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SETD5_MOUSE
ID   SETD5_MOUSE             Reviewed;        1441 AA.
AC   Q5XJV7; Q80T94; Q8BKD5; Q8BX30;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD5 {ECO:0000305};
DE            EC=2.1.1.359 {ECO:0000269|PubMed:31515109};
DE            EC=2.1.1.367 {ECO:0000305|PubMed:22939622};
DE   AltName: Full=SET domain-containing protein 5 {ECO:0000305};
GN   Name=Setd5 {ECO:0000303|PubMed:27864380, ECO:0000312|MGI:MGI:1920145};
GN   Synonyms=Kiaa1757 {ECO:0000303|PubMed:12693553};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 245-1071.
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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-852, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-852 AND THR-855,
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70 AND SER-74 (ISOFORM 2),
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22939622; DOI=10.1016/j.cell.2012.06.048;
RA   Pinheiro I., Margueron R., Shukeir N., Eisold M., Fritzsch C.,
RA   Richter F.M., Mittler G., Genoud C., Goyama S., Kurokawa M., Son J.,
RA   Reinberg D., Lachner M., Jenuwein T.;
RT   "Prdm3 and Prdm16 are H3K9me1 methyltransferases required for mammalian
RT   heterochromatin integrity.";
RL   Cell 150:948-960(2012).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LEO1; CTR9; CDC73 AND
RP   NCOR1, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=27864380; DOI=10.1242/dev.141465;
RA   Osipovich A.B., Gangula R., Vianna P.G., Magnuson M.A.;
RT   "Setd5 is essential for mammalian development and the co-transcriptional
RT   regulation of histone acetylation.";
RL   Development 143:4595-4607(2016).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH HDAC3.
RX   PubMed=30455454; DOI=10.1038/s41593-018-0266-2;
RA   Deliu E., Arecco N., Morandell J., Dotter C.P., Contreras X., Girardot C.,
RA   Kaesper E.L., Kozlova A., Kishi K., Chiaradia I., Noh K.M., Novarino G.;
RT   "Haploinsufficiency of the intellectual disability gene SETD5 disturbs
RT   developmental gene expression and cognition.";
RL   Nat. Neurosci. 21:1717-1727(2018).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=31515109; DOI=10.1016/j.neuron.2019.07.013;
RA   Sessa A., Fagnocchi L., Mastrototaro G., Massimino L., Zaghi M.,
RA   Indrigo M., Cattaneo S., Martini D., Gabellini C., Pucci C., Fasciani A.,
RA   Belli R., Taverna S., Andreazzoli M., Zippo A., Broccoli V.;
RT   "SETD5 regulates chromatin methylation state and preserves global
RT   transcriptional fidelity during brain development and neuronal wiring.";
RL   Neuron 104:271-289(2019).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=30655503; DOI=10.1038/s41398-018-0344-y;
RA   Moore S.M., Seidman J.S., Ellegood J., Gao R., Savchenko A., Troutman T.D.,
RA   Abe Y., Stender J., Lee D., Wang S., Voytek B., Lerch J.P., Suh H.,
RA   Glass C.K., Muotri A.R.;
RT   "Setd5 haploinsufficiency alters neuronal network connectivity and leads to
RT   autistic-like behaviors in mice.";
RL   Transl. Psychiatry 9:24-24(2019).
CC   -!- FUNCTION: Chromatin regulator required for brain development: acts as a
CC       regulator of RNA elongation rate, thereby regulating neural stem cell
CC       (NSC) proliferation and synaptic transmission (PubMed:30455454,
CC       PubMed:31515109). May act by mediating trimethylation of 'Lys-36' of
CC       histone H3 (H3K36me3), which is essential to allow on-time RNA
CC       elongation dynamics (PubMed:31515109). Also monomethylates 'Lys-9' of
CC       histone H3 (H3K9me1) in vitro (PubMed:22939622). The relevance of
CC       histone methyltransferase activity is however subject to discussion
CC       (PubMed:27864380, PubMed:30455454). {ECO:0000269|PubMed:22939622,
CC       ECO:0000269|PubMed:27864380, ECO:0000269|PubMed:30455454,
CC       ECO:0000269|PubMed:31515109}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.367;
CC         Evidence={ECO:0000305|PubMed:22939622};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC         + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC         COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC         Evidence={ECO:0000269|PubMed:31515109};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60325;
CC         Evidence={ECO:0000269|PubMed:31515109};
CC   -!- SUBUNIT: Interacts with components of the PAF1 complex (PAF1C) such as
CC       LEO1, CTR9 and CDC73 (PubMed:27864380). Interacts with NCOR1
CC       (PubMed:27864380). Interacts with HDAC3 (PubMed:30455454).
CC       {ECO:0000269|PubMed:27864380, ECO:0000269|PubMed:30455454}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27864380}. Chromosome
CC       {ECO:0000269|PubMed:31515109}. Note=Localizes to active transcribed
CC       genes. {ECO:0000269|PubMed:31515109}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5XJV7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5XJV7-2; Sequence=VSP_024097;
CC       Name=3;
CC         IsoId=Q5XJV7-3; Sequence=VSP_024096;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:27864380}.
CC   -!- DISRUPTION PHENOTYPE: Mid-gestation lethality due to severe
CC       developmental delay such as vascular abnormalities in the embryo and
CC       placenta, reduced cellular proliferation and increased apoptosis
CC       (PubMed:27864380). Defects are probably due to a widespread impairment
CC       in the regulation of gene expression (PubMed:27864380). Setd5-
CC       haploinsufficient mice display altered neuronal network connectivity
CC       leading to autistic-like behaviors (PubMed:30655503, PubMed:30455454,
CC       PubMed:31515109). Haploinsufficient Setd5 cortical neurons show reduced
CC       synaptic density and neuritic outgrowtho, with corresponding decreases
CC       in network activity and synchrony by electrophysiology
CC       (PubMed:30655503). Haploinsufficient mice display several autism-like
CC       behaviors, including hyperactivity, cognitive deficit, and altered
CC       social interactions (PubMed:30455454, PubMed:31515109,
CC       PubMed:30655503). {ECO:0000269|PubMed:27864380,
CC       ECO:0000269|PubMed:30455454, ECO:0000269|PubMed:30655503,
CC       ECO:0000269|PubMed:31515109}.
CC   -!- CAUTION: According to a report, lacks histone methyltransferase
CC       activity and regulates chromatin by interacting with HDAC3 and PAF1
CC       complex (PAF1C) complex (PubMed:30455454). According to another
CC       publication, displays histone methyltransferase activity and directly
CC       trimethylates 'Lys-36' of histone H3 (H3K36me3) (PubMed:31515109).
CC       {ECO:0000269|PubMed:30455454, ECO:0000269|PubMed:31515109}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33569.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC65833.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK122551; BAC65833.1; ALT_INIT; mRNA.
DR   EMBL; AK049143; BAC33569.1; ALT_INIT; mRNA.
DR   EMBL; AK053541; BAC35420.1; -; mRNA.
DR   EMBL; BC083184; AAH83184.1; -; mRNA.
DR   CCDS; CCDS20411.1; -. [Q5XJV7-1]
DR   CCDS; CCDS90096.1; -. [Q5XJV7-2]
DR   RefSeq; NP_082661.1; NM_028385.1. [Q5XJV7-1]
DR   RefSeq; NP_766593.1; NM_173005.1. [Q5XJV7-2]
DR   RefSeq; XP_011239784.1; XM_011241482.2. [Q5XJV7-2]
DR   AlphaFoldDB; Q5XJV7; -.
DR   BioGRID; 215631; 6.
DR   IntAct; Q5XJV7; 6.
DR   STRING; 10090.ENSMUSP00000047398; -.
DR   iPTMnet; Q5XJV7; -.
DR   PhosphoSitePlus; Q5XJV7; -.
DR   EPD; Q5XJV7; -.
DR   jPOST; Q5XJV7; -.
DR   MaxQB; Q5XJV7; -.
DR   PaxDb; Q5XJV7; -.
DR   PeptideAtlas; Q5XJV7; -.
DR   PRIDE; Q5XJV7; -.
DR   ProteomicsDB; 261498; -. [Q5XJV7-1]
DR   ProteomicsDB; 261499; -. [Q5XJV7-2]
DR   ProteomicsDB; 261500; -. [Q5XJV7-3]
DR   Antibodypedia; 60053; 89 antibodies from 17 providers.
DR   DNASU; 72895; -.
DR   Ensembl; ENSMUST00000042889; ENSMUSP00000047398; ENSMUSG00000034269. [Q5XJV7-1]
DR   Ensembl; ENSMUST00000113155; ENSMUSP00000108780; ENSMUSG00000034269. [Q5XJV7-2]
DR   Ensembl; ENSMUST00000113157; ENSMUSP00000108782; ENSMUSG00000034269. [Q5XJV7-2]
DR   GeneID; 72895; -.
DR   KEGG; mmu:72895; -.
DR   UCSC; uc009deq.1; mouse. [Q5XJV7-1]
DR   UCSC; uc009der.1; mouse. [Q5XJV7-2]
DR   UCSC; uc009deu.1; mouse. [Q5XJV7-3]
DR   CTD; 55209; -.
DR   MGI; MGI:1920145; Setd5.
DR   VEuPathDB; HostDB:ENSMUSG00000034269; -.
DR   eggNOG; KOG1844; Eukaryota.
DR   GeneTree; ENSGT00940000157446; -.
DR   HOGENOM; CLU_002373_0_0_1; -.
DR   InParanoid; Q5XJV7; -.
DR   OMA; XVSLLEY; -.
DR   OrthoDB; 86638at2759; -.
DR   PhylomeDB; Q5XJV7; -.
DR   TreeFam; TF106417; -.
DR   BioGRID-ORCS; 72895; 8 hits in 79 CRISPR screens.
DR   ChiTaRS; Setd5; mouse.
DR   PRO; PR:Q5XJV7; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q5XJV7; protein.
DR   Bgee; ENSMUSG00000034269; Expressed in undifferentiated genital tubercle and 237 other tissues.
DR   Genevisible; Q5XJV7; MM.
DR   GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; IBA:GO_Central.
DR   GO; GO:0034967; C:Set3 complex; IBA:GO_Central.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IMP:UniProtKB.
DR   GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:UniProtKB.
DR   GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR   GO; GO:0097198; P:histone H3-K36 trimethylation; IMP:UniProtKB.
DR   GO; GO:1902275; P:regulation of chromatin organization; IMP:UniProtKB.
DR   GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; IMP:UniProtKB.
DR   GO; GO:0035065; P:regulation of histone acetylation; IMP:UniProtKB.
DR   GO; GO:0051963; P:regulation of synapse assembly; IMP:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   CDD; cd19181; SET_SETD5; 1.
DR   Gene3D; 2.170.270.10; -; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR044433; SETD5_SET.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF82199; SSF82199; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Chromosome; Methyltransferase;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..1441
FT                   /note="Histone-lysine N-methyltransferase SETD5"
FT                   /id="PRO_0000281906"
FT   DOMAIN          269..390
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..683
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..816
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          849..883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1036..1228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1243..1441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..180
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..497
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        498..538
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        539..555
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..683
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1066..1081
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1082..1167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1243..1416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         829
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0A6"
FT   MOD_RES         852
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         855
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9C0A6"
FT   VAR_SEQ         1..792
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_024096"
FT   VAR_SEQ         59
FT                   /note="A -> ADHNYGAPPPPTPPASPPVQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024097"
FT   CONFLICT        1381
FT                   /note="L -> F (in Ref. 3; AAH83184)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q5XJV7-2:70
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q5XJV7-2:74
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   1441 AA;  157426 MW;  67120734D6EB6DD9 CRC64;
     MSIAIPLGVT TPDTSYSDMA AGSDPESVEA SPAVNEKSVY STHNYGTTQR HGCRGLPYAT
     IIPRSDLNGL PSPVEERCGD SPNSEGETVP TWCPCGLSQD GFLLNCDKCR GMSRGKVIRL
     HRRKQDNISG GDSSATESWD EELSPSTVLY TATQHTPTSI TLTVRRTKPK KRKKSPEKGR
     AAPKTKKIKN SPSEAQNLDE NTTEGWENRI RLWTDQYEEA FTNQYSADVQ NALEQHLHSN
     KEFVGKPAIL DTINKTELAC NNTVIGSQMQ LQLGRVTRVQ KHRKILRAAR DLALDTLIIE
     YRGKVMLRQQ FEVNGHFFKK PYPFVLFYSK FNGVEMCVDA RTFGNDARFI RRSCTPNAEV
     RHMIADGMIH LCIYAVSAIT KDAEVTIAFD YEYSNCNYKV DCACHKGNRN CPIQKRNPNA
     AELPLPPPPS FPTIGAETRR RKARRKELEL EQQNEVPEEN PDPQPQEVPE KVTVSNEHEE
     VDNPEEKPEE EEKEEATDDQ ENSAHSRRTR EDRKVEAIMH AFESLEKRKK RRDQPVEQSS
     SDIEITTSSS EIVVGEETKT AAPESEVSSP VSNVAIPSTP QSTGVNTRRS SHAGDVAAEK
     PIPKPPPAKP SRPRPKSRIS RYRTSSAQRL KRQKQAIAQQ AELSQAALEE GGSNNSVTPP
     EAGNTDSSGE NRQLTGSDPT VISVTGSHVN RAASKYPKTK KYLVTEWLND KAEKQECPVE
     CPLRITTDPT VLATTLNMLP GLIHSPLICT TPKHYIRFGS PFMPERRRRP LLPDGTFSSC
     KKRWIKQALE EGMTQTSSVP QETRTQHLYQ SNETSNSSSI CKDNADLLSP LKKWKSRYLM
     EQNITKLLQP LSPVTPPPPS SGSKSPQLTT PGQTHPGEEE CRNGYSLMFS PITSLTTASR
     SNTPLQFELC HRKDLDLTKV GFPDSSTHSC ADRPSLLNCN HPDLASHPSV VPTSEAGFPS
     RSGDGPQTLL RNSDQAFRTE FNLMYAYSPL NAMPRADGLY RGSPLVGDRK PLHLDGGYCS
     PAEGFSSRYE HGFMKDLSRG SMSPGGERTC EGVPSAPQNP PQRKKVSLLE YRKRKQEAKE
     NSGGGNDSSQ SKSKSSGAGQ GSSNSVSDTG AHGVQGSSAG TPSSPHKKFS PSHSSASHLE
     AVSPSDSRGT SSSHCRPQEN ISSRWMVPTS VERLREGGSI PKVLRSSVRV AQKGEPSPTW
     ESNITEKESD PADGEGPEPL SSALSKGATV YSPSRYSYQL LQCDSPRTES QSLLQQSSSP
     FRGHPTQSPG YSYRTTALRP GNPPSHGSSE SSLSSTSYPS PAHPVSTDSL APFTGTPGYY
     SSQPHSGNST GSNLPRRSCS SSAASPTPQG PSDSPTSDSV SQSSTGTLSS TSFPQNSRSS
     LPSDLRTISL PNAGQSAAYQ ASRVSAVSNS QHYPHRGSGG VHQYRLQPLQ GSGVKTQTGL
     S
 
 
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