UBL7_HUMAN
ID UBL7_HUMAN Reviewed; 380 AA.
AC Q96S82; D3DW57; Q96I03;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 169.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Cao X.;
RT "Cloning and identification of a novel ubiquitin-like protein, BMSC-UbP,
RT 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
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., Lin D.H.,
RA Hu H.Y.;
RT "Solution structure of the ubiquitin-associated domain of human BMSC-UbP
RT and its complex with ubiquitin.";
RL Protein Sci. 15:1248-1259(2006).
CC -!- SUBUNIT: Binds ubiquitin. {ECO:0000269|PubMed:16731964}.
CC -!- INTERACTION:
CC Q96S82; O43747-2: AP1G1; NbExp=6; IntAct=EBI-348604, EBI-10185819;
CC Q96S82; Q7Z479: CAPN7; NbExp=3; IntAct=EBI-348604, EBI-10213454;
CC Q96S82; P07992: ERCC1; NbExp=4; IntAct=EBI-348604, EBI-750962;
CC Q96S82; P07992-3: ERCC1; NbExp=3; IntAct=EBI-348604, EBI-12699417;
CC Q96S82; P62508-3: ESRRG; NbExp=3; IntAct=EBI-348604, EBI-12001340;
CC Q96S82; P28702-3: RXRB; NbExp=3; IntAct=EBI-348604, EBI-16429492;
CC Q96S82; P61758: VBP1; NbExp=7; IntAct=EBI-348604, EBI-357430;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, skeletal
CC muscle, testis, thyroid and adrenal gland.
CC {ECO:0000269|PubMed:12644319}.
CC -!- INDUCTION: Down-regulated by phorbol myristate acetate (PMA) in bone
CC marrow stroma cells.
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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 CCDS; CCDS10263.1; -.
DR RefSeq; NP_001273668.1; NM_001286739.1.
DR RefSeq; NP_001273669.1; NM_001286740.1.
DR RefSeq; NP_001273670.1; NM_001286741.1.
DR RefSeq; NP_001273671.1; NM_001286742.1.
DR RefSeq; NP_116296.1; NM_032907.4.
DR RefSeq; NP_957717.1; NM_201265.1.
DR PDB; 2CWB; NMR; -; A=336-380.
DR PDB; 2DEN; NMR; -; A=336-380.
DR PDBsum; 2CWB; -.
DR PDBsum; 2DEN; -.
DR AlphaFoldDB; Q96S82; -.
DR SMR; Q96S82; -.
DR BioGRID; 124418; 60.
DR IntAct; Q96S82; 22.
DR MINT; Q96S82; -.
DR STRING; 9606.ENSP00000457703; -.
DR GlyGen; Q96S82; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96S82; -.
DR MetOSite; Q96S82; -.
DR PhosphoSitePlus; Q96S82; -.
DR BioMuta; UBL7; -.
DR DMDM; 48474599; -.
DR EPD; Q96S82; -.
DR jPOST; Q96S82; -.
DR MassIVE; Q96S82; -.
DR MaxQB; Q96S82; -.
DR PaxDb; Q96S82; -.
DR PeptideAtlas; Q96S82; -.
DR PRIDE; Q96S82; -.
DR ProteomicsDB; 78083; -.
DR Antibodypedia; 26955; 125 antibodies from 23 providers.
DR DNASU; 84993; -.
DR Ensembl; ENST00000361351.8; ENSP00000354883.4; ENSG00000138629.16.
DR Ensembl; ENST00000395081.7; ENSP00000378518.2; ENSG00000138629.16.
DR Ensembl; ENST00000564488.5; ENSP00000454828.1; ENSG00000138629.16.
DR Ensembl; ENST00000565335.5; ENSP00000457708.1; ENSG00000138629.16.
DR Ensembl; ENST00000567435.5; ENSP00000457703.1; ENSG00000138629.16.
DR Ensembl; ENST00000673054.1; ENSP00000500520.1; ENSG00000288408.1.
DR Ensembl; ENST00000673073.1; ENSP00000500266.1; ENSG00000288408.1.
DR Ensembl; ENST00000673120.1; ENSP00000500882.1; ENSG00000288408.1.
DR Ensembl; ENST00000673153.1; ENSP00000500164.1; ENSG00000288408.1.
DR Ensembl; ENST00000673461.1; ENSP00000500442.1; ENSG00000288408.1.
DR GeneID; 84993; -.
DR KEGG; hsa:84993; -.
DR MANE-Select; ENST00000395081.7; ENSP00000378518.2; NM_032907.5; NP_116296.1.
DR UCSC; uc002axw.3; human.
DR CTD; 84993; -.
DR DisGeNET; 84993; -.
DR GeneCards; UBL7; -.
DR HGNC; HGNC:28221; UBL7.
DR HPA; ENSG00000138629; Low tissue specificity.
DR MIM; 609748; gene.
DR neXtProt; NX_Q96S82; -.
DR OpenTargets; ENSG00000138629; -.
DR PharmGKB; PA142670645; -.
DR VEuPathDB; HostDB:ENSG00000138629; -.
DR eggNOG; KOG0010; Eukaryota.
DR GeneTree; ENSGT00390000015967; -.
DR HOGENOM; CLU_036815_2_0_1; -.
DR InParanoid; Q96S82; -.
DR OMA; HAINLLM; -.
DR OrthoDB; 975164at2759; -.
DR PhylomeDB; Q96S82; -.
DR TreeFam; TF327176; -.
DR PathwayCommons; Q96S82; -.
DR SignaLink; Q96S82; -.
DR BioGRID-ORCS; 84993; 15 hits in 1080 CRISPR screens.
DR ChiTaRS; UBL7; human.
DR EvolutionaryTrace; Q96S82; -.
DR GenomeRNAi; 84993; -.
DR Pharos; Q96S82; Tdark.
DR PRO; PR:Q96S82; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q96S82; protein.
DR Bgee; ENSG00000138629; Expressed in primary visual cortex and 99 other tissues.
DR ExpressionAtlas; Q96S82; baseline and differential.
DR Genevisible; Q96S82; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0033554; P:cellular response to stress; IEA:UniProt.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IEA:UniProt.
DR GO; GO:0030162; P:regulation of proteolysis; IEA:UniProt.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..380
FT /note="Ubiquitin-like protein 7"
FT /id="PRO_0000211021"
FT DOMAIN 18..98
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 333..377
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 200..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CONFLICT 262
FT /note="A -> V (in Ref. 1; AAK67643)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="L -> R (in Ref. 1; AAK67643)"
FT /evidence="ECO:0000305"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:2CWB"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:2CWB"
FT HELIX 353..363
FT /evidence="ECO:0007829|PDB:2CWB"
FT HELIX 367..376
FT /evidence="ECO:0007829|PDB:2CWB"
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
