Full text data of URM1
URM1
(C9orf74)
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin-related modifier 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-related modifier 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BTM9
ID URM1_HUMAN Reviewed; 101 AA.
AC Q9BTM9; B3KMH3; B4DV08; Q5T4B4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=Ubiquitin-related modifier 1;
GN Name=URM1; Synonyms=C9orf74;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Small intestine;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [5]
RP FUNCTION IN 2-THIOLATION OF TRNA, IDENTIFICATION IN A COMPLEX WITH
RP CTU1 AND C16ORF84, AND THIOCARBOXYLATION AT GLY-101.
RX PubMed=19017811; DOI=10.1073/pnas.0808756105;
RA Schlieker C.D., Van der Veen A.G., Damon J.R., Spooner E.,
RA Ploegh H.L.;
RT "A functional proteomics approach links the ubiquitin-related modifier
RT Urm1 to a tRNA modification pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18255-18260(2008).
RN [6]
RP FUNCTION IN PROTEIN CONJUGATION, AND IDENTIFICATION OF SUBSTRATES.
RX PubMed=21209336; DOI=10.1073/pnas.1014402108;
RA Van der Veen A.G., Schorpp K., Schlieker C., Buti L., Damon J.R.,
RA Spooner E., Ploegh H.L., Jentsch S.;
RT "Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-
RT directed protein modifier.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1763-1770(2011).
CC -!- FUNCTION: Acts as a sulfur carrier required for 2-thiolation of
CC mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys),
CC tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-
CC thiolation reaction by being thiocarboxylated (-COSH) at its C-
CC terminus by MOCS3. The sulfur is then transferred to tRNA to form
CC 2-thiolation of mcm(5)S(2)U. Also acts as an ubiquitin-like
CC protein (UBL) that is covalently conjugated via an isopeptide bond
CC to lysine residues of target proteins such as MOCS3, ATPBD3, CTU2,
CC USP15 and CAS. The thiocarboxylated form serves as substrate for
CC conjugation and oxidative stress specifically induces the
CC formation of UBL-protein conjugates.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-
CC tRNA biosynthesis.
CC -!- SUBUNIT: Component of a complex at least composed of URM1,
CC CTU2/NCS2 and CTU1/ATPBD3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BTM9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTM9-2; Sequence=VSP_040026;
CC -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first
CC acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3,
CC then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
CC -!- SIMILARITY: Belongs to the URM1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI13492.1; Type=Erroneous gene model prediction;
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; AK001880; BAG50985.1; -; mRNA.
DR EMBL; AK300877; BAG62520.1; -; mRNA.
DR EMBL; AL359091; CAI13492.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL359091; CAI13493.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87782.1; -; Genomic_DNA.
DR EMBL; BC003581; AAH03581.1; -; mRNA.
DR RefSeq; NP_001129419.1; NM_001135947.2.
DR RefSeq; NP_112176.1; NM_030914.3.
DR UniGene; Hs.495229; -.
DR ProteinModelPortal; Q9BTM9; -.
DR SMR; Q9BTM9; 1-101.
DR DIP; DIP-48631N; -.
DR IntAct; Q9BTM9; 4.
DR MINT; MINT-1401016; -.
DR STRING; 9606.ENSP00000412922; -.
DR DMDM; 68565265; -.
DR PaxDb; Q9BTM9; -.
DR PRIDE; Q9BTM9; -.
DR Ensembl; ENST00000372853; ENSP00000361944; ENSG00000167118.
DR Ensembl; ENST00000452446; ENSP00000412922; ENSG00000167118.
DR GeneID; 81605; -.
DR KEGG; hsa:81605; -.
DR UCSC; uc004buv.3; human.
DR CTD; 81605; -.
DR GeneCards; GC09P131133; -.
DR HGNC; HGNC:28378; URM1.
DR MIM; 612693; gene.
DR neXtProt; NX_Q9BTM9; -.
DR PharmGKB; PA162408677; -.
DR eggNOG; NOG282764; -.
DR HOGENOM; HOG000280990; -.
DR HOVERGEN; HBG059837; -.
DR InParanoid; Q9BTM9; -.
DR KO; K12161; -.
DR OMA; DSILFIS; -.
DR OrthoDB; EOG7DRJ5B; -.
DR PhylomeDB; Q9BTM9; -.
DR UniPathway; UPA00988; -.
DR ChiTaRS; URM1; human.
DR GenomeRNAi; 81605; -.
DR NextBio; 71912; -.
DR PRO; PR:Q9BTM9; -.
DR ArrayExpress; Q9BTM9; -.
DR Bgee; Q9BTM9; -.
DR CleanEx; HS_URM1; -.
DR Genevestigator; Q9BTM9; -.
DR GO; GO:0005829; C:cytosol; IC:UniProtKB.
DR GO; GO:0034227; P:tRNA thio-modification; IMP:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:UniProtKB.
DR Gene3D; 3.10.20.30; -; 1.
DR HAMAP; MF_03048; Urm1; 1; -.
DR InterPro; IPR012675; Beta-grasp_dom.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR015221; Urm1.
DR PANTHER; PTHR14986; PTHR14986; 1.
DR Pfam; PF09138; Urm1; 1.
DR PIRSF; PIRSF037379; Ubiquitin-related_modifier_1; 1.
DR SUPFAM; SSF54285; SSF54285; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Isopeptide bond;
KW Reference proteome; tRNA processing; Ubl conjugation pathway.
FT CHAIN 1 101 Ubiquitin-related modifier 1.
FT /FTId=PRO_0000089714.
FT MOD_RES 101 101 1-thioglycine.
FT CROSSLNK 101 101 Glycyl lysine isopeptide (Gly-Lys)
FT (interchain with K-? in acceptor
FT proteins) (By similarity).
FT VAR_SEQ 79 101 LGELDYQLQDQDSVLFISTLHGG -> LVSTLGDIPPPAPA
FT LAASVGKRWASPQAHIEWLGNPPPHSSPTLRLLESPTPGEE
FT GMGSWGHGSTPPS (in isoform 2).
FT /FTId=VSP_040026.
SQ SEQUENCE 101 AA; 11380 MW; 8DE9B11957866155 CRC64;
MAAPLSVEVE FGGGAELLFD GIKKHRVTLP GQEEPWDIRN LLIWIKKNLL KERPELFIQG
DSVRPGILVL INDADWELLG ELDYQLQDQD SVLFISTLHG G
//
ID URM1_HUMAN Reviewed; 101 AA.
AC Q9BTM9; B3KMH3; B4DV08; Q5T4B4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 98.
DE RecName: Full=Ubiquitin-related modifier 1;
GN Name=URM1; Synonyms=C9orf74;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta, and Small intestine;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [5]
RP FUNCTION IN 2-THIOLATION OF TRNA, IDENTIFICATION IN A COMPLEX WITH
RP CTU1 AND C16ORF84, AND THIOCARBOXYLATION AT GLY-101.
RX PubMed=19017811; DOI=10.1073/pnas.0808756105;
RA Schlieker C.D., Van der Veen A.G., Damon J.R., Spooner E.,
RA Ploegh H.L.;
RT "A functional proteomics approach links the ubiquitin-related modifier
RT Urm1 to a tRNA modification pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18255-18260(2008).
RN [6]
RP FUNCTION IN PROTEIN CONJUGATION, AND IDENTIFICATION OF SUBSTRATES.
RX PubMed=21209336; DOI=10.1073/pnas.1014402108;
RA Van der Veen A.G., Schorpp K., Schlieker C., Buti L., Damon J.R.,
RA Spooner E., Ploegh H.L., Jentsch S.;
RT "Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-
RT directed protein modifier.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1763-1770(2011).
CC -!- FUNCTION: Acts as a sulfur carrier required for 2-thiolation of
CC mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys),
CC tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-
CC thiolation reaction by being thiocarboxylated (-COSH) at its C-
CC terminus by MOCS3. The sulfur is then transferred to tRNA to form
CC 2-thiolation of mcm(5)S(2)U. Also acts as an ubiquitin-like
CC protein (UBL) that is covalently conjugated via an isopeptide bond
CC to lysine residues of target proteins such as MOCS3, ATPBD3, CTU2,
CC USP15 and CAS. The thiocarboxylated form serves as substrate for
CC conjugation and oxidative stress specifically induces the
CC formation of UBL-protein conjugates.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-
CC tRNA biosynthesis.
CC -!- SUBUNIT: Component of a complex at least composed of URM1,
CC CTU2/NCS2 and CTU1/ATPBD3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BTM9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTM9-2; Sequence=VSP_040026;
CC -!- PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first
CC acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of MOCS3,
CC then thiocarboxylated (-COSH) via the rhodanese domain of MOCS3.
CC -!- SIMILARITY: Belongs to the URM1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI13492.1; Type=Erroneous gene model prediction;
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; AK001880; BAG50985.1; -; mRNA.
DR EMBL; AK300877; BAG62520.1; -; mRNA.
DR EMBL; AL359091; CAI13492.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL359091; CAI13493.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87782.1; -; Genomic_DNA.
DR EMBL; BC003581; AAH03581.1; -; mRNA.
DR RefSeq; NP_001129419.1; NM_001135947.2.
DR RefSeq; NP_112176.1; NM_030914.3.
DR UniGene; Hs.495229; -.
DR ProteinModelPortal; Q9BTM9; -.
DR SMR; Q9BTM9; 1-101.
DR DIP; DIP-48631N; -.
DR IntAct; Q9BTM9; 4.
DR MINT; MINT-1401016; -.
DR STRING; 9606.ENSP00000412922; -.
DR DMDM; 68565265; -.
DR PaxDb; Q9BTM9; -.
DR PRIDE; Q9BTM9; -.
DR Ensembl; ENST00000372853; ENSP00000361944; ENSG00000167118.
DR Ensembl; ENST00000452446; ENSP00000412922; ENSG00000167118.
DR GeneID; 81605; -.
DR KEGG; hsa:81605; -.
DR UCSC; uc004buv.3; human.
DR CTD; 81605; -.
DR GeneCards; GC09P131133; -.
DR HGNC; HGNC:28378; URM1.
DR MIM; 612693; gene.
DR neXtProt; NX_Q9BTM9; -.
DR PharmGKB; PA162408677; -.
DR eggNOG; NOG282764; -.
DR HOGENOM; HOG000280990; -.
DR HOVERGEN; HBG059837; -.
DR InParanoid; Q9BTM9; -.
DR KO; K12161; -.
DR OMA; DSILFIS; -.
DR OrthoDB; EOG7DRJ5B; -.
DR PhylomeDB; Q9BTM9; -.
DR UniPathway; UPA00988; -.
DR ChiTaRS; URM1; human.
DR GenomeRNAi; 81605; -.
DR NextBio; 71912; -.
DR PRO; PR:Q9BTM9; -.
DR ArrayExpress; Q9BTM9; -.
DR Bgee; Q9BTM9; -.
DR CleanEx; HS_URM1; -.
DR Genevestigator; Q9BTM9; -.
DR GO; GO:0005829; C:cytosol; IC:UniProtKB.
DR GO; GO:0034227; P:tRNA thio-modification; IMP:UniProtKB.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IMP:UniProtKB.
DR Gene3D; 3.10.20.30; -; 1.
DR HAMAP; MF_03048; Urm1; 1; -.
DR InterPro; IPR012675; Beta-grasp_dom.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR015221; Urm1.
DR PANTHER; PTHR14986; PTHR14986; 1.
DR Pfam; PF09138; Urm1; 1.
DR PIRSF; PIRSF037379; Ubiquitin-related_modifier_1; 1.
DR SUPFAM; SSF54285; SSF54285; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; Isopeptide bond;
KW Reference proteome; tRNA processing; Ubl conjugation pathway.
FT CHAIN 1 101 Ubiquitin-related modifier 1.
FT /FTId=PRO_0000089714.
FT MOD_RES 101 101 1-thioglycine.
FT CROSSLNK 101 101 Glycyl lysine isopeptide (Gly-Lys)
FT (interchain with K-? in acceptor
FT proteins) (By similarity).
FT VAR_SEQ 79 101 LGELDYQLQDQDSVLFISTLHGG -> LVSTLGDIPPPAPA
FT LAASVGKRWASPQAHIEWLGNPPPHSSPTLRLLESPTPGEE
FT GMGSWGHGSTPPS (in isoform 2).
FT /FTId=VSP_040026.
SQ SEQUENCE 101 AA; 11380 MW; 8DE9B11957866155 CRC64;
MAAPLSVEVE FGGGAELLFD GIKKHRVTLP GQEEPWDIRN LLIWIKKNLL KERPELFIQG
DSVRPGILVL INDADWELLG ELDYQLQDQD SVLFISTLHG G
//
MIM
612693
*RECORD*
*FIELD* NO
612693
*FIELD* TI
*612693 UBIQUITIN-RELATED MODIFIER 1, S. CEREVISIAE, HOMOLOG OF; URM1
*FIELD* TX
CLONING
read more
By searching databases for sequences similar to mouse Urm1, Singh et al.
(2005) identified human URM1. The deduced 101-amino acid protein shares
93% identity with mouse Urm1.
Schlieker et al. (2008) cloned human URM1 from a HeLa cell cDNA library.
BIOCHEMICAL FEATURES
Using nuclear magnetic resonance spectroscopy, Singh et al. (2005)
determined the solution structure of mouse Urm1. They found that Urm1
assumed a beta-grasp fold similar to those of eukaryotic ubiquitin (UBB;
191339) and the bacterial sulfur carrier proteins MoaD and ThiS.
GENE FUNCTION
Schlieker et al. (2008) showed that knockdown of URM1 via short hairpin
RNA reduced the growth rate of HeLa cells. Knockdown of URM1 in human
cell lines increased cell size, caused multinucleation, and increased
the population of cells with 4n or more chromosomes, suggesting that
URM1 is required for cytokinesis and thus for orderly cell cycle
progression. Use of a URM1-dependent suicide inhibitor with HEK293 cells
showed that URM1 interacted with ATPBD3 (612694). Biochemical analysis
revealed that the C-terminal thiocarboxylated glycine of URM1 functioned
as a sulfur carrier for the thiolation of tRNAs by ATPBD3. Knockdown of
either URM1 or ATPBD3 in HeLa cells reduced thiolation of uracil in the
anticodon region of tRNA-lys(UUU) (see TRNAK1; 189918).
MAPPING
Hartz (2009) mapped the URM1 gene to chromosome 9q34.11 based on an
alignment of the URM1 sequence (GenBank GENBANK AK001880) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 3/25/2009.
2. Schlieker, C. D.; Van der Veen, A. G.; Damon, J. R.; Spooner, E.;
Ploegh, H. L.: A functional proteomics approach links the ubiquitin-related
modifier Urm1 to a tRNA modification pathway. Proc. Nat. Acad. Sci. 105:
18255-18260, 2008.
3. Singh, S.; Tonelli, M.; Tyler, R. C.; Bahrami, A.; Lee, M. S.;
Markley, J. L.: Three-dimensional structure of the AAH26994.1 protein
from Mus musculus, a putative eukaryotic Urm1. Protein Sci. 14:
2095-2102, 2005.
*FIELD* CD
Patricia A. Hartz: 3/25/2009
*FIELD* ED
wwang: 01/29/2010
mgross: 3/25/2009
*RECORD*
*FIELD* NO
612693
*FIELD* TI
*612693 UBIQUITIN-RELATED MODIFIER 1, S. CEREVISIAE, HOMOLOG OF; URM1
*FIELD* TX
CLONING
read more
By searching databases for sequences similar to mouse Urm1, Singh et al.
(2005) identified human URM1. The deduced 101-amino acid protein shares
93% identity with mouse Urm1.
Schlieker et al. (2008) cloned human URM1 from a HeLa cell cDNA library.
BIOCHEMICAL FEATURES
Using nuclear magnetic resonance spectroscopy, Singh et al. (2005)
determined the solution structure of mouse Urm1. They found that Urm1
assumed a beta-grasp fold similar to those of eukaryotic ubiquitin (UBB;
191339) and the bacterial sulfur carrier proteins MoaD and ThiS.
GENE FUNCTION
Schlieker et al. (2008) showed that knockdown of URM1 via short hairpin
RNA reduced the growth rate of HeLa cells. Knockdown of URM1 in human
cell lines increased cell size, caused multinucleation, and increased
the population of cells with 4n or more chromosomes, suggesting that
URM1 is required for cytokinesis and thus for orderly cell cycle
progression. Use of a URM1-dependent suicide inhibitor with HEK293 cells
showed that URM1 interacted with ATPBD3 (612694). Biochemical analysis
revealed that the C-terminal thiocarboxylated glycine of URM1 functioned
as a sulfur carrier for the thiolation of tRNAs by ATPBD3. Knockdown of
either URM1 or ATPBD3 in HeLa cells reduced thiolation of uracil in the
anticodon region of tRNA-lys(UUU) (see TRNAK1; 189918).
MAPPING
Hartz (2009) mapped the URM1 gene to chromosome 9q34.11 based on an
alignment of the URM1 sequence (GenBank GENBANK AK001880) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 3/25/2009.
2. Schlieker, C. D.; Van der Veen, A. G.; Damon, J. R.; Spooner, E.;
Ploegh, H. L.: A functional proteomics approach links the ubiquitin-related
modifier Urm1 to a tRNA modification pathway. Proc. Nat. Acad. Sci. 105:
18255-18260, 2008.
3. Singh, S.; Tonelli, M.; Tyler, R. C.; Bahrami, A.; Lee, M. S.;
Markley, J. L.: Three-dimensional structure of the AAH26994.1 protein
from Mus musculus, a putative eukaryotic Urm1. Protein Sci. 14:
2095-2102, 2005.
*FIELD* CD
Patricia A. Hartz: 3/25/2009
*FIELD* ED
wwang: 01/29/2010
mgross: 3/25/2009