SMC1B_HUMAN
ID SMC1B_HUMAN Reviewed; 1235 AA.
AC Q8NDV3; A0AV46; B0QY23; B0QY24; Q5TIC3; Q6ZUF9; Q9Y3G5;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Structural maintenance of chromosomes protein 1B;
DE Short=SMC protein 1B;
DE Short=SMC-1-beta;
DE Short=SMC-1B;
GN Name=SMC1B; Synonyms=SMC1L2;
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=14660695; DOI=10.1093/molbev/msh023;
RA Cobbe N., Heck M.M.S.;
RT "The evolution of SMC proteins: phylogenetic analysis and structural
RT implications.";
RL Mol. Biol. Evol. 21:332-347(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS VAL-473
RP AND MET-1050.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 731-1235 (ISOFORM 3), AND VARIANT
RP MET-1050.
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Meiosis-specific component of cohesin complex. Required for
CC the maintenance of meiotic cohesion, but not, or only to a minor
CC extent, for its establishment. Contributes to axial element (AE)
CC formation and the organization of chromatin loops along the AE. Plays a
CC key role in synapsis, recombination and chromosome movements. The
CC cohesin complex is required for the cohesion of sister chromatids after
CC DNA replication. The cohesin complex apparently forms a large
CC proteinaceous ring within which sister chromatids can be trapped. At
CC anaphase, the complex is cleaved and dissociates from chromatin,
CC allowing sister chromatids to segregate. The meiosis-specific cohesin
CC complex probably replaces mitosis specific cohesin complex when it
CC dissociates from chromatin during prophase I (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterodimer with SMC3. Component of a meiosis-specific
CC cohesin complex, probably composed of the SMC1B and SMC3 heterodimer
CC attached via their SMC hinge domain, RAD21 (or its meiosis-specific
CC related protein REC8), which link them, and STAG3, which interacts with
CC RAD21 or REC8 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q920F6}.
CC Chromosome {ECO:0000250|UniProtKB:Q920F6}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q920F6}. Note=Associates with chromatin. In
CC prophase I stage of meiosis, localizes along the AE of synaptonemal
CC complexes. In late-pachytene-diplotene, the bulk of protein dissociates
CC from the chromosome arms probably because of phosphorylation by PLK,
CC except at centromeres, where cohesin complexes remain. Remains
CC chromatin associated at the centromeres up to metaphase II. At anaphase
CC II, dissociates from centromeres, allowing chromosomes segregation (By
CC similarity). {ECO:0000250|UniProtKB:Q920F6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NDV3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NDV3-2; Sequence=VSP_035027, VSP_035028;
CC Name=3;
CC IsoId=Q8NDV3-3; Sequence=VSP_035027;
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC3, forming a V-shaped heterodimer.
CC The two heads of the heterodimer are then connected by different ends
CC of the cleavable RAD21 or REC8 protein, forming a ring structure (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC86266.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ504806; CAD43404.2; -; mRNA.
DR EMBL; AL008718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL021391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126208; AAI26209.1; -; mRNA.
DR EMBL; AK125736; BAC86266.1; ALT_INIT; mRNA.
DR CCDS; CCDS43027.1; -. [Q8NDV3-3]
DR CCDS; CCDS74876.1; -. [Q8NDV3-2]
DR RefSeq; NP_001278430.1; NM_001291501.1.
DR RefSeq; NP_683515.4; NM_148674.4.
DR AlphaFoldDB; Q8NDV3; -.
DR SMR; Q8NDV3; -.
DR BioGRID; 118018; 9.
DR IntAct; Q8NDV3; 4.
DR STRING; 9606.ENSP00000350036; -.
DR iPTMnet; Q8NDV3; -.
DR PhosphoSitePlus; Q8NDV3; -.
DR BioMuta; SMC1B; -.
DR DMDM; 57015410; -.
DR EPD; Q8NDV3; -.
DR jPOST; Q8NDV3; -.
DR MassIVE; Q8NDV3; -.
DR MaxQB; Q8NDV3; -.
DR PaxDb; Q8NDV3; -.
DR PeptideAtlas; Q8NDV3; -.
DR PRIDE; Q8NDV3; -.
DR ProteomicsDB; 73058; -. [Q8NDV3-1]
DR ProteomicsDB; 73059; -. [Q8NDV3-2]
DR ProteomicsDB; 73060; -. [Q8NDV3-3]
DR Antibodypedia; 233; 126 antibodies from 23 providers.
DR DNASU; 27127; -.
DR Ensembl; ENST00000357450.9; ENSP00000350036.4; ENSG00000077935.17.
DR Ensembl; ENST00000404354.3; ENSP00000385902.3; ENSG00000077935.17.
DR GeneID; 27127; -.
DR KEGG; hsa:27127; -.
DR UCSC; uc003bgc.4; human. [Q8NDV3-1]
DR CTD; 27127; -.
DR DisGeNET; 27127; -.
DR GeneCards; SMC1B; -.
DR HGNC; HGNC:11112; SMC1B.
DR HPA; ENSG00000077935; Tissue enriched (testis).
DR MIM; 608685; gene.
DR neXtProt; NX_Q8NDV3; -.
DR PharmGKB; PA35962; -.
DR VEuPathDB; HostDB:ENSG00000077935; -.
DR eggNOG; KOG0018; Eukaryota.
DR HOGENOM; CLU_001042_0_2_1; -.
DR InParanoid; Q8NDV3; -.
DR OrthoDB; 326079at2759; -.
DR PhylomeDB; Q8NDV3; -.
DR TreeFam; TF101156; -.
DR PathwayCommons; Q8NDV3; -.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR SignaLink; Q8NDV3; -.
DR BioGRID-ORCS; 27127; 11 hits in 1070 CRISPR screens.
DR ChiTaRS; SMC1B; human.
DR GeneWiki; SMC1B; -.
DR GenomeRNAi; 27127; -.
DR Pharos; Q8NDV3; Tbio.
DR PRO; PR:Q8NDV3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q8NDV3; protein.
DR Bgee; ENSG00000077935; Expressed in right testis and 23 other tissues.
DR Genevisible; Q8NDV3; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000800; C:lateral element; IEA:Ensembl.
DR GO; GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR CDD; cd03275; ABC_SMC1_euk; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR028468; Smc1_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; ATP-binding; Cell cycle; Centromere;
KW Chromosome; Coiled coil; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1235
FT /note="Structural maintenance of chromosomes protein 1B"
FT /id="PRO_0000118993"
FT DOMAIN 514..629
FT /note="SMC hinge"
FT COILED 156..490
FT /evidence="ECO:0000255"
FT COILED 666..934
FT /evidence="ECO:0000255"
FT COILED 970..994
FT /evidence="ECO:0000255"
FT COILED 1022..1049
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 648
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 713
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14683"
FT MOD_RES 1033
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CU62"
FT VAR_SEQ 808..814
FT /note="YFYKKML -> LEFEKQK (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_035027"
FT VAR_SEQ 1092..1165
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035028"
FT VARIANT 473
FT /note="F -> V (in dbSNP:rs136603)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_045913"
FT VARIANT 758
FT /note="R -> Q (in dbSNP:rs9614653)"
FT /id="VAR_057324"
FT VARIANT 1008
FT /note="S -> A (in dbSNP:rs16993928)"
FT /id="VAR_057325"
FT VARIANT 1050
FT /note="L -> M (in dbSNP:rs5764698)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_045914"
FT CONFLICT 99
FT /note="R -> L (in Ref. 1; CAD43404)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="Y -> D (in Ref. 4; BAC86266)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="S -> G (in Ref. 4; BAC86266)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1235 AA; 143908 MW; A06223197817017F CRC64;
MAHLELLLVE NFKSWRGRQV IGPFRRFTCI IGPNGSGKSN VMDALSFVMG EKIANLRVKN
IQELIHGAHI GKPISSSASV KIIYVEESGE EKTFARIIRG GCSEFRFNDN LVSRSVYIAE
LEKIGIIVKA QNCLVFQGTV ESISVKKPKE RTQFFEEIST SGELIGEYEE KKRKLQKAEE
DAQFNFNKKK NIAAERRQAK LEKEEAERYQ SLLEELKMNK IQLQLFQLYH NEKKIHLLNT
KLEHVNRDLS VKRESLSHHE NIVKARKKEH GMLTRQLQQT EKELKSVETL LNQKRPQYIK
AKENTSHHLK KLDVAKKSIK DSEKQCSKQE DDIKALETEL ADLDAAWRSF EKQIEEEILH
KKRDIELEAS QLDRYKELKE QVRKKVATMT QQLEKLQWEQ KTDEERLAFE KRRHGEVQGN
LKQIKEQIED HKKRIEKLEE YTKTCMDCLK EKKQQEETLV DEIEKTKSRM SEFNEELNLI
RSELQNAGID THEGKRQQKR AEVLEHLKRL YPDSVFGRLF DLCHPIHKKY QLAVTKVFGR
FITAIVVASE KVAKDCIRFL KEERAEPETF LALDYLDIKP INERLRELKG CKMVIDVIKT
QFPQLKKVIQ FVCGNGLVCE TMEEARHIAL SGPERQKTVA LDGTLFLKSG VISGGSSDLK
YKARCWDEKE LKNLRDRRSQ KIQELKGLMK TLRKETDLKQ IQTLIQGTQT RLKYSQNELE
MIKKKHLVAF YQEQSQLQSE LLNIESQCIM LSEGIKERQR RIKEFQEKID KVEDDIFQHF
CEEIGVENIR EFENKHVKRQ QEIDQKRYFY KKMLTRLNVQ LEYSRSHLKK KLNKINTLKE
TIQKGSEDID HLKKAEENCL QTVNELMAKQ QQLKDIRVTQ NSSAEKVQTQ IEEERKKFLA
VDREVGKLQK EVVSIQTSLE QKRLEKHNLL LDCKVQDIEI ILLSGSLDDI IEVEMGTEAE
STQATIDIYE KEEAFEIDYS SLKEDLKALQ SDQEIEAHLR LLLQQVASQE DILLKTAAPN
LRALENLKTV RDKFQESTDA FEASRKEARL CRQEFEQVKK RRYDLFTQCF EHVSISIDQI
YKKLCRNNSA QAFLSPENPE EPYLEGISYN CVAPGKRFMP MDNLSGGEKC VAALALLFAV
HSFRPAPFFV LDEVDAALDN TNIGKVSSYI KEQTQDQFQM IVISLKEEFY SRADALIGIY
PEYDDCMFSR VLTLDLSQYP DTEGQESSKR HGESR
