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Structural maintenance of chromosomes flexible hinge domain-containing protein 1

 SMHD1_MOUSE             Reviewed;        2007 AA.
Q6P5D8; Q6PDM8; Q6PE93; Q6ZQ78; Q811H3; Q8BP09; Q9D4M7;
29-APR-2008, integrated into UniProtKB/Swiss-Prot.
29-APR-2008, sequence version 2.
25-OCT-2017, entry version 104.
RecName: Full=Structural maintenance of chromosomes flexible hinge domain-containing protein 1;
Name=Smchd1; Synonyms=Kiaa0650;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-272 AND 1116-2007.
STRAIN=C57BL/6J; TISSUE=Muellerian duct;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 660-2007.
STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, Eye, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 942-2007.
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[5]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=18425126; DOI=10.1038/ng.142;
Blewitt M.E., Gendrel A.V., Pang Z., Sparrow D.B., Whitelaw N.,
Craig J.M., Apedaile A., Hilton D.J., Dunwoodie S.L., Brockdorff N.,
Kay G.F., Whitelaw E.;
"SmcHD1, containing a structural-maintenance-of-chromosomes hinge
domain, has a critical role in X inactivation.";
Nat. Genet. 40:663-669(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
DISRUPTION PHENOTYPE.
PubMed=21553025; DOI=10.1007/s00412-011-0318-9;
Roberts A.R., Blewitt M.E., Youngson N.A., Whitelaw E., Chong S.;
"Reduced dosage of the modifiers of epigenetic reprogramming Dnmt1,
Dnmt3L, SmcHD1 and Foxo3a has no detectable effect on mouse telomere
length in vivo.";
Chromosoma 120:377-385(2011).
[8]
FUNCTION.
PubMed=22841499; DOI=10.1016/j.devcel.2012.06.011;
Gendrel A.V., Apedaile A., Coker H., Termanis A., Zvetkova I.,
Godwin J., Tang Y.A., Huntley D., Montana G., Taylor S.,
Giannoulatou E., Heard E., Stancheva I., Brockdorff N.;
"Smchd1-dependent and -independent pathways determine developmental
dynamics of CpG island methylation on the inactive X chromosome.";
Dev. Cell 23:265-279(2012).
[9]
SUMOYLATION WITH SUMO1.
PubMed=23213215; DOI=10.1073/pnas.1215366110;
Tirard M., Hsiao H.H., Nikolov M., Urlaub H., Melchior F., Brose N.;
"In vivo localization and identification of SUMOylated proteins in the
brain of His6-HA-SUMO1 knock-in mice.";
Proc. Natl. Acad. Sci. U.S.A. 109:21122-21127(2012).
[10]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-1803, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[11]
SUBUNIT, REGION, AND DOMAIN.
PubMed=27059856; DOI=10.1042/BCJ20160189;
Chen K., Dobson R.C., Lucet I.S., Young S.N., Pearce F.G.,
Blewitt M.E., Murphy J.M.;
"The epigenetic regulator Smchd1 contains a functional GHKL-type
ATPase domain.";
Biochem. J. 473:1733-1744(2016).
[12]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=28067911; DOI=10.1038/ng.3765;
Gordon C.T., Xue S., Yigit G., Filali H., Chen K., Rosin N.,
Yoshiura K.I., Oufadem M., Beck T.J., McGowan R., Magee A.C.,
Altmueller J., Dion C., Thiele H., Gurzau A.D., Nuernberg P.,
Meschede D., Muehlbauer W., Okamoto N., Varghese V., Irving R.,
Sigaudy S., Williams D., Ahmed S.F., Bonnard C., Kong M.K., Ratbi I.,
Fejjal N., Fikri M., Elalaoui S.C., Reigstad H., Bole-Feysot C.,
Nitschke P., Ragge N., Levy N., Tuncbilek G., Teo A.S.,
Cunningham M.L., Sefiani A., Kayserili H., Murphy J.M.,
Chatdokmaiprai C., Hillmer A.M., Wattanasirichaigoon D., Lyonnet S.,
Magdinier F., Javed A., Blewitt M.E., Amiel J., Wollnik B.,
Reversade B.;
"De novo mutations in SMCHD1 cause Bosma arhinia microphthalmia
syndrome and abrogate nasal development.";
Nat. Genet. 49:249-255(2017).
-!- FUNCTION: Required for maintenance of X inactivation in females
and hypermethylation of CpG islands associated with inactive X.
Involved in a pathway that mediates the methylation of a subset of
CpG islands slowly and requires the methyltransferase DNMT3B
(PubMed:18425126, PubMed:22841499). May be required for DUX4
silencing in somatic cells (By similarity). The protein contains
an N-terminal ATPase activity domain probably necessary for its
engagement with chromatin. {ECO:0000250|UniProtKB:A6NHR9,
ECO:0000269|PubMed:18425126, ECO:0000269|PubMed:22841499}.
-!- SUBUNIT: Active as a monomer. {ECO:0000269|PubMed:27059856}.
-!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:18425126}.
-!- TISSUE SPECIFICITY: During embryogenesis, specifically expressed
in immature olfactory sensory neurons.
{ECO:0000269|PubMed:28067911}.
-!- DEVELOPMENTAL STAGE: Expressed in the nasal placodes and optic
vesicles at day 9.5 dpc and in the nasal epithelium at 12.5 dpc.
Expressed in the nasal cavity in 14.5 dpc animals.
{ECO:0000269|PubMed:28067911}.
-!- DOMAIN: The ATPase activity domain is probably necessary for its
engagement with chromatin (PubMed:27059856).
{ECO:0000269|PubMed:27059856}.
-!- PTM: Sumoylated with SUMO1. {ECO:0000269|PubMed:23213215}.
-!- DISRUPTION PHENOTYPE: Defects in Smchd1 are the cause of the
MommeD1 (modifier of murine metastable epialleles) phenotype, a
semi-dominant suppressor of variegation. Mice display female-
specific mid-gestation lethality and hypomethylation of the X-
linked gene Hprt1, due to defects in X inactivation. Mice do not
show defects on telomeres length. {ECO:0000269|PubMed:18425126,
ECO:0000269|PubMed:21553025}.
-!- SEQUENCE CAUTION:
Sequence=AAH44905.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB30222.1; Type=Frameshift; Positions=1122; Evidence={ECO:0000305};
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EMBL; AC107664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC126942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK016419; BAB30222.1; ALT_FRAME; mRNA.
EMBL; AK078494; BAC37307.1; -; mRNA.
EMBL; BC044905; AAH44905.1; ALT_INIT; mRNA.
EMBL; BC058205; AAH58205.1; -; mRNA.
EMBL; BC058618; AAH58618.1; -; mRNA.
EMBL; BC062946; AAH62946.1; -; mRNA.
EMBL; AK129181; BAC97991.1; -; mRNA.
CCDS; CCDS28958.2; -.
RefSeq; NP_083163.3; NM_028887.3.
UniGene; Mm.194450; -.
BioGrid; 216686; 20.
IntAct; Q6P5D8; 20.
MINT; MINT-4127034; -.
STRING; 10090.ENSMUSP00000121835; -.
iPTMnet; Q6P5D8; -.
PhosphoSitePlus; Q6P5D8; -.
EPD; Q6P5D8; -.
MaxQB; Q6P5D8; -.
PaxDb; Q6P5D8; -.
PeptideAtlas; Q6P5D8; -.
PRIDE; Q6P5D8; -.
Ensembl; ENSMUST00000127430; ENSMUSP00000121835; ENSMUSG00000024054.
GeneID; 74355; -.
KEGG; mmu:74355; -.
UCSC; uc008dmh.2; mouse.
CTD; 23347; -.
MGI; MGI:1921605; Smchd1.
eggNOG; ENOG410IISP; Eukaryota.
eggNOG; ENOG410XRY2; LUCA.
GeneTree; ENSGT00390000006950; -.
HOVERGEN; HBG108493; -.
InParanoid; Q6P5D8; -.
OMA; LMILPDP; -.
OrthoDB; EOG091G05DG; -.
PhylomeDB; Q6P5D8; -.
TreeFam; TF329426; -.
ChiTaRS; Smchd1; mouse.
PRO; PR:Q6P5D8; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024054; -.
Genevisible; Q6P5D8; MM.
GO; GO:0001740; C:Barr body; IDA:MGI.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0051276; P:chromosome organization; IEA:InterPro.
GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; IMP:MGI.
GO; GO:0060821; P:inactivation of X chromosome by DNA methylation; IMP:MGI.
GO; GO:0043584; P:nose development; ISS:UniProtKB.
CDD; cd00075; HATPase_c; 1.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR010935; SMC_hinge.
InterPro; IPR036277; SMC_hinge_sf.
Pfam; PF06470; SMC_hinge; 1.
SMART; SM00968; SMC_hinge; 1.
SUPFAM; SSF55874; SSF55874; 1.
SUPFAM; SSF75553; SSF75553; 1.
1: Evidence at protein level;
Acetylation; Chromosome; Complete proteome; Isopeptide bond;
Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:A6NHR9}.
CHAIN 2 2007 Structural maintenance of chromosomes
flexible hinge domain-containing protein
1.
/FTId=PRO_0000332145.
REGION 111 702 ATPase activity domain.
{ECO:0000269|PubMed:27059856}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:A6NHR9}.
MOD_RES 833 833 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1350 1350 N6-acetyllysine.
{ECO:0000250|UniProtKB:A6NHR9}.
MOD_RES 1500 1500 Phosphothreonine.
{ECO:0000250|UniProtKB:A6NHR9}.
MOD_RES 1803 1803 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1975 1975 Phosphoserine.
{ECO:0000250|UniProtKB:A6NHR9}.
CROSSLNK 1375 1375 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:A6NHR9}.
CONFLICT 1120 1120 K -> E (in Ref. 1; BAB30222).
{ECO:0000305}.
CONFLICT 1611 1611 P -> S (in Ref. 4; BAC97991).
{ECO:0000305}.
SEQUENCE 2007 AA; 225648 MW; 1A41FC47C54B5415 CRC64;
MAAEGASDPA GLSEGSGRDG AVDGCRTVYL FDRRGKDSEL GDRALQVSEH ADYAGFRASV
CQTIGISSEE KFVITTTSRK EITCNNFDHT VKDGVTLYLL QSVDQSLLTA TKERIDFLPH
YDTLVKSGMY EYYASEGQNP LPFALAELID NSLSATSRNN GVRRIQIKLL FDETQGKPAV
AVVDNGRGMT SKQLNNWAVY RLSKFTRQGD FESDHSGYVR PLPVPRSLNS DISYFGVGGK
QAVFFVGQSA RMISKPIDSK DVHELVLSKE DFEKKEKNKE AIYSGYIRNR KPADSAHITN
DDERFLHNLI EEEKEKDSFT AVVITGVQPE HIQYLKNYLH LWTRQLTHIY HYYIHGPKGN
EISTAKAIGP FNNIDIEISL FEKGKTPKII NLREIQDDMQ TLYINTASDS FEFKAHVEGD
GVVEGVIRYH PFLYDRETFP DDPCFPSKLK DEDDDDDCFI SEKAARGKRP IFECFWNGRL
IPYTSVGDFD WCAPPKKRGL VPIECFNRIS GALFTNDKFQ VSTNKLTFMD LELKLKDKNT
LFTRILNGQE QRMKIDREFA LWLKDCHEKH DKQIKFTLFK GIITRPDLPT KKQGPWATFS
AIEWDGKIYK AGQLVKTIKT LPLCYGSIVR FFLHGDHDGE VYATGGEVQI AMEPQALYDE
IKTVPIAKLD RTVAEKTIRK YVEDEMARLP DRLSVTWPEG DELLPNEVRP AGTPIGALRI
EILNKKGEAM QKLPGTSHGG SKKLLVELKV ILHTSSGNKE IISHISQHGG KWPYWFKKME
NIQKLGNYTL KLQVVLNESN ADTYAGRSLP SKVIKFSVKE GKPEKFSFGL LDSPFRVGVP
FNIPLELQDE FGHTTQLLSD IEPVLEASGL SLHYEGITKG PNCVIQGVVA KGPVNSCQGK
NFNLKVILPG LKEDSQILKI RLLPGPPHQL KVKPDSEVLV IENGTAFPFQ VEVVDESDNI
TAQPKLIVHC KFLGAPNLPV YTVDCSSSGT SILTGSPIQV QNIKKDQKTL TARIEIPSCK
DVSPVEKTIK LLPSSHAACL QIFSVEEQKA IQIKHQDEVT WVAGDVIRNL IFQMYDEGER
EINITPSLAE KIKVNWTPEV NKEHLVQGLL PDVQVPTSVK DVRYCHVSFQ DDHVCLESAF
TVRPLPDDPK HLKCELKGGK TVQMGQELQG EIVVIIADQY GNQISSFSPD SLSTLSITGD
GLDSSNLKIT LEANSQSVSV QGIRFTPGPP GPKDLCFTWR EFSDFLRVQL VSGPPTKLLL
MDWPELKESI PVINGRQLEN PLIVQLCDQW DNPALVPNVK ICLIKASSLR LLPSNQQHKT
DDKGRANLGV FTVCAPRGEH TVQVKGVYNK STIEGPTIKL TILPDPEKPI RLNVKYDQDA
SFIAGDIFTD FMVSVISESG SVIKNINPTR ISMKMWKLSS GMSRPPANAE TFSCNKIKGN
DKEDGCFYFR EKTIPNKVGA YCIQFDFMID KTNILSSQQV IVDVLPNQPM KLVPDSQPAT
PAVSNVRSIA SRTLVKDLRL SITDNYGNHT GMDLVGTVVA TIKGFNEEDT DTPLFIGKVR
TLEFPFVKGS AEITTLVLAE NSPGRDSTEY FIIFEPRLST VSGTLESYSL PFMFYNDVKK
QQQMAALTKE KDELSKSITM YRSLFDANKQ LVDEMKCQAE EAKLKETQLR NELKAYNIDI
PATQQTTHIE ALLEKKITEQ NELKKRPRRL CTLPNYTKRS GDILGKIAHL AQIEDDRAAM
VISWHLASDM DCVVTLTTDA ARAIYDETQG RQQVLPLDSI YRKTLPDWKR PLPHFRNGKL
HFKPFGNPVF ARDLLTFPDN IEHCETVFGM LLGDTIILDN LDAANHYRKE VVKITHCPTL
LTRDGDRIRS NGKFGGLQNK APPMDKLRGM VFGAPVPKQC VVLGKQIDLI QQYRTALYRL
SSVNEDLDNQ LQYLHTPDMK KKKQELDEQE KSLKRIEQKL GMTPVRRCNE SLCHSPKIEV
TECPIPTKRM RRESTRQNRR PKGDVPN


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Genprice Inc, Invoices and accounting
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