCE 85 AA; 9118 MW; EDB2412E5E5836D8 CRC64;
MSKVSFKITL TSDPRLPYKV LSVPESTPFT AVLKFAAEEF KVPAATSAII TNDGIGINPA
QTAGNVFLKH GSELRIIPRD RVGSC
//
MIM
610553
*RECORD*
*FIELD* NO
610553
*FIELD* TI
*610553 UBIQUITIN-FOLD MODIFIER 1; UFM1
*FIELD* TX
DESCRIPTION
UFM1 is a ubiquitin-like protein that is conjugated to target proteins
read moreby E1-like activating enzyme UBA5 (UBE1DC1; 610552) and E2-like
conjugating enzyme UFC1 (610554) in a manner analogous to ubiquitylation
(see UBE2M; 603173) (Komatsu et al., 2004).
CLONING
Using coimmunoprecipitation with FLAG-tagged ubiquitin-like activating
enzyme UBE1DC1 expressed in HEK293 cells, Komatsu et al. (2004) purified
fragments of proteins physically associated with UBE1DC1. By database
analysis with these fragments followed by PCR of human liver cDNA, they
cloned UFM1 and UFC1. The deduced 85-amino acid UFM1 protein has a
predicted molecular mass of 9.1 kD and shares no overall sequence
identity to ubiquitin or other modifiers; however, UFM1 and ubiquitin
(UBB; 191339) share highly similar predicted tertiary structures.
Western blot analysis of mouse tissues with anti-UFM1 serum detected
expression of mouse Ufm1 protein in all tissues examined, including
brain, heart, lung, liver, and kidney. Immunocytochemistry of HeLa cells
using anti-UFM1 serum showed predominant distribution of UFM1 in the
nucleus, with diffuse staining in the cytoplasm. Immunoreactivity within
the nucleus localized as dot-like structures that may represent UFM1
conjugates.
GENE FUNCTION
Using Myc-tagged UFM1 coexpressed with FLAG-tagged UBE1DC1, FLAG-tagged
UFC1, and mutant constructs, as well as in vitro UFM1 conjugation
assays, Komatsu et al. (2004) showed that UFM1 is a ubiquitin-like
protein that is activated by the E1-like enzyme UBE1DC1 by formation of
a thioester bond and conjugated by the E2-like enzyme UFC1 with a
similar thioester linkage. Using FLAG- and His-tagged UFM1 constructs in
HEK293 followed by purification and analysis of protein complexes
formed, Komatsu et al. (2004) showed that UFM1 is conjugated to target
proteins in cells by a covalent linkage, possibly via an isopeptide bond
between the C-terminal gly83 of UFM1 and a lysine residue in the target
protein.
*FIELD* RF
1. Komatsu, M.; Chiba, T.; Tatsumi, K.; Iemura, S.; Tanida, I.; Okazaki,
N.; Ueno, T.; Kominami, E.; Natsume, T.; Tanaka, K.: A novel protein-conjugating
system for Ufm1, a ubiquitin-fold modifier. EMBO J. 23: 1977-1986,
2004.
*FIELD* CD
Dorothy S. Reilly: 11/7/2006
*FIELD* ED
wwang: 12/17/2008
carol: 11/7/2006
*RECORD*
*FIELD* NO
610553
*FIELD* TI
*610553 UBIQUITIN-FOLD MODIFIER 1; UFM1
*FIELD* TX
DESCRIPTION
UFM1 is a ubiquitin-like protein that is conjugated to target proteins
read moreby E1-like activating enzyme UBA5 (UBE1DC1; 610552) and E2-like
conjugating enzyme UFC1 (610554) in a manner analogous to ubiquitylation
(see UBE2M; 603173) (Komatsu et al., 2004).
CLONING
Using coimmunoprecipitation with FLAG-tagged ubiquitin-like activating
enzyme UBE1DC1 expressed in HEK293 cells, Komatsu et al. (2004) purified
fragments of proteins physically associated with UBE1DC1. By database
analysis with these fragments followed by PCR of human liver cDNA, they
cloned UFM1 and UFC1. The deduced 85-amino acid UFM1 protein has a
predicted molecular mass of 9.1 kD and shares no overall sequence
identity to ubiquitin or other modifiers; however, UFM1 and ubiquitin
(UBB; 191339) share highly similar predicted tertiary structures.
Western blot analysis of mouse tissues with anti-UFM1 serum detected
expression of mouse Ufm1 protein in all tissues examined, including
brain, heart, lung, liver, and kidney. Immunocytochemistry of HeLa cells
using anti-UFM1 serum showed predominant distribution of UFM1 in the
nucleus, with diffuse staining in the cytoplasm. Immunoreactivity within
the nucleus localized as dot-like structures that may represent UFM1
conjugates.
GENE FUNCTION
Using Myc-tagged UFM1 coexpressed with FLAG-tagged UBE1DC1, FLAG-tagged
UFC1, and mutant constructs, as well as in vitro UFM1 conjugation
assays, Komatsu et al. (2004) showed that UFM1 is a ubiquitin-like
protein that is activated by the E1-like enzyme UBE1DC1 by formation of
a thioester bond and conjugated by the E2-like enzyme UFC1 with a
similar thioester linkage. Using FLAG- and His-tagged UFM1 constructs in
HEK293 followed by purification and analysis of protein complexes
formed, Komatsu et al. (2004) showed that UFM1 is conjugated to target
proteins in cells by a covalent linkage, possibly via an isopeptide bond
between the C-terminal gly83 of UFM1 and a lysine residue in the target
protein.
*FIELD* RF
1. Komatsu, M.; Chiba, T.; Tatsumi, K.; Iemura, S.; Tanida, I.; Okazaki,
N.; Ueno, T.; Kominami, E.; Natsume, T.; Tanaka, K.: A novel protein-conjugating
system for Ufm1, a ubiquitin-fold modifier. EMBO J. 23: 1977-1986,
2004.
*FIELD* CD
Dorothy S. Reilly: 11/7/2006
*FIELD* ED
wwang: 12/17/2008
carol: 11/7/2006