Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8NDV3 (SMC1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Structural maintenance of chromosomes protein 1B

Short name=SMC protein 1B
Short name=SMC-1-beta
Short name=SMC-1B
Gene names
Name:SMC1B
Synonyms:SMC1L2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1235 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

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.

Domain

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.

Sequence similarities

Belongs to the SMC family. SMC1 subfamily.

Sequence caution

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NDV3-1)

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.
Isoform 2 (identifier: Q8NDV3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     808-814: YFYKKML → LEFEKQK
     1092-1165: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8NDV3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     808-814: YFYKKML → LEFEKQK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12351235Structural maintenance of chromosomes protein 1B
PRO_0000118993

Regions

Nucleotide binding32 – 398ATP Potential
Region491 – 665175Flexible hinge
Coiled coil156 – 490335 Potential
Coiled coil666 – 934269 Potential
Coiled coil970 – 99425 Potential
Coiled coil1022 – 104928 Potential
Compositional bias1124 – 115936Ala/Asp-rich (DA-box)

Natural variations

Alternative sequence808 – 8147YFYKKML → LEFEKQK in isoform 2 and isoform 3.
VSP_035027
Alternative sequence1092 – 116574Missing in isoform 2.
VSP_035028
Natural variant4731F → V. Ref.3
Corresponds to variant rs136603 [ dbSNP | Ensembl ].
VAR_045913
Natural variant7581R → Q.
Corresponds to variant rs9614653 [ dbSNP | Ensembl ].
VAR_057324
Natural variant10081S → A.
Corresponds to variant rs16993928 [ dbSNP | Ensembl ].
VAR_057325
Natural variant10501L → M. Ref.3 Ref.4
Corresponds to variant rs5764698 [ dbSNP | Ensembl ].
VAR_045914

Experimental info

Sequence conflict991R → L in CAD43404. Ref.1
Sequence conflict7311Y → D in BAC86266. Ref.4
Sequence conflict7521S → G in BAC86266. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: A06223197817017F

FASTA1,235143,908
        10         20         30         40         50         60 
MAHLELLLVE NFKSWRGRQV IGPFRRFTCI IGPNGSGKSN VMDALSFVMG EKIANLRVKN 

        70         80         90        100        110        120 
IQELIHGAHI GKPISSSASV KIIYVEESGE EKTFARIIRG GCSEFRFNDN LVSRSVYIAE 

       130        140        150        160        170        180 
LEKIGIIVKA QNCLVFQGTV ESISVKKPKE RTQFFEEIST SGELIGEYEE KKRKLQKAEE 

       190        200        210        220        230        240 
DAQFNFNKKK NIAAERRQAK LEKEEAERYQ SLLEELKMNK IQLQLFQLYH NEKKIHLLNT 

       250        260        270        280        290        300 
KLEHVNRDLS VKRESLSHHE NIVKARKKEH GMLTRQLQQT EKELKSVETL LNQKRPQYIK 

       310        320        330        340        350        360 
AKENTSHHLK KLDVAKKSIK DSEKQCSKQE DDIKALETEL ADLDAAWRSF EKQIEEEILH 

       370        380        390        400        410        420 
KKRDIELEAS QLDRYKELKE QVRKKVATMT QQLEKLQWEQ KTDEERLAFE KRRHGEVQGN 

       430        440        450        460        470        480 
LKQIKEQIED HKKRIEKLEE YTKTCMDCLK EKKQQEETLV DEIEKTKSRM SEFNEELNLI 

       490        500        510        520        530        540 
RSELQNAGID THEGKRQQKR AEVLEHLKRL YPDSVFGRLF DLCHPIHKKY QLAVTKVFGR 

       550        560        570        580        590        600 
FITAIVVASE KVAKDCIRFL KEERAEPETF LALDYLDIKP INERLRELKG CKMVIDVIKT 

       610        620        630        640        650        660 
QFPQLKKVIQ FVCGNGLVCE TMEEARHIAL SGPERQKTVA LDGTLFLKSG VISGGSSDLK 

       670        680        690        700        710        720 
YKARCWDEKE LKNLRDRRSQ KIQELKGLMK TLRKETDLKQ IQTLIQGTQT RLKYSQNELE 

       730        740        750        760        770        780 
MIKKKHLVAF YQEQSQLQSE LLNIESQCIM LSEGIKERQR RIKEFQEKID KVEDDIFQHF 

       790        800        810        820        830        840 
CEEIGVENIR EFENKHVKRQ QEIDQKRYFY KKMLTRLNVQ LEYSRSHLKK KLNKINTLKE 

       850        860        870        880        890        900 
TIQKGSEDID HLKKAEENCL QTVNELMAKQ QQLKDIRVTQ NSSAEKVQTQ IEEERKKFLA 

       910        920        930        940        950        960 
VDREVGKLQK EVVSIQTSLE QKRLEKHNLL LDCKVQDIEI ILLSGSLDDI IEVEMGTEAE 

       970        980        990       1000       1010       1020 
STQATIDIYE KEEAFEIDYS SLKEDLKALQ SDQEIEAHLR LLLQQVASQE DILLKTAAPN 

      1030       1040       1050       1060       1070       1080 
LRALENLKTV RDKFQESTDA FEASRKEARL CRQEFEQVKK RRYDLFTQCF EHVSISIDQI 

      1090       1100       1110       1120       1130       1140 
YKKLCRNNSA QAFLSPENPE EPYLEGISYN CVAPGKRFMP MDNLSGGEKC VAALALLFAV 

      1150       1160       1170       1180       1190       1200 
HSFRPAPFFV LDEVDAALDN TNIGKVSSYI KEQTQDQFQM IVISLKEEFY SRADALIGIY 

      1210       1220       1230 
PEYDDCMFSR VLTLDLSQYP DTEGQESSKR HGESR 

« Hide

Isoform 2 [UniParc].

Checksum: AE2578854CC1A3BE
Show »

FASTA1,161135,838
Isoform 3 [UniParc].

Checksum: BF22F243CA070B15
Show »

FASTA1,235143,837

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_683515.3. NM_148674.3.
UniGeneHs.334176.

3D structure databases

ProteinModelPortalQ8NDV3.
SMRQ8NDV3. Positions 7-161, 499-675, 1038-1219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118018. 1 interaction.
STRING9606.ENSP00000350036.

PTM databases

PhosphoSiteQ8NDV3.

Polymorphism databases

DMDM57015410.

Proteomic databases

PaxDbQ8NDV3.
PRIDEQ8NDV3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357450; ENSP00000350036; ENSG00000077935. [Q8NDV3-3]
ENST00000404354; ENSP00000385902; ENSG00000077935. [Q8NDV3-2]
GeneID27127.
KEGGhsa:27127.
UCSCuc003bgc.3. human. [Q8NDV3-3]
uc003bgd.3. human. [Q8NDV3-2]

Organism-specific databases

CTD27127.
GeneCardsGC22M045739.
H-InvDBHIX0027884.
HGNCHGNC:11112. SMC1B.
HPAHPA001500.
MIM608685. gene.
neXtProtNX_Q8NDV3.
PharmGKBPA35962.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1196.
HOVERGENHBG039593.
KOK06636.
OMAQLYHNEK.
OrthoDBEOG7K3TK5.
PhylomeDBQ8NDV3.
TreeFamTF101156.

Enzyme and pathway databases

ReactomeREACT_111183. Meiosis.
REACT_115566. Cell Cycle.

Gene expression databases

BgeeQ8NDV3.
CleanExHS_SMC1B.
GenevestigatorQ8NDV3.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
InterProIPR027417. P-loop_NTPase.
IPR003395. RecF/RecN/SMC_N.
IPR024704. SMC.
IPR028468. Smc1.
IPR010935. SMC_hinge.
[Graphical view]
PANTHERPTHR18937:SF12. PTHR18937:SF12. 1 hit.
PfamPF06470. SMC_hinge. 1 hit.
PF02463. SMC_N. 1 hit.
[Graphical view]
PIRSFPIRSF005719. SMC. 1 hit.
SMARTSM00968. SMC_hinge. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 4 hits.
SSF75553. SSF75553. 1 hit.
ProtoNetSearch...

Other

GeneWikiSMC1B.
GenomeRNAi27127.
NextBio49836.
PROQ8NDV3.
SOURCESearch...

Entry information

Entry nameSMC1B_HUMAN
AccessionPrimary (citable) accession number: Q8NDV3
Secondary accession number(s): A0AV46 expand/collapse secondary AC list , B0QY23, B0QY24, Q5TIC3, Q6ZUF9, Q9Y3G5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: January 4, 2005
Last modified: April 16, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM