SP7_HUMAN
ID SP7_HUMAN Reviewed; 431 AA.
AC Q8TDD2; B3KY26; Q3MJ72; Q7Z718;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Transcription factor Sp7;
DE AltName: Full=Zinc finger protein osterix;
GN Name=SP7; Synonyms=OSX;
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] (ISOFORM 1).
RX PubMed=11792318; DOI=10.1016/s0092-8674(01)00622-5;
RA Nakashima K., Zhou X., Kunkel G., Zhang Z., Deng J.M., Behringer R.R.,
RA de Crombrugghe B.;
RT "The novel zinc finger-containing transcription factor osterix is required
RT for osteoblast differentiation and bone formation.";
RL Cell 108:17-29(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14604442; DOI=10.1186/1471-2164-4-43;
RA Milona M.-A., Gough J.E., Edgar A.J.;
RT "Expression of alternatively spliced isoforms of human Sp7 in osteoblast-
RT like cells.";
RL BMC Genomics 4:43-43(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Osteosarcoma;
RX PubMed=15474293; DOI=10.1016/j.gene.2004.05.026;
RA Gao Y., Jheon A., Nourkeyhani H., Kobayashi H., Ganss B.;
RT "Molecular cloning, structure, expression, and chromosomal localization of
RT the human Osterix (SP7) gene.";
RL Gene 341:101-110(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INVOLVEMENT IN OI12.
RX PubMed=20579626; DOI=10.1016/j.ajhg.2010.05.016;
RA Lapunzina P., Aglan M., Temtamy S., Caparros-Martin J.A., Valencia M.,
RA Leton R., Martinez-Glez V., Elhossini R., Amr K., Vilaboa N.,
RA Ruiz-Perez V.L.;
RT "Identification of a frameshift mutation in Osterix in a patient with
RT recessive osteogenesis imperfecta.";
RL Am. J. Hum. Genet. 87:110-114(2010).
RN [9]
RP FUNCTION, UBIQUITINATION AT LYS-58 AND LYS-230, AND MUTAGENESIS OF LYS-58
RP AND LYS-230.
RX PubMed=23457570; DOI=10.1371/journal.pone.0056451;
RA Peng Y., Shi K., Wang L., Lu J., Li H., Pan S., Ma C.;
RT "Characterization of Osterix protein stability and physiological role in
RT osteoblast differentiation.";
RL PLoS ONE 8:E56451-E56451(2013).
RN [10]
RP 9AATAD MOTIF.
RX PubMed=31375868; DOI=10.1007/s00018-019-03251-w;
RA Piskacek M., Havelka M., Jendruchova K., Knight A., Keegan L.P.;
RT "The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with
RT valines and intron reservoirs.";
RL Cell. Mol. Life Sci. 77:1793-1810(2020).
CC -!- FUNCTION: Transcriptional activator essential for osteoblast
CC differentiation (PubMed:23457570). Binds to SP1 and EKLF consensus
CC sequences and to other G/C-rich sequences (By similarity).
CC {ECO:0000250|UniProtKB:Q8VI67, ECO:0000269|PubMed:23457570}.
CC -!- SUBUNIT: Interacts with RIOX1; the interaction is direct and inhibits
CC transcription activator activity. {ECO:0000250|UniProtKB:Q8VI67}.
CC -!- INTERACTION:
CC Q8TDD2; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-10713842, EBI-11986315;
CC Q8TDD2; O95995: GAS8; NbExp=3; IntAct=EBI-10713842, EBI-1052570;
CC Q8TDD2; P47897: QARS1; NbExp=5; IntAct=EBI-10713842, EBI-347462;
CC Q8TDD2; Q9BVG3: TRIM62; NbExp=5; IntAct=EBI-10713842, EBI-6929619;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8VI67}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=alpha, long;
CC IsoId=Q8TDD2-1; Sequence=Displayed;
CC Name=2; Synonyms=beta, short;
CC IsoId=Q8TDD2-2; Sequence=VSP_047639;
CC -!- TISSUE SPECIFICITY: Restricted to bone-derived cell.
CC {ECO:0000269|PubMed:15474293}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:31375868}.
CC -!- PTM: Ubiquitination at leads to proteasomal degradation. SP7 is a
CC short-live protein with an endogenous half-life of approximately 12
CC hours. {ECO:0000269|PubMed:23457570}.
CC -!- PTM: Propionylated. Depropionylation at Lys-371 by SIRT7 activates
CC transcription factor activity and positively regulates bone formation
CC by osteoblasts. {ECO:0000250|UniProtKB:Q8VI67}.
CC -!- DISEASE: Osteogenesis imperfecta 12 (OI12) [MIM:613849]: A form of
CC osteogenesis imperfecta, a connective tissue disorder characterized by
CC low bone mass, bone fragility and susceptibility to fractures after
CC minimal trauma. Disease severity ranges from very mild forms without
CC fractures to intrauterine fractures and perinatal lethality.
CC Extraskeletal manifestations, which affect a variable number of
CC patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI12 is an autosomal recessive form characterized by recurrent
CC fractures, mild bone deformations, generalized osteoporosis, delayed
CC teeth eruption, no dentinogenesis imperfecta, normal hearing, and white
CC sclerae. {ECO:0000269|PubMed:20579626}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Generally expressed at much higher level
CC than isoform 1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF466179; AAO33377.1; -; mRNA.
DR EMBL; AY150673; AAN85556.1; -; mRNA.
DR EMBL; AY150674; AAN85557.1; -; mRNA.
DR EMBL; AF477981; AAL84281.1; -; mRNA.
DR EMBL; AK128520; BAG54688.1; -; mRNA.
DR EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW96695.1; -; Genomic_DNA.
DR EMBL; CH471054; EAW96697.1; -; Genomic_DNA.
DR EMBL; BC101549; AAI01550.1; -; mRNA.
DR EMBL; BC113613; AAI13614.1; -; mRNA.
DR CCDS; CCDS44897.1; -. [Q8TDD2-1]
DR CCDS; CCDS73475.1; -. [Q8TDD2-2]
DR RefSeq; NP_001166938.1; NM_001173467.2. [Q8TDD2-1]
DR RefSeq; NP_001287766.1; NM_001300837.1. [Q8TDD2-2]
DR RefSeq; NP_690599.1; NM_152860.1. [Q8TDD2-1]
DR RefSeq; XP_011536202.1; XM_011537900.2. [Q8TDD2-2]
DR AlphaFoldDB; Q8TDD2; -.
DR SMR; Q8TDD2; -.
DR BioGRID; 125723; 297.
DR IntAct; Q8TDD2; 286.
DR MINT; Q8TDD2; -.
DR STRING; 9606.ENSP00000443827; -.
DR iPTMnet; Q8TDD2; -.
DR PhosphoSitePlus; Q8TDD2; -.
DR BioMuta; SP7; -.
DR DMDM; 30913318; -.
DR MassIVE; Q8TDD2; -.
DR MaxQB; Q8TDD2; -.
DR PaxDb; Q8TDD2; -.
DR PeptideAtlas; Q8TDD2; -.
DR PRIDE; Q8TDD2; -.
DR ProteomicsDB; 69477; -.
DR ProteomicsDB; 74269; -. [Q8TDD2-1]
DR Antibodypedia; 3133; 181 antibodies from 33 providers.
DR DNASU; 121340; -.
DR Ensembl; ENST00000303846.3; ENSP00000302812.3; ENSG00000170374.6. [Q8TDD2-1]
DR Ensembl; ENST00000536324.4; ENSP00000443827.2; ENSG00000170374.6. [Q8TDD2-1]
DR Ensembl; ENST00000537210.2; ENSP00000441367.2; ENSG00000170374.6. [Q8TDD2-2]
DR GeneID; 121340; -.
DR KEGG; hsa:121340; -.
DR MANE-Select; ENST00000536324.4; ENSP00000443827.2; NM_001173467.3; NP_001166938.1.
DR UCSC; uc001sct.4; human. [Q8TDD2-1]
DR CTD; 121340; -.
DR DisGeNET; 121340; -.
DR GeneCards; SP7; -.
DR HGNC; HGNC:17321; SP7.
DR HPA; ENSG00000170374; Not detected.
DR MalaCards; SP7; -.
DR MIM; 606633; gene.
DR MIM; 613849; phenotype.
DR neXtProt; NX_Q8TDD2; -.
DR OpenTargets; ENSG00000170374; -.
DR Orphanet; 216820; Osteogenesis imperfecta type 4.
DR PharmGKB; PA134917046; -.
DR VEuPathDB; HostDB:ENSG00000170374; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161293; -.
DR HOGENOM; CLU_019484_4_2_1; -.
DR InParanoid; Q8TDD2; -.
DR OMA; PTRSSCD; -.
DR OrthoDB; 664813at2759; -.
DR PhylomeDB; Q8TDD2; -.
DR TreeFam; TF350150; -.
DR PathwayCommons; Q8TDD2; -.
DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR SignaLink; Q8TDD2; -.
DR SIGNOR; Q8TDD2; -.
DR BioGRID-ORCS; 121340; 16 hits in 1091 CRISPR screens.
DR GeneWiki; Sp7_transcription_factor; -.
DR GenomeRNAi; 121340; -.
DR Pharos; Q8TDD2; Tbio.
DR PRO; PR:Q8TDD2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8TDD2; protein.
DR Bgee; ENSG00000170374; Expressed in tibia and 30 other tissues.
DR ExpressionAtlas; Q8TDD2; baseline and differential.
DR Genevisible; Q8TDD2; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISS:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; ISS:BHF-UCL.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0071529; P:cementum mineralization; IEA:Ensembl.
DR GO; GO:0071344; P:diphosphate metabolic process; IEA:Ensembl.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IDA:BHF-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:BHF-UCL.
DR GO; GO:2000738; P:positive regulation of stem cell differentiation; IDA:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0051336; P:regulation of hydrolase activity; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Osteogenesis imperfecta; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..431
FT /note="Transcription factor Sp7"
FT /id="PRO_0000047150"
FT ZN_FING 294..318
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 324..348
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 354..376
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 30..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 156..164
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:31375868"
FT COMPBIAS 186..218
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="N6-propionyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI67"
FT MOD_RES 45
FT /note="N6-propionyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI67"
FT MOD_RES 361
FT /note="N6-propionyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI67"
FT MOD_RES 371
FT /note="N6-propionyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VI67"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23457570"
FT CROSSLNK 230
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:23457570"
FT VAR_SEQ 1..18
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14604442"
FT /id="VSP_047639"
FT MUTAGEN 58
FT /note="K->R: Enhances osteogenic differentiation in C2C12
FT cells."
FT /evidence="ECO:0000269|PubMed:23457570"
FT MUTAGEN 230
FT /note="K->R: Enhances osteogenic differentiation in C2C12
FT cells."
FT /evidence="ECO:0000269|PubMed:23457570"
SQ SEQUENCE 431 AA; 44994 MW; 454A6FEA84309FF9 CRC64;
MASSLLEEEV HYGSSPLAML TAACSKFGGS SPLRDSTTLG KAGTKKPYSV GSDLSASKTM
GDAYPAPFTS TNGLLSPAGS PPAPTSGYAN DYPPFSHSFP GPTGTQDPGL LVPKGHSSSD
CLPSVYTSLD MTHPYGSWYK AGIHAGISPG PGNTPTPWWD MHPGGNWLGG GQGQGDGLQG
TLPTGPAQPP LNPQLPTYPS DFAPLNPAPY PAPHLLQPGP QHVLPQDVYK PKAVGNSGQL
EGSGGAKPPR GASTGGSGGY GGSGAGRSSC DCPNCQELER LGAAAAGLRK KPIHSCHIPG
CGKVYGKASH LKAHLRWHTG ERPFVCNWLF CGKRFTRSDE LERHVRTHTR EKKFTCLLCS
KRFTRSDHLS KHQRTHGEPG PGPPPSGPKE LGEGRSTGEE EASQTPRPSA SPATPEKAPG
GSPEQSNLLE I
