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Q8NDV3

- SMC1B_HUMAN

UniProt

Q8NDV3 - SMC1B_HUMAN

Protein

Structural maintenance of chromosomes protein 1B

Gene

SMC1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (04 Jan 2005)
      Previous versions | rss
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    Functioni

    Meiosis-specific component of cohesin complex. Required for the maintenance of meiotic cohesion, but not, or only to a minor extent, for its establishment. Contributes to axial element (AE) formation and the organization of chromatin loops along the AE. Plays a key role in synapsis, recombination and chromosome movements. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi32 – 398ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: Ensembl

    GO - Biological processi

    1. meiotic nuclear division Source: UniProtKB-KW
    2. sister chromatid cohesion Source: Ensembl

    Keywords - Biological processi

    Cell cycle, Meiosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_75792. Meiotic synapsis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Structural maintenance of chromosomes protein 1B
    Short name:
    SMC protein 1B
    Short name:
    SMC-1-beta
    Short name:
    SMC-1B
    Gene namesi
    Name:SMC1B
    Synonyms:SMC1L2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:11112. SMC1B.

    Subcellular locationi

    Nucleus. Chromosome By similarity. Chromosomecentromere By similarity
    Note: Associates with chromatin. In prophase I stage of meiosis, localizes along the AE of synaptonemal complexes. In late-pachytene-diplotene, the bulk of protein dissociates from the chromosome arms probably because of phosphorylation by PLK, except at centromeres, where cohesin complexes remain. Remains chromatin associated at the centromeres up to metaphase II. At anaphase II, dissociates from centromeres, allowing chromosomes segregation By similarity.By similarity

    GO - Cellular componenti

    1. chromosome, centromeric region Source: UniProtKB-SubCell
    2. lateral element Source: Ensembl
    3. meiotic cohesin complex Source: UniProtKB
    4. nuclear meiotic cohesin complex Source: Ensembl

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35962.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12351235Structural maintenance of chromosomes protein 1BPRO_0000118993Add
    BLAST

    Proteomic databases

    MaxQBiQ8NDV3.
    PaxDbiQ8NDV3.
    PRIDEiQ8NDV3.

    PTM databases

    PhosphoSiteiQ8NDV3.

    Expressioni

    Gene expression databases

    BgeeiQ8NDV3.
    CleanExiHS_SMC1B.
    GenevestigatoriQ8NDV3.

    Organism-specific databases

    HPAiHPA001500.

    Interactioni

    Subunit structurei

    Forms a heterodimer with SMC3. Component of a meiosis-specific cohesin complex, probably composed of the SMC1B and SMC3 heterodimer attached via their hinge domain, RAD21 (or its meiosis-specific related protein REC8), which link them, and STAG3, which interacts with RAD21 or REC8 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi118018. 1 interaction.
    STRINGi9606.ENSP00000350036.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8NDV3.
    SMRiQ8NDV3. Positions 3-188, 499-675, 1021-1219.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni491 – 665175Flexible hingeAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili156 – 490335Sequence AnalysisAdd
    BLAST
    Coiled coili666 – 934269Sequence AnalysisAdd
    BLAST
    Coiled coili970 – 99425Sequence AnalysisAdd
    BLAST
    Coiled coili1022 – 104928Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1124 – 115936Ala/Asp-rich (DA-box)Add
    BLAST

    Domaini

    The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of SMC3, forming a V-shaped heterodimer. The two heads of the heterodimer are then connected by different ends of the cleavable RAD21 or REC8 protein, forming a ring structure By similarity.By similarity

    Sequence similaritiesi

    Belongs to the SMC family. SMC1 subfamily.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG1196.
    HOVERGENiHBG039593.
    KOiK06636.
    OMAiQLYHNEK.
    OrthoDBiEOG7K3TK5.
    PhylomeDBiQ8NDV3.
    TreeFamiTF101156.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    InterProiIPR027417. P-loop_NTPase.
    IPR003395. RecF/RecN/SMC_N.
    IPR024704. SMC.
    IPR010935. SMC_hinge.
    [Graphical view]
    PfamiPF06470. SMC_hinge. 1 hit.
    PF02463. SMC_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005719. SMC. 1 hit.
    SMARTiSM00968. SMC_hinge. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 4 hits.
    SSF75553. SSF75553. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8NDV3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAHLELLLVE NFKSWRGRQV IGPFRRFTCI IGPNGSGKSN VMDALSFVMG     50
    EKIANLRVKN IQELIHGAHI GKPISSSASV KIIYVEESGE EKTFARIIRG 100
    GCSEFRFNDN LVSRSVYIAE LEKIGIIVKA QNCLVFQGTV ESISVKKPKE 150
    RTQFFEEIST SGELIGEYEE KKRKLQKAEE DAQFNFNKKK NIAAERRQAK 200
    LEKEEAERYQ SLLEELKMNK IQLQLFQLYH NEKKIHLLNT KLEHVNRDLS 250
    VKRESLSHHE NIVKARKKEH GMLTRQLQQT EKELKSVETL LNQKRPQYIK 300
    AKENTSHHLK KLDVAKKSIK DSEKQCSKQE DDIKALETEL ADLDAAWRSF 350
    EKQIEEEILH KKRDIELEAS QLDRYKELKE QVRKKVATMT QQLEKLQWEQ 400
    KTDEERLAFE KRRHGEVQGN LKQIKEQIED HKKRIEKLEE YTKTCMDCLK 450
    EKKQQEETLV DEIEKTKSRM SEFNEELNLI RSELQNAGID THEGKRQQKR 500
    AEVLEHLKRL YPDSVFGRLF DLCHPIHKKY QLAVTKVFGR FITAIVVASE 550
    KVAKDCIRFL KEERAEPETF LALDYLDIKP INERLRELKG CKMVIDVIKT 600
    QFPQLKKVIQ FVCGNGLVCE TMEEARHIAL SGPERQKTVA LDGTLFLKSG 650
    VISGGSSDLK YKARCWDEKE LKNLRDRRSQ KIQELKGLMK TLRKETDLKQ 700
    IQTLIQGTQT RLKYSQNELE MIKKKHLVAF YQEQSQLQSE LLNIESQCIM 750
    LSEGIKERQR RIKEFQEKID KVEDDIFQHF CEEIGVENIR EFENKHVKRQ 800
    QEIDQKRYFY KKMLTRLNVQ LEYSRSHLKK KLNKINTLKE TIQKGSEDID 850
    HLKKAEENCL QTVNELMAKQ QQLKDIRVTQ NSSAEKVQTQ IEEERKKFLA 900
    VDREVGKLQK EVVSIQTSLE QKRLEKHNLL LDCKVQDIEI ILLSGSLDDI 950
    IEVEMGTEAE STQATIDIYE KEEAFEIDYS SLKEDLKALQ SDQEIEAHLR 1000
    LLLQQVASQE DILLKTAAPN LRALENLKTV RDKFQESTDA FEASRKEARL 1050
    CRQEFEQVKK RRYDLFTQCF EHVSISIDQI YKKLCRNNSA QAFLSPENPE 1100
    EPYLEGISYN CVAPGKRFMP MDNLSGGEKC VAALALLFAV HSFRPAPFFV 1150
    LDEVDAALDN TNIGKVSSYI KEQTQDQFQM IVISLKEEFY SRADALIGIY 1200
    PEYDDCMFSR VLTLDLSQYP DTEGQESSKR HGESR 1235
    Length:1,235
    Mass (Da):143,908
    Last modified:January 4, 2005 - v2
    Checksum:iA06223197817017F
    GO
    Isoform 2 (identifier: Q8NDV3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         808-814: YFYKKML → LEFEKQK
         1092-1165: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,161
    Mass (Da):135,838
    Checksum:iAE2578854CC1A3BE
    GO
    Isoform 3 (identifier: Q8NDV3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         808-814: YFYKKML → LEFEKQK

    Note: No experimental confirmation available.

    Show »
    Length:1,235
    Mass (Da):143,837
    Checksum:iBF22F243CA070B15
    GO

    Sequence cautioni

    The sequence BAC86266.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti99 – 991R → L in CAD43404. (PubMed:14660695)Curated
    Sequence conflicti731 – 7311Y → D in BAC86266. (PubMed:14702039)Curated
    Sequence conflicti752 – 7521S → G in BAC86266. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti473 – 4731F → V.1 Publication
    Corresponds to variant rs136603 [ dbSNP | Ensembl ].
    VAR_045913
    Natural varianti758 – 7581R → Q.
    Corresponds to variant rs9614653 [ dbSNP | Ensembl ].
    VAR_057324
    Natural varianti1008 – 10081S → A.
    Corresponds to variant rs16993928 [ dbSNP | Ensembl ].
    VAR_057325
    Natural varianti1050 – 10501L → M.2 Publications
    Corresponds to variant rs5764698 [ dbSNP | Ensembl ].
    VAR_045914

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei808 – 8147YFYKKML → LEFEKQK in isoform 2 and isoform 3. 2 PublicationsVSP_035027
    Alternative sequencei1092 – 116574Missing in isoform 2. 1 PublicationVSP_035028Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ504806 mRNA. Translation: CAD43404.2.
    AL008718, AL021391 Genomic DNA. Translation: CAQ08671.1.
    AL008718, AL021391 Genomic DNA. Translation: CAQ08672.1.
    BC126208 mRNA. Translation: AAI26209.1.
    AK125736 mRNA. Translation: BAC86266.1. Different initiation.
    CCDSiCCDS43027.1. [Q8NDV3-3]
    RefSeqiNP_001278430.1. NM_001291501.1.
    NP_683515.4. NM_148674.4.
    UniGeneiHs.334176.

    Genome annotation databases

    EnsembliENST00000357450; ENSP00000350036; ENSG00000077935. [Q8NDV3-3]
    ENST00000404354; ENSP00000385902; ENSG00000077935. [Q8NDV3-2]
    GeneIDi27127.
    KEGGihsa:27127.
    UCSCiuc003bgc.3. human. [Q8NDV3-3]
    uc003bgd.3. human. [Q8NDV3-2]

    Polymorphism databases

    DMDMi57015410.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ504806 mRNA. Translation: CAD43404.2 .
    AL008718 , AL021391 Genomic DNA. Translation: CAQ08671.1 .
    AL008718 , AL021391 Genomic DNA. Translation: CAQ08672.1 .
    BC126208 mRNA. Translation: AAI26209.1 .
    AK125736 mRNA. Translation: BAC86266.1 . Different initiation.
    CCDSi CCDS43027.1. [Q8NDV3-3 ]
    RefSeqi NP_001278430.1. NM_001291501.1.
    NP_683515.4. NM_148674.4.
    UniGenei Hs.334176.

    3D structure databases

    ProteinModelPortali Q8NDV3.
    SMRi Q8NDV3. Positions 3-188, 499-675, 1021-1219.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118018. 1 interaction.
    STRINGi 9606.ENSP00000350036.

    PTM databases

    PhosphoSitei Q8NDV3.

    Polymorphism databases

    DMDMi 57015410.

    Proteomic databases

    MaxQBi Q8NDV3.
    PaxDbi Q8NDV3.
    PRIDEi Q8NDV3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000357450 ; ENSP00000350036 ; ENSG00000077935 . [Q8NDV3-3 ]
    ENST00000404354 ; ENSP00000385902 ; ENSG00000077935 . [Q8NDV3-2 ]
    GeneIDi 27127.
    KEGGi hsa:27127.
    UCSCi uc003bgc.3. human. [Q8NDV3-3 ]
    uc003bgd.3. human. [Q8NDV3-2 ]

    Organism-specific databases

    GeneCardsi GC22M045739.
    H-InvDB HIX0027884.
    HGNCi HGNC:11112. SMC1B.
    HPAi HPA001500.
    MIMi 608685. gene.
    neXtProti NX_Q8NDV3.
    PharmGKBi PA35962.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1196.
    HOVERGENi HBG039593.
    KOi K06636.
    OMAi QLYHNEK.
    OrthoDBi EOG7K3TK5.
    PhylomeDBi Q8NDV3.
    TreeFami TF101156.

    Enzyme and pathway databases

    Reactomei REACT_75792. Meiotic synapsis.

    Miscellaneous databases

    GeneWikii SMC1B.
    GenomeRNAii 27127.
    NextBioi 49836.
    PROi Q8NDV3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8NDV3.
    CleanExi HS_SMC1B.
    Genevestigatori Q8NDV3.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    InterProi IPR027417. P-loop_NTPase.
    IPR003395. RecF/RecN/SMC_N.
    IPR024704. SMC.
    IPR010935. SMC_hinge.
    [Graphical view ]
    Pfami PF06470. SMC_hinge. 1 hit.
    PF02463. SMC_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005719. SMC. 1 hit.
    SMARTi SM00968. SMC_hinge. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 4 hits.
    SSF75553. SSF75553. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The evolution of SMC proteins: phylogenetic analysis and structural implications."
      Cobbe N., Heck M.M.S.
      Mol. Biol. Evol. 21:332-347(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS VAL-473 AND MET-1050.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 731-1235 (ISOFORM 3), VARIANT MET-1050.
      Tissue: Testis.

    Entry informationi

    Entry nameiSMC1B_HUMAN
    AccessioniPrimary (citable) accession number: Q8NDV3
    Secondary accession number(s): A0AV46
    , B0QY23, B0QY24, Q5TIC3, Q6ZUF9, Q9Y3G5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 25, 2003
    Last sequence update: January 4, 2005
    Last modified: October 1, 2014
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3