Full text data of UBL7
UBL7
(BMSCUBP)
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin-like protein 7 (Bone marrow stromal cell ubiquitin-like protein; BMSC-UbP; Ubiquitin-like protein SB132)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-like protein 7 (Bone marrow stromal cell ubiquitin-like protein; BMSC-UbP; Ubiquitin-like protein SB132)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q96S82
ID UBL7_HUMAN Reviewed; 380 AA.
AC Q96S82; D3DW57; Q96I03;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-MAR-2004, sequence version 2.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Ubiquitin-like protein 7;
DE AltName: Full=Bone marrow stromal cell ubiquitin-like protein;
DE Short=BMSC-UbP;
DE AltName: Full=Ubiquitin-like protein SB132;
GN Name=UBL7; Synonyms=BMSCUBP; ORFNames=SB132;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow stroma;
RX PubMed=12644319; DOI=10.1016/S0165-2478(03)00004-X;
RA Liu S., Yu Y., An H., Li N., Lin N., Wang W., Zhang W., Wan T.,
RA Cao X.;
RT "Cloning and identification of a novel ubiquitin-like protein, BMSC-
RT UbP, from human bone marrow stromal cells.";
RL Immunol. Lett. 86:169-175(2003).
RN [2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Muscle, and Uterus;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASS
RP 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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 [11]
RP STRUCTURE BY NMR OF 292-380 IN COMPLEX WITH UBIQUITIN.
RX PubMed=16731964; DOI=10.1110/ps.051995006;
RA Chang Y.G., Song A.X., Gao Y.G., Shi Y.H., Lin X.J., Cao X.T.,
RA Lin D.H., Hu H.Y.;
RT "Solution structure of the ubiquitin-associated domain of human BMSC-
RT UbP and its complex with ubiquitin.";
RL Protein Sci. 15:1248-1259(2006).
CC -!- SUBUNIT: Binds ubiquitin.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart,
CC skeletal muscle, testis, thyroid and adrenal gland.
CC -!- INDUCTION: Down-regulated by phorbol myristate acetate (PMA) in
CC bone marrow stroma cells.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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; AY037166; AAK67643.1; -; mRNA.
DR EMBL; CH471136; EAW99332.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99335.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99339.1; -; Genomic_DNA.
DR EMBL; BC007913; AAH07913.1; -; mRNA.
DR EMBL; BC030055; AAH30055.1; -; mRNA.
DR EMBL; BC033919; AAH33919.1; -; mRNA.
DR RefSeq; NP_116296.1; NM_032907.4.
DR RefSeq; NP_957717.1; NM_201265.1.
DR UniGene; Hs.334713; -.
DR PDB; 2CWB; NMR; -; A=336-380.
DR PDB; 2DEN; NMR; -; A=336-380.
DR PDBsum; 2CWB; -.
DR PDBsum; 2DEN; -.
DR ProteinModelPortal; Q96S82; -.
DR SMR; Q96S82; 5-97, 336-380.
DR IntAct; Q96S82; 6.
DR MINT; MINT-1034167; -.
DR STRING; 9606.ENSP00000354883; -.
DR PhosphoSite; Q96S82; -.
DR DMDM; 48474599; -.
DR PaxDb; Q96S82; -.
DR PRIDE; Q96S82; -.
DR DNASU; 84993; -.
DR Ensembl; ENST00000361351; ENSP00000354883; ENSG00000138629.
DR Ensembl; ENST00000395081; ENSP00000378518; ENSG00000138629.
DR Ensembl; ENST00000564488; ENSP00000454828; ENSG00000138629.
DR Ensembl; ENST00000565335; ENSP00000457708; ENSG00000138629.
DR Ensembl; ENST00000567435; ENSP00000457703; ENSG00000138629.
DR GeneID; 84993; -.
DR KEGG; hsa:84993; -.
DR UCSC; uc002axw.1; human.
DR CTD; 84993; -.
DR GeneCards; GC15M074738; -.
DR HGNC; HGNC:28221; UBL7.
DR HPA; HPA040423; -.
DR MIM; 609748; gene.
DR neXtProt; NX_Q96S82; -.
DR PharmGKB; PA142670645; -.
DR eggNOG; NOG124076; -.
DR HOVERGEN; HBG054051; -.
DR InParanoid; Q96S82; -.
DR OMA; DDFHPSA; -.
DR PhylomeDB; Q96S82; -.
DR ChiTaRS; UBL7; human.
DR EvolutionaryTrace; Q96S82; -.
DR GenomeRNAi; 84993; -.
DR NextBio; 75587; -.
DR PRO; PR:Q96S82; -.
DR ArrayExpress; Q96S82; -.
DR Bgee; Q96S82; -.
DR CleanEx; HS_UBL7; -.
DR Genevestigator; Q96S82; -.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR000449; UBA/Ts_N.
DR InterPro; IPR015496; Ubiquilin.
DR InterPro; IPR000626; Ubiquitin_dom.
DR PANTHER; PTHR10677; PTHR10677; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1 380 Ubiquitin-like protein 7.
FT /FTId=PRO_0000211021.
FT DOMAIN 18 98 Ubiquitin-like.
FT DOMAIN 333 377 UBA.
FT MOD_RES 230 230 Phosphoserine.
FT CONFLICT 262 262 A -> V (in Ref. 1; AAK67643).
FT CONFLICT 272 272 L -> R (in Ref. 1; AAK67643).
FT HELIX 339 346
FT TURN 347 349
FT HELIX 353 363
FT HELIX 367 376
SQ SEQUENCE 380 AA; 40510 MW; 0B64DF79597E0931 CRC64;
MSLSDWHLAV KLADQPLTPK SILRLPETEL GEYSLGGYSI SFLKQLIAGK LQESVPDPEL
IDLIYCGRKL KDDQTLDFYG IQPGSTVHVL RKSWPEPDQK PEPVDKVAAM REFRVLHTAL
HSSSSYREAV FKMLSNKESL DQIIVATPGL SSDPIALGVL QDKDLFSVFA DPNMLDTLVP
AHPALVNAIV LVLHSVAGSA PMPGTDSSSR SMPSSSYRDM PGGFLFEGLS DDEDDFHPNT
RSTPSSSTPS SRPASLGYSG AAGPRPITQS ELATALALAS TPESSSHTPT PGTQGHSSGT
SPMSSGVQSG TPITNDLFSQ ALQHALQASG QPSLQSQWQP QLQQLRDMGI QDDELSLRAL
QATGGDIQAA LELIFAGGAP
//
ID UBL7_HUMAN Reviewed; 380 AA.
AC Q96S82; D3DW57; Q96I03;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-MAR-2004, sequence version 2.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Ubiquitin-like protein 7;
DE AltName: Full=Bone marrow stromal cell ubiquitin-like protein;
DE Short=BMSC-UbP;
DE AltName: Full=Ubiquitin-like protein SB132;
GN Name=UBL7; Synonyms=BMSCUBP; ORFNames=SB132;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow stroma;
RX PubMed=12644319; DOI=10.1016/S0165-2478(03)00004-X;
RA Liu S., Yu Y., An H., Li N., Lin N., Wang W., Zhang W., Wan T.,
RA Cao X.;
RT "Cloning and identification of a novel ubiquitin-like protein, BMSC-
RT UbP, from human bone marrow stromal cells.";
RL Immunol. Lett. 86:169-175(2003).
RN [2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Muscle, and Uterus;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASS
RP 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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, 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 [11]
RP STRUCTURE BY NMR OF 292-380 IN COMPLEX WITH UBIQUITIN.
RX PubMed=16731964; DOI=10.1110/ps.051995006;
RA Chang Y.G., Song A.X., Gao Y.G., Shi Y.H., Lin X.J., Cao X.T.,
RA Lin D.H., Hu H.Y.;
RT "Solution structure of the ubiquitin-associated domain of human BMSC-
RT UbP and its complex with ubiquitin.";
RL Protein Sci. 15:1248-1259(2006).
CC -!- SUBUNIT: Binds ubiquitin.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart,
CC skeletal muscle, testis, thyroid and adrenal gland.
CC -!- INDUCTION: Down-regulated by phorbol myristate acetate (PMA) in
CC bone marrow stroma cells.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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; AY037166; AAK67643.1; -; mRNA.
DR EMBL; CH471136; EAW99332.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99335.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99339.1; -; Genomic_DNA.
DR EMBL; BC007913; AAH07913.1; -; mRNA.
DR EMBL; BC030055; AAH30055.1; -; mRNA.
DR EMBL; BC033919; AAH33919.1; -; mRNA.
DR RefSeq; NP_116296.1; NM_032907.4.
DR RefSeq; NP_957717.1; NM_201265.1.
DR UniGene; Hs.334713; -.
DR PDB; 2CWB; NMR; -; A=336-380.
DR PDB; 2DEN; NMR; -; A=336-380.
DR PDBsum; 2CWB; -.
DR PDBsum; 2DEN; -.
DR ProteinModelPortal; Q96S82; -.
DR SMR; Q96S82; 5-97, 336-380.
DR IntAct; Q96S82; 6.
DR MINT; MINT-1034167; -.
DR STRING; 9606.ENSP00000354883; -.
DR PhosphoSite; Q96S82; -.
DR DMDM; 48474599; -.
DR PaxDb; Q96S82; -.
DR PRIDE; Q96S82; -.
DR DNASU; 84993; -.
DR Ensembl; ENST00000361351; ENSP00000354883; ENSG00000138629.
DR Ensembl; ENST00000395081; ENSP00000378518; ENSG00000138629.
DR Ensembl; ENST00000564488; ENSP00000454828; ENSG00000138629.
DR Ensembl; ENST00000565335; ENSP00000457708; ENSG00000138629.
DR Ensembl; ENST00000567435; ENSP00000457703; ENSG00000138629.
DR GeneID; 84993; -.
DR KEGG; hsa:84993; -.
DR UCSC; uc002axw.1; human.
DR CTD; 84993; -.
DR GeneCards; GC15M074738; -.
DR HGNC; HGNC:28221; UBL7.
DR HPA; HPA040423; -.
DR MIM; 609748; gene.
DR neXtProt; NX_Q96S82; -.
DR PharmGKB; PA142670645; -.
DR eggNOG; NOG124076; -.
DR HOVERGEN; HBG054051; -.
DR InParanoid; Q96S82; -.
DR OMA; DDFHPSA; -.
DR PhylomeDB; Q96S82; -.
DR ChiTaRS; UBL7; human.
DR EvolutionaryTrace; Q96S82; -.
DR GenomeRNAi; 84993; -.
DR NextBio; 75587; -.
DR PRO; PR:Q96S82; -.
DR ArrayExpress; Q96S82; -.
DR Bgee; Q96S82; -.
DR CleanEx; HS_UBL7; -.
DR Genevestigator; Q96S82; -.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR000449; UBA/Ts_N.
DR InterPro; IPR015496; Ubiquilin.
DR InterPro; IPR000626; Ubiquitin_dom.
DR PANTHER; PTHR10677; PTHR10677; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1 380 Ubiquitin-like protein 7.
FT /FTId=PRO_0000211021.
FT DOMAIN 18 98 Ubiquitin-like.
FT DOMAIN 333 377 UBA.
FT MOD_RES 230 230 Phosphoserine.
FT CONFLICT 262 262 A -> V (in Ref. 1; AAK67643).
FT CONFLICT 272 272 L -> R (in Ref. 1; AAK67643).
FT HELIX 339 346
FT TURN 347 349
FT HELIX 353 363
FT HELIX 367 376
SQ SEQUENCE 380 AA; 40510 MW; 0B64DF79597E0931 CRC64;
MSLSDWHLAV KLADQPLTPK SILRLPETEL GEYSLGGYSI SFLKQLIAGK LQESVPDPEL
IDLIYCGRKL KDDQTLDFYG IQPGSTVHVL RKSWPEPDQK PEPVDKVAAM REFRVLHTAL
HSSSSYREAV FKMLSNKESL DQIIVATPGL SSDPIALGVL QDKDLFSVFA DPNMLDTLVP
AHPALVNAIV LVLHSVAGSA PMPGTDSSSR SMPSSSYRDM PGGFLFEGLS DDEDDFHPNT
RSTPSSSTPS SRPASLGYSG AAGPRPITQS ELATALALAS TPESSSHTPT PGTQGHSSGT
SPMSSGVQSG TPITNDLFSQ ALQHALQASG QPSLQSQWQP QLQQLRDMGI QDDELSLRAL
QATGGDIQAA LELIFAGGAP
//
MIM
609748
*RECORD*
*FIELD* NO
609748
*FIELD* TI
*609748 UBIQUITIN-LIKE 7; UBL7
*FIELD* TX
CLONING
From large-scale screening of a bone marrow stromal cell (BMSC) cDNA
read morelibrary, Liu et al. (2003) identified UBL7, a novel cDNA encoding a
deduced 380-amino acid protein with a predicted molecular mass of 40.6
kD. The protein, which they designated BMSC-UbP, contains a UBQ domain
at its N terminus and a ubiquitin-associated domain at its C terminus.
It shares moderate homology with several ubiquitin-like proteins
including UBQLN1 (605046) and UBQLN2 (300264). Northern blot analysis
revealed an approximately 1.3-kb UBL7 transcript in all human tissues
tested. RT-PCR detected expression of UBL7 in several tumor cell lines.
GENE FUNCTION
Liu et al. (2003) found that expression of UBL7 was significantly
down-regulated in PMA-stimulated BMSC but was not obviously changed in
LPS-stimulated BMSC. UBL7 expression was up-regulated in LPS-stimulated
acute promyelocytic HL60 cells but remained unchanged in PMA-stimulated
HL60 cells. Liu et al. (2003) suggested that UBL7 may play a role in the
regulation of BMSC function or cell differentiation through an evocator-
and cell-specific pattern.
MAPPING
By sequence analysis, Liu et al. (2003) mapped the UCL7 gene to
chromosome 15q22.3-q23.
*FIELD* RF
1. Liu, S.; Yu, Y.; An, H.; Li, N.; Lin, N.; Wang, W.; Zhang, W.;
Wan, T.; Cao, X.: Cloning and identification of a novel ubiquitin-like
protein, BMSC-UbP, from bone marrow stromal cells. Immun. Lett. 68:
169-175, 2003.
*FIELD* CD
Jennifer L. Goldstein: 12/1/2005
*FIELD* ED
carol: 12/01/2005
carol: 12/1/2005
*RECORD*
*FIELD* NO
609748
*FIELD* TI
*609748 UBIQUITIN-LIKE 7; UBL7
*FIELD* TX
CLONING
From large-scale screening of a bone marrow stromal cell (BMSC) cDNA
read morelibrary, Liu et al. (2003) identified UBL7, a novel cDNA encoding a
deduced 380-amino acid protein with a predicted molecular mass of 40.6
kD. The protein, which they designated BMSC-UbP, contains a UBQ domain
at its N terminus and a ubiquitin-associated domain at its C terminus.
It shares moderate homology with several ubiquitin-like proteins
including UBQLN1 (605046) and UBQLN2 (300264). Northern blot analysis
revealed an approximately 1.3-kb UBL7 transcript in all human tissues
tested. RT-PCR detected expression of UBL7 in several tumor cell lines.
GENE FUNCTION
Liu et al. (2003) found that expression of UBL7 was significantly
down-regulated in PMA-stimulated BMSC but was not obviously changed in
LPS-stimulated BMSC. UBL7 expression was up-regulated in LPS-stimulated
acute promyelocytic HL60 cells but remained unchanged in PMA-stimulated
HL60 cells. Liu et al. (2003) suggested that UBL7 may play a role in the
regulation of BMSC function or cell differentiation through an evocator-
and cell-specific pattern.
MAPPING
By sequence analysis, Liu et al. (2003) mapped the UCL7 gene to
chromosome 15q22.3-q23.
*FIELD* RF
1. Liu, S.; Yu, Y.; An, H.; Li, N.; Lin, N.; Wang, W.; Zhang, W.;
Wan, T.; Cao, X.: Cloning and identification of a novel ubiquitin-like
protein, BMSC-UbP, from bone marrow stromal cells. Immun. Lett. 68:
169-175, 2003.
*FIELD* CD
Jennifer L. Goldstein: 12/1/2005
*FIELD* ED
carol: 12/01/2005
carol: 12/1/2005