Gene name:
SMC1B(SMC1L2);
Protein name:
Structural maintenance of chromosomes protein 1B(SMC protein 1B;SMC-1-beta;SMC-1B);
Alternative:
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
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.
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.
Subcellular Location:
Nucleus
Chromosome
Chromosome
centromere
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.
Protein Attributes:
50:
MAHLELLLVE | NFKSWRGRQV | IGPFRRFTCI | IGPNGSGKSN | VMDALSFVMG |
100:
EKIANLRVKN | IQELIHGAHI | GKPISSSASV | KIIYVEESGE | EKTFARIIRG |
150:
GCSEFRFNDN | LVSRSVYIAE | LEKIGIIVKA | QNCLVFQGTV | ESISVKKPKE |
200:
RTQFFEEIST | SGELIGEYEE | KKRKLQKAEE | DAQFNFNKKK | NIAAERRQAK |
250:
LEKEEAERYQ | SLLEELKMNK | IQLQLFQLYH | NEKKIHLLNT | KLEHVNRDLS |
300:
VKRESLSHHE | NIVKARKKEH | GMLTRQLQQT | EKELKSVETL | LNQKRPQYIK |
350:
AKENTSHHLK | KLDVAKKSIK | DSEKQCSKQE | DDIKALETEL | ADLDAAWRSF |
400:
EKQIEEEILH | KKRDIELEAS | QLDRYKELKE | QVRKKVATMT | QQLEKLQWEQ |
450:
KTDEERLAFE | KRRHGEVQGN | LKQIKEQIED | HKKRIEKLEE | YTKTCMDCLK |
500:
EKKQQEETLV | DEIEKTKSRM | SEFNEELNLI | RSELQNAGID | THEGKRQQKR |
550:
AEVLEHLKRL | YPDSVFGRLF | DLCHPIHKKY | QLAVTKVFGR | FITAIVVASE |
600:
KVAKDCIRFL | KEERAEPETF | LALDYLDIKP | INERLRELKG | CKMVIDVIKT |
650:
QFPQLKKVIQ | FVCGNGLVCE | TMEEARHIAL | SGPERQKTVA | LDGTLFLKSG |
700:
VISGGSSDLK | YKARCWDEKE | LKNLRDRRSQ | KIQELKGLMK | TLRKETDLKQ |
750:
IQTLIQGTQT | RLKYSQNELE | MIKKKHLVAF | YQEQSQLQSE | LLNIESQCIM |
800:
LSEGIKERQR | RIKEFQEKID | KVEDDIFQHF | CEEIGVENIR | EFENKHVKRQ |
850:
QEIDQKRYFY | KKMLTRLNVQ | LEYSRSHLKK | KLNKINTLKE | TIQKGSEDID |
900:
HLKKAEENCL | QTVNELMAKQ | QQLKDIRVTQ | NSSAEKVQTQ | IEEERKKFLA |
950:
VDREVGKLQK | EVVSIQTSLE | QKRLEKHNLL | LDCKVQDIEI | ILLSGSLDDI |
1000:
IEVEMGTEAE | STQATIDIYE | KEEAFEIDYS | SLKEDLKALQ | SDQEIEAHLR |
1050:
LLLQQVASQE | DILLKTAAPN | LRALENLKTV | RDKFQESTDA | FEASRKEARL |
1100:
CRQEFEQVKK | RRYDLFTQCF | EHVSISIDQI | YKKLCRNNSA | QAFLSPENPE |
1150:
EPYLEGISYN | CVAPGKRFMP | MDNLSGGEKC | VAALALLFAV | HSFRPAPFFV |
1200:
LDEVDAALDN | TNIGKVSSYI | KEQTQDQFQM | IVISLKEEFY | SRADALIGIY |
1235:
PEYDDCMFSR | VLTLDLSQYP | DTEGQESSKR | HGESR
Vaild Sequence:
Related Databases
Uniprot:
