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Structural maintenance of chromosomes protein 1A (SMC protein 1A) (SMC-1-alpha) (SMC-1A) (Chromosome segregation protein SmcB) (Sb1.8)

 SMC1A_MOUSE             Reviewed;        1233 AA.
Q9CU62; A2AFQ5; Q3V480; Q9CUX9; Q9D959; Q9WTU1;
25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 4.
05-DEC-2018, entry version 164.
RecName: Full=Structural maintenance of chromosomes protein 1A;
Short=SMC protein 1A;
Short=SMC-1-alpha;
Short=SMC-1A;
AltName: Full=Chromosome segregation protein SmcB;
AltName: Full=Sb1.8;
Name=Smc1a; Synonyms=Sb1.8, Smc1, Smc1l1, Smcb;
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 [MRNA], CHARACTERIZATION, AND IDENTIFICATION IN A
COHESIN COMPLEX WITH SMC3 AND RAD21.
TISSUE=Embryo;
PubMed=10375619; DOI=10.1016/S0378-1119(99)00160-2;
Darwiche N., Freeman L.A., Strunnikov A.;
"Characterization of the components of the putative mammalian sister
chromatid cohesion complex.";
Gene 233:39-47(1999).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 1-301 AND 977-1233.
STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus, Pancreas, and Thymus;
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).
[5]
INTERACTION WITH STAG3.
PubMed=11483963; DOI=10.1038/35087082;
Prieto I., Suja J.A., Pezzi N., Kremer L., Martinez-A C., Rufas J.S.,
Barbero J.L.;
"Mammalian STAG3 is a cohesin specific to sister chromatid arms in
meiosis I.";
Nat. Cell Biol. 3:761-766(2001).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, and Spleen;
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]
TISSUE SPECIFICITY.
PubMed=22977523; DOI=10.3892/etm.2011.232;
So E.Y., Ouchi T.;
"Functional interaction of BRCA1/ATM-associated BAAT1 with the DNA-PK
catalytic subunit.";
Exp. Ther. Med. 2:443-447(2011).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1037, 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).
-!- FUNCTION: Involved in chromosome cohesion during cell cycle and in
DNA repair. Involved in DNA repair via its interaction with BRCA1
and its related phosphorylation by ATM, and works as a downstream
effector in the ATM/NBS1 branch of S-phase checkpoint (By
similarity). Central component of cohesin complex. 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 cohesin
complex may also play a role in spindle pole assembly during
mitosis. Involved in DNA repair via its interaction with BRCA1 and
its related phosphorylation by ATM, or via its phosphorylation by
ATR. Works as a downstream effector both in the ATM/NBS1 branch
and in the ATR/MSH2 branch of S-phase checkpoint. {ECO:0000250}.
-!- SUBUNIT: Forms a heterodimer with SMC3 in cohesin complexes.
Cohesin complexes are composed of the SMC1 (SMC1A or SMC1B) and
SMC3 heterodimer attached via their SMC hinge domain, RAD21 which
link them, and one STAG protein (STAG1, STAG2 or STAG3), which
interacts with RAD21. In germ cell cohesin complexes, SMC1A is
mutually exclusive with SMC1B (PubMed:10375619). Interacts with
STAG3 (PubMed:11483963). Found in a complex with CDCA5, SMC3 and
RAD21, PDS5A/SCC-112 and PDS5B/APRIN. Found in a complex
containing POLE and SMC3. Interacts with BRCA1, SYCP2, NDC80, RPGR
and BRAT1. Found in a cohesin complex with SMC3, STAG1 and RAD21.
The SMC1A-SMC3 heterodimer interacts with the NIPBL-MAU2
heterodimer (By similarity). {ECO:0000250|UniProtKB:O97593,
ECO:0000250|UniProtKB:Q14683, ECO:0000250|UniProtKB:Q9Z1M9,
ECO:0000269|PubMed:10375619, ECO:0000269|PubMed:11483963}.
-!- INTERACTION:
Q61687:Atrx; NbExp=4; IntAct=EBI-2550016, EBI-2657527;
Q6A078:Cep290; NbExp=2; IntAct=EBI-2550016, EBI-1811999;
Q9Z2D6:Mecp2; NbExp=3; IntAct=EBI-2550016, EBI-1188816;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
Note=Associates with chromatin. The phosphorylated form on Ser-957
and Ser-966 associates with chromatin during G1/S/G2 phases but
not during M phase, suggesting that phosphorylation does not
regulate cohesin function (By similarity). Before prophase it is
scattered along chromosome arms. During prophase, most of cohesin
complexes dissociate from chromatin probably because of
phosphorylation by PLK, except at centromeres, where cohesin
complexes remain. At anaphase, the RAD21 subunit of the cohesin
complex is cleaved, leading to the dissociation of the complex
from chromosomes, allowing chromosome separation. In germ cells,
cohesin complex dissociates from chromatin at prophase I, and may
be replaced by a meiosis-specific cohesin complex. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitous (at protein level).
{ECO:0000269|PubMed:22977523}.
-!- DOMAIN: The flexible SMC 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 protein,
forming a ring structure (By similarity). {ECO:0000250}.
-!- PTM: Phosphorylated upon ionizing radiation or DNA methylation.
Phosphorylation of Ser-957 and Ser-966 activates it and is
required for S-phase checkpoint activation (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the SMC family. SMC1 subfamily.
{ECO:0000305}.
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EMBL; AF047600; AAD27753.1; -; mRNA.
EMBL; AL672180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC131667; AAI31668.1; -; mRNA.
EMBL; AK007334; BAE43202.1; -; mRNA.
EMBL; AK013648; BAB28937.1; -; mRNA.
EMBL; AK017948; BAB31016.3; -; mRNA.
EMBL; AK088183; BAC40193.1; -; mRNA.
CCDS; CCDS30473.1; -.
RefSeq; NP_062684.2; NM_019710.2.
UniGene; Mm.482095; -.
PDB; 2WD5; X-ray; 2.70 A; A=461-685.
PDBsum; 2WD5; -.
ProteinModelPortal; Q9CU62; -.
SMR; Q9CU62; -.
BioGrid; 204874; 42.
CORUM; Q9CU62; -.
DIP; DIP-57021N; -.
IntAct; Q9CU62; 39.
MINT; Q9CU62; -.
STRING; 10090.ENSMUSP00000044645; -.
iPTMnet; Q9CU62; -.
PhosphoSitePlus; Q9CU62; -.
EPD; Q9CU62; -.
MaxQB; Q9CU62; -.
PaxDb; Q9CU62; -.
PeptideAtlas; Q9CU62; -.
PRIDE; Q9CU62; -.
Ensembl; ENSMUST00000045312; ENSMUSP00000044645; ENSMUSG00000041133.
GeneID; 24061; -.
KEGG; mmu:24061; -.
UCSC; uc009upx.2; mouse.
CTD; 8243; -.
MGI; MGI:1344345; Smc1a.
eggNOG; KOG0018; Eukaryota.
eggNOG; COG1196; LUCA.
GeneTree; ENSGT00940000155614; -.
HOGENOM; HOG000195481; -.
HOVERGEN; HBG039593; -.
InParanoid; Q9CU62; -.
KO; K06636; -.
OMA; YMEAIVV; -.
OrthoDB; EOG091G00R5; -.
TreeFam; TF101156; -.
Reactome; R-MMU-2467813; Separation of Sister Chromatids.
Reactome; R-MMU-2468052; Establishment of Sister Chromatid Cohesion.
Reactome; R-MMU-2470946; Cohesin Loading onto Chromatin.
Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
EvolutionaryTrace; Q9CU62; -.
PRO; PR:Q9CU62; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000041133; Expressed in 286 organ(s), highest expression level in rostral migratory stream.
CleanEx; MM_SMC1A; -.
ExpressionAtlas; Q9CU62; baseline and differential.
Genevisible; Q9CU62; MM.
GO; GO:0008278; C:cohesin complex; IDA:CAFA.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
GO; GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
GO; GO:0097431; C:mitotic spindle pole; ISO:MGI.
GO; GO:0016363; C:nuclear matrix; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:CAFA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0036033; F:mediator complex binding; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0051321; P:meiotic cell cycle; IPI:MGI.
GO; GO:0007064; P:mitotic sister chromatid cohesion; IEA:InterPro.
GO; GO:0032876; P:negative regulation of DNA endoreduplication; ISO:MGI.
GO; GO:1901673; P:regulation of mitotic spindle assembly; ISO:MGI.
GO; GO:0072423; P:response to DNA damage checkpoint signaling; ISS:UniProtKB.
GO; GO:0009314; P:response to radiation; ISS:UniProtKB.
GO; GO:0007062; P:sister chromatid cohesion; ISO:MGI.
GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR003395; RecF/RecN/SMC_N.
InterPro; IPR024704; SMC.
InterPro; IPR029683; SMC1A_metazoan.
InterPro; IPR010935; SMC_hinge.
InterPro; IPR036277; SMC_hinge_sf.
PANTHER; PTHR18937:SF170; PTHR18937:SF170; 1.
Pfam; PF06470; SMC_hinge; 1.
Pfam; PF02463; SMC_N; 1.
PIRSF; PIRSF005719; SMC; 1.
SMART; SM00968; SMC_hinge; 1.
SUPFAM; SSF52540; SSF52540; 1.
SUPFAM; SSF75553; SSF75553; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
Centromere; Chromosome; Coiled coil; Complete proteome; DNA damage;
DNA repair; Meiosis; Mitosis; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 1233 Structural maintenance of chromosomes
protein 1A.
/FTId=PRO_0000118990.
DOMAIN 515 629 SMC hinge.
NP_BIND 32 39 ATP. {ECO:0000255}.
COILED 104 124 {ECO:0000255}.
COILED 163 503 {ECO:0000255}.
COILED 667 935 {ECO:0000255}.
COILED 988 1068 {ECO:0000255}.
COMPBIAS 1128 1163 Ala/Asp-rich (DA-box).
MOD_RES 358 358 Phosphoserine.
{ECO:0000250|UniProtKB:Q14683}.
MOD_RES 360 360 Phosphoserine.
{ECO:0000250|UniProtKB:Q14683}.
MOD_RES 648 648 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q14683}.
MOD_RES 713 713 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q14683}.
MOD_RES 957 957 Phosphoserine.
{ECO:0000250|UniProtKB:Q14683}.
MOD_RES 962 962 Phosphoserine.
{ECO:0000250|UniProtKB:Q14683}.
MOD_RES 966 966 Phosphoserine.
{ECO:0000250|UniProtKB:Q14683}.
MOD_RES 970 970 Phosphoserine.
{ECO:0000250|UniProtKB:Q14683}.
MOD_RES 1037 1037 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
CONFLICT 321 321 N -> H (in Ref. 1; AAD27753).
{ECO:0000305}.
CONFLICT 679 679 E -> G (in Ref. 1; AAD27753).
{ECO:0000305}.
CONFLICT 922 922 K -> E (in Ref. 1; AAD27753).
{ECO:0000305}.
CONFLICT 944 944 K -> E (in Ref. 1; AAD27753).
{ECO:0000305}.
CONFLICT 977 977 A -> G (in Ref. 4; BAE43202).
{ECO:0000305}.
CONFLICT 1013 1013 Q -> R (in Ref. 1; AAD27753).
{ECO:0000305}.
HELIX 501 510 {ECO:0000244|PDB:2WD5}.
HELIX 512 514 {ECO:0000244|PDB:2WD5}.
STRAND 515 518 {ECO:0000244|PDB:2WD5}.
HELIX 519 522 {ECO:0000244|PDB:2WD5}.
STRAND 523 527 {ECO:0000244|PDB:2WD5}.
HELIX 528 530 {ECO:0000244|PDB:2WD5}.
HELIX 531 538 {ECO:0000244|PDB:2WD5}.
HELIX 539 542 {ECO:0000244|PDB:2WD5}.
STRAND 545 548 {ECO:0000244|PDB:2WD5}.
HELIX 550 562 {ECO:0000244|PDB:2WD5}.
STRAND 568 572 {ECO:0000244|PDB:2WD5}.
TURN 573 575 {ECO:0000244|PDB:2WD5}.
HELIX 583 587 {ECO:0000244|PDB:2WD5}.
STRAND 592 594 {ECO:0000244|PDB:2WD5}.
HELIX 595 597 {ECO:0000244|PDB:2WD5}.
STRAND 598 602 {ECO:0000244|PDB:2WD5}.
HELIX 603 605 {ECO:0000244|PDB:2WD5}.
HELIX 606 612 {ECO:0000244|PDB:2WD5}.
TURN 613 615 {ECO:0000244|PDB:2WD5}.
STRAND 617 621 {ECO:0000244|PDB:2WD5}.
HELIX 622 630 {ECO:0000244|PDB:2WD5}.
STRAND 631 634 {ECO:0000244|PDB:2WD5}.
STRAND 638 640 {ECO:0000244|PDB:2WD5}.
STRAND 652 654 {ECO:0000244|PDB:2WD5}.
HELIX 656 662 {ECO:0000244|PDB:2WD5}.
HELIX 665 670 {ECO:0000244|PDB:2WD5}.
TURN 671 673 {ECO:0000244|PDB:2WD5}.
SEQUENCE 1233 AA; 143235 MW; E62CEB174854D9A6 CRC64;
MGFLKLIEIE NFKSYKGRQI IGPFQRFTAI IGPNGSGKSN LMDAISFVLG EKTSNLRVKT
LRDLIHGAPV GKPAANRAFV SMVYSEEGAE DRTFARVIVG GSSEYKINNK VVQLHEYSEE
LEKLGILIKA RNFLVFQGAV ESIAMKNPKE RTALFEEISR SGELAQEYDK RKKEMVKAEE
DTQFNYHRKK NIAAERKEAK QEKEEADRYQ RLKDEVVRAQ VQLQLFKLYH NEVEIEKLNK
ELASKNKEIE KDKKRMDKVE DELKEKKKEL GKMMREQQQI EKEIKEKDSE LNQKRPQYIK
AKENTSHKIK KLEAAKKSLQ NAQKHYKKRK GDMDELEKEM LSVEKARQEF EERMEEESQS
QGRDLTLEEN QVKKYHRLKE EASKRAATLA QELEKFNRDQ KADQDRLDLE ERKKVETEAK
IKQKLREIEE NQKRIEKLEE YITTSKQSLE EQKKLEGELT EEVEMAKRRI DEINKELNQV
MEQLGDARID RQESSRQQRK AEIMESIKRL YPGSVYGRLI DLCQPTQKKY QIAVTKVLGK
NMDAIIVDSE KTGRDCIQYI KEQRGEPETF LPLDYLEVKP TDEKLRELKG AKLVIDVIRY
EPPHIKKALQ YACGNALVCD NVEDARRIAF GGHQRHKTVA LDGTLFQKSG VISGGASDLK
AKARRWDEKA VDKLKEKKER LTEELKEQMK AKRKEAELRQ VQSQAHGLQM RLKYSQSDLE
QTKTRHLALN LQEKSKLESE LANFGPRIND IKRIIQSRER EMKDLKEKMN QVEDEVFEEF
CREIGVRNIR EFEEEKVKRQ NEIAKKRLEF ENQKTRLGIQ LDFEKNQLKE DQDKVHMWEQ
TVKKDENEIE KLKKEEQRHM KIIDETMAQL QDLKNQHLAK KSEVNDKNHE MEEIRKKLGG
ANKEMTHLQK EVTAIETKLE QKRSDRHNLL QACKMQDIKL PLSKGTMDDI SQEEGSSQGE
ESVSGSQRTS SIYAREALIE IDYGDLCEDL KDAQAEEEIK QEMNTLQQKL NEQQSVLQRI
AAPNMKAMEK LESVRDKFQE TSDEFEAARK RAKKAKQAFE QIKKERFDRF NACFESVATN
IDEIYKALSR NSSAQAFLGP ENPEEPYLDG INYNCVAPGK RFRPMDNLSG GEKTVAALAL
LFAIHSYKPA PFFVLDEIDA ALDNTNIGKV ANYIKEQSTC NFQAIVISLK EEFYTKAESL
IGVYPEQGDC VISKVLTFDL TKYPDANPNP NEQ


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EIAAB38768 CAPC,Chromosome-associated polypeptide C,hCAP-C,Homo sapiens,Human,SMC protein 4,SMC4,SMC-4,SMC4L1,Structural maintenance of chromosomes protein 4,XCAP-C homolog
EIAAB38760 Chicken,Chromosome scaffold protein ScII,Gallus gallus,SCII,SMC protein 2,SMC2,SMC-2,SMC2L1,Structural maintenance of chromosomes protein 2
EIAAB38756 DXS423E,Homo sapiens,Human,KIAA0178,Sb1.8,SB1.8,SMC protein 1A,SMC1,SMC1A,SMC-1A,SMC-1-alpha,SMC1L1,Structural maintenance of chromosomes protein 1A
EIAAB38770 Kiaa0594,MLZ-453,Mouse,mSMC5,Mus musculus,Protein expressed in male leptotene and zygotene spermatocytes 453,SMC protein 5,Smc5,SMC-5,Smc5l1,Structural maintenance of chromosomes protein 5
EIAAB38754 Bos taurus,Bovine,SMC protein 1A,SMC1,SMC1A,SMC-1A,SMC1L1,Structural maintenance of chromosomes protein 1A
EIAAB38758 Mouse,Mus musculus,SMC protein 1B,Smc1b,SMC-1B,SMC-1-beta,Smc1l2,Structural maintenance of chromosomes protein 1B
EIAAB38757 Rat,Rattus norvegicus,SMC protein 1A,Smc1,Smc1a,SMC-1A,Smc1l1,Structural maintenance of chromosomes protein 1A
EIAAB38759 Homo sapiens,Human,SMC protein 1B,SMC1B,SMC-1B,SMC-1-beta,SMC1L2,Structural maintenance of chromosomes protein 1B
EIAAB38772 Homo sapiens,hSMC6,Human,SMC protein 6,SMC6,SMC-6,SMC6L1,Structural maintenance of chromosomes protein 6
EIAAB38773 Kiaa4103,Mouse,mSMC6,Mus musculus,SMC protein 6,Smc6,SMC-6,Smc6l1,Structural maintenance of chromosomes protein 6
EIAAB38771 Homo sapiens,hSMC5,Human,KIAA0594,SMC protein 5,SMC5,SMC-5,SMC5L1,Structural maintenance of chromosomes protein 5
27-035 Condensin complexes I and II play essential roles in mitotic chromosome assembly and segregation. Both condensins contain 2 invariant structural maintenance of chromosome (SMC) subunits, SMC2 and SMC4 0.05 mg
27-036 Condensin complexes I and II play essential roles in mitotic chromosome assembly and segregation. Both condensins contain 2 invariant structural maintenance of chromosome (SMC) subunits, SMC2 and SMC4 0.05 mg
EIAAB38765 Bos taurus,Bovine,Chondroitin sulfate proteoglycan 6,CSPG6,SMC protein 3,SMC3,SMC-3,SMC3L1,Structural maintenance of chromosomes protein 3
U17PA_MOUSE Rat ELISA Kit FOR Structural maintenance of chromosomes protein 3 96T
EH2268 Structural maintenance of chromosomes protein 4 Elisa Kit 96T
E0693h Rat ELISA Kit FOR Structural maintenance of chromosomes protein 3 96T


 

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