Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Helicase-like transcription factor (EC 2.3.2.27) (EC 3.6.4.-) (DNA-binding protein/plasminogen activator inhibitor 1 regulator) (HIP116) (RING finger protein 80) (RING-type E3 ubiquitin transferase HLTF) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3) (Sucrose nonfermenting protein 2-like 3)

 HLTF_HUMAN              Reviewed;        1009 AA.
Q14527; D3DNH3; Q14536; Q16051; Q7KYJ6; Q86YA5; Q92652; Q96KM9;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 2.
25-OCT-2017, entry version 168.
RecName: Full=Helicase-like transcription factor;
EC=2.3.2.27;
EC=3.6.4.-;
AltName: Full=DNA-binding protein/plasminogen activator inhibitor 1 regulator;
AltName: Full=HIP116;
AltName: Full=RING finger protein 80;
AltName: Full=RING-type E3 ubiquitin transferase HLTF {ECO:0000305};
AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3;
AltName: Full=Sucrose nonfermenting protein 2-like 3;
Name=HLTF; Synonyms=HIP116A, RNF80, SMARCA3, SNF2L3, ZBU1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Cervix carcinoma;
PubMed=7876228; DOI=10.1074/jbc.270.9.4575;
Sheridan P.L., Schorpp M., Voz M.L., Jones K.A.;
"Cloning of an SNF2/SWI2-related protein that binds specifically to
the SPH motifs of the SV40 enhancer and to the HIV-1 promoter.";
J. Biol. Chem. 270:4575-4587(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ALTERNATIVE
INITIATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=8672239; DOI=10.1089/dna.1996.15.429;
Ding H., Descheemaeker K., Marynen P., Nelles L., Carvalho T.,
Carmo-Fonseca M., Collen D., Belayew A.;
"Characterization of a helicase-like transcription factor involved in
the expression of the human plasminogen activator inhibitor-1 gene.";
DNA Cell Biol. 15:429-442(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Ribaucour F., Wiedig M., Benotmane A.M., Coppee F., Belayew A.;
"Characterization of the human SMARCA3/HLTF gene.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 38-213.
PubMed=8342330;
Descheemaeker K.;
"On the regulation of the plasminogen activator inhibitor-1 gene
expression.";
Verh. K. Acad. Geneeskd. Belg. 55:225-264(1993).
[7]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=9126292; DOI=10.1006/dbio.1996.8486;
Gong X., Kaushal S., Ceccarelli E., Bogdanova N., Neville C.,
Nguyen T., Clark H., Khatib Z.A., Valentine M., Look A.T.,
Rosenthal N.;
"Developmental regulation of Zbu1, a DNA-binding member of the
SWI2/SNF2 family.";
Dev. Biol. 183:166-182(1997).
[8]
FUNCTION, AND INTERACTION WITH SP1 AND SP3.
PubMed=10391891; DOI=10.1074/jbc.274.28.19573;
Ding H., Benotmane A.M., Suske G., Collen D., Belayew A.;
"Functional interactions between Sp1 or Sp3 and the helicase-like
transcription factor mediate basal expression from the human
plasminogen activator inhibitor-1 gene.";
J. Biol. Chem. 274:19573-19580(1999).
[9]
EPIGENETIC INACTIVATION IN COLON CANCER.
PubMed=11904375; DOI=10.1073/pnas.062459899;
Moinova H.R., Chen W.-D., Shen L., Smiraglia D., Olechnowicz J.,
Ravi L., Kasturi L., Myeroff L., Plass C., Parsons R., Minna J.,
Willson J.K.V., Green S.B., Issa J.-P., Markowitz S.D.;
"HLTF gene silencing in human colon cancer.";
Proc. Natl. Acad. Sci. U.S.A. 99:4562-4567(2002).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-398; SER-400
AND THR-736, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[12]
FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH PCNA;
UBE2N AND RAD18.
PubMed=18316726; DOI=10.1073/pnas.0800563105;
Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L.,
Prakash S., Haracska L.;
"Human HLTF functions as a ubiquitin ligase for proliferating cell
nuclear antigen polyubiquitination.";
Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008).
[13]
FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, AND INTERACTION WITH PCNA;
RAD18; SHPRH AND UBE2N.
PubMed=18719106; DOI=10.1073/pnas.0805685105;
Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X.,
Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
"Polyubiquitination of proliferating cell nuclear antigen by HLTF and
SHPRH prevents genomic instability from stalled replication forks.";
Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION AT TYR-195.
PubMed=21457752; DOI=10.1016/j.mce.2011.03.009;
Helmer R.A., Dertien J.S., Chilton B.S.;
"Prolactin induces Jak2 phosphorylation of RUSHY195.";
Mol. Cell. Endocrinol. 338:79-83(2011).
[18]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-27, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-112 AND LYS-211, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[20]
STRUCTURE BY NMR OF 51-171.
Structural genomics consortium (SGC);
"NMR structure of the HLTF hiran domain.";
Submitted (OCT-2010) to the PDB data bank.
-!- FUNCTION: Has both helicase and E3 ubiquitin ligase activities.
Possesses intrinsic ATP-dependent nucleosome-remodeling activity;
This activity may be required for transcriptional activation or
repression of specific target promoters (By similarity). These may
include the SERPINE1 and HIV-1 promoters and the SV40 enhancer, to
which this protein can bind directly. Plays a role in error-free
postreplication repair (PRR) of damaged DNA and maintains genomic
stability through acting as a ubiquitin ligase for 'Lys-63'-linked
polyubiquitination of chromatin-bound PCNA. {ECO:0000250,
ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:18316726,
ECO:0000269|PubMed:18719106, ECO:0000269|PubMed:7876228,
ECO:0000269|PubMed:8672239, ECO:0000269|PubMed:9126292}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with SP1 and SP3 independently of DNA; the
interaction with these transcriptional factors may be required for
basal transcription of target genes. Interacts with EGR1; the
interaction requires prior binding to DNA and represses c-Rel via
a DNA looping mechanism (By similarity). Interacts with GATA4 (By
similarity). Interacts with PCNA; the interaction promotes
polyubiquitination of PCNA through association with the UBE2B-
RAD18 and UBE2V2-UBE2N ubiquitin ligase complexes. Interacts with
RAD18, SHPRH, UBE2V2 and UBE2N. {ECO:0000250,
ECO:0000269|PubMed:10391891, ECO:0000269|PubMed:18316726,
ECO:0000269|PubMed:18719106}.
-!- INTERACTION:
P12004:PCNA; NbExp=2; IntAct=EBI-1045161, EBI-358311;
Q9NS91:RAD18; NbExp=3; IntAct=EBI-1045161, EBI-2339393;
P60903:S100A10; NbExp=2; IntAct=EBI-1045161, EBI-717048;
P61088:UBE2N; NbExp=4; IntAct=EBI-1045161, EBI-1052908;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000269|PubMed:8672239}. Nucleus, nucleolus {ECO:0000250}.
Nucleus, nucleoplasm {ECO:0000250}. Note=Nuclear localization is
stimulated by progesterone. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=1;
IsoId=Q14527-1; Sequence=Displayed;
Name=2;
IsoId=Q14527-2; Sequence=VSP_018873;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver,
lung, pancreas, placenta and skeletal muscle.
{ECO:0000269|PubMed:8672239, ECO:0000269|PubMed:9126292}.
-!- MISCELLANEOUS: Subject to frequent epigenetic inactivation by
promoter methylation in colon cancer.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16
subfamily. {ECO:0000305}.
-!- CAUTION: In contrast with other SMARC proteins, there is currently
no evidence that it associates with actin or actin-related
proteins. It may rather act as a sequence-specific DNA binding
ATPase, whose precise function remains to be fully characterized.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HLTFID42332ch3q24.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L34673; AAA67436.1; -; mRNA.
EMBL; Z46606; CAA86571.1; -; mRNA.
EMBL; Z46606; CAA86572.1; -; mRNA.
EMBL; AJ418064; CAD10805.1; -; Genomic_DNA.
EMBL; CH471052; EAW78889.1; -; Genomic_DNA.
EMBL; CH471052; EAW78892.1; -; Genomic_DNA.
EMBL; CH471052; EAW78893.1; -; Genomic_DNA.
EMBL; BC044659; AAH44659.1; -; mRNA.
EMBL; S64671; AAB27691.1; -; mRNA.
CCDS; CCDS33875.1; -. [Q14527-1]
PIR; S49618; S49618.
RefSeq; NP_001305863.1; NM_001318934.1.
RefSeq; NP_001305864.1; NM_001318935.1. [Q14527-1]
RefSeq; NP_003062.2; NM_003071.3. [Q14527-1]
RefSeq; NP_620636.1; NM_139048.2. [Q14527-1]
RefSeq; XP_016862568.1; XM_017007079.1.
UniGene; Hs.3068; -.
PDB; 2MZN; NMR; -; A=51-171.
PDB; 4HRE; X-ray; 2.79 A; G/H/K/L=26-39.
PDB; 4HRH; X-ray; 3.00 A; C/D=26-39.
PDB; 4S0N; X-ray; 1.50 A; A/B/C/D=55-180.
PDB; 4XZF; X-ray; 1.38 A; A=58-174.
PDB; 4XZG; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I=57-174.
PDB; 5BNH; X-ray; 1.70 A; A/D=55-175.
PDB; 5K5F; NMR; -; A=51-171.
PDBsum; 2MZN; -.
PDBsum; 4HRE; -.
PDBsum; 4HRH; -.
PDBsum; 4S0N; -.
PDBsum; 4XZF; -.
PDBsum; 4XZG; -.
PDBsum; 5BNH; -.
PDBsum; 5K5F; -.
ProteinModelPortal; Q14527; -.
SMR; Q14527; -.
BioGrid; 112480; 57.
DIP; DIP-29828N; -.
IntAct; Q14527; 32.
MINT; MINT-1639589; -.
STRING; 9606.ENSP00000308944; -.
iPTMnet; Q14527; -.
PhosphoSitePlus; Q14527; -.
BioMuta; HLTF; -.
DMDM; 60390864; -.
EPD; Q14527; -.
MaxQB; Q14527; -.
PaxDb; Q14527; -.
PeptideAtlas; Q14527; -.
PRIDE; Q14527; -.
DNASU; 6596; -.
Ensembl; ENST00000310053; ENSP00000308944; ENSG00000071794. [Q14527-1]
Ensembl; ENST00000392912; ENSP00000376644; ENSG00000071794. [Q14527-1]
Ensembl; ENST00000494055; ENSP00000420429; ENSG00000071794. [Q14527-1]
GeneID; 6596; -.
KEGG; hsa:6596; -.
UCSC; uc003ewq.2; human. [Q14527-1]
CTD; 6596; -.
DisGeNET; 6596; -.
EuPathDB; HostDB:ENSG00000071794.15; -.
GeneCards; HLTF; -.
H-InvDB; HIX0024319; -.
HGNC; HGNC:11099; HLTF.
HPA; HPA015284; -.
HPA; HPA049001; -.
MIM; 603257; gene.
neXtProt; NX_Q14527; -.
OpenTargets; ENSG00000071794; -.
PharmGKB; PA35949; -.
eggNOG; KOG1001; Eukaryota.
eggNOG; COG0553; LUCA.
GeneTree; ENSGT00880000137978; -.
HOVERGEN; HBG079192; -.
InParanoid; Q14527; -.
KO; K15711; -.
OMA; IMDNKLA; -.
OrthoDB; EOG091G013T; -.
PhylomeDB; Q14527; -.
TreeFam; TF332703; -.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
SIGNOR; Q14527; -.
UniPathway; UPA00143; -.
ChiTaRS; HLTF; human.
GeneWiki; HLTF; -.
GenomeRNAi; 6596; -.
PRO; PR:Q14527; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000071794; -.
CleanEx; HS_HLTF; -.
ExpressionAtlas; Q14527; baseline and differential.
Genevisible; Q14527; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0061630; F:ubiquitin protein ligase activity; EXP:Reactome.
GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
CDD; cd00079; HELICc; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014905; HIRAN.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000330; SNF2_N.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF08797; HIRAN; 1.
Pfam; PF00176; SNF2_N; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00910; HIRAN; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF52540; SSF52540; 4.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative initiation; ATP-binding;
Chromatin regulator; Complete proteome; Cytoplasm; DNA-binding;
Helicase; Hydrolase; Isopeptide bond; Metal-binding; Methylation;
Multifunctional enzyme; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transcription; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 1009 Helicase-like transcription factor.
/FTId=PRO_0000030722.
DOMAIN 435 606 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 837 996 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DNA_BIND 38 287
NP_BIND 294 301 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
ZN_FING 760 801 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 925 1009 Interaction with SP1 and SP3.
{ECO:0000269|PubMed:10391891}.
MOTIF 557 560 DEGH box.
MOD_RES 27 27 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 195 195 Phosphotyrosine; by JAK2.
{ECO:0000269|PubMed:21457752}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 398 398 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 400 400 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 736 736 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
CROSSLNK 112 112 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 211 211 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 122 Missing (in isoform 2).
{ECO:0000303|PubMed:8672239}.
/FTId=VSP_018873.
VARIANT 311 311 N -> S (in dbSNP:rs2305868).
/FTId=VAR_052121.
VARIANT 362 362 E -> Q (in dbSNP:rs2228257).
/FTId=VAR_052122.
VARIANT 819 819 R -> H (in dbSNP:rs2229361).
/FTId=VAR_029265.
CONFLICT 35 35 P -> L (in Ref. 2; CAA86571).
{ECO:0000305}.
CONFLICT 211 213 KTE -> PEF (in Ref. 6; AAB27691).
{ECO:0000305}.
CONFLICT 337 337 D -> G (in Ref. 2; CAA86571/CAA86572 and
3; CAD10805). {ECO:0000305}.
CONFLICT 382 382 S -> T (in Ref. 1; AAA67436).
{ECO:0000305}.
CONFLICT 429 429 Missing (in Ref. 5; AAH44659).
{ECO:0000305}.
CONFLICT 913 913 K -> R (in Ref. 2; CAA86571/CAA86572 and
3; CAD10805). {ECO:0000305}.
HELIX 51 54 {ECO:0000244|PDB:2MZN}.
STRAND 58 68 {ECO:0000244|PDB:4XZF}.
HELIX 70 72 {ECO:0000244|PDB:4XZF}.
STRAND 81 87 {ECO:0000244|PDB:4XZF}.
STRAND 98 101 {ECO:0000244|PDB:4XZF}.
STRAND 107 111 {ECO:0000244|PDB:4XZF}.
HELIX 113 124 {ECO:0000244|PDB:4XZF}.
STRAND 129 134 {ECO:0000244|PDB:4XZF}.
STRAND 141 152 {ECO:0000244|PDB:4XZF}.
HELIX 154 156 {ECO:0000244|PDB:4XZF}.
HELIX 157 166 {ECO:0000244|PDB:4XZF}.
SEQUENCE 1009 AA; 113929 MW; 0AB96F6C8484FD15 CRC64;
MSWMFKRDPV WKYLQTVQYG VHGNFPRLSY PTFFPRFEFQ DVIPPDDFLT SDEEVDSVLF
GSLRGHVVGL RYYTGVVNNN EMVALQRDPN NPYDKNAIKV NNVNGNQVGH LKKELAGALA
YIMDNKLAQI EGVVPFGANN AFTMPLHMTF WGKEENRKAV SDQLKKHGFK LGPAPKTLGF
NLESGWGSGR AGPSYSMPVH AAVQMTTEQL KTEFDKLFED LKEDDKTHEM EPAEAIETPL
LPHQKQALAW MVSRENSKEL PPFWEQRNDL YYNTITNFSE KDRPENVHGG ILADDMGLGK
TLTAIAVILT NFHDGRPLPI ERVKKNLLKK EYNVNDDSMK LGGNNTSEKA DGLSKDASRC
SEQPSISDIK EKSKFRMSEL SSSRPKRRKT AVQYIESSDS EEIETSELPQ KMKGKLKNVQ
SETKGRAKAG SSKVIEDVAF ACALTSSVPT TKKKMLKKGA CAVEGSKKTD VEERPRTTLI
ICPLSVLSNW IDQFGQHIKS DVHLNFYVYY GPDRIREPAL LSKQDIVLTT YNILTHDYGT
KGDSPLHSIR WLRVILDEGH AIRNPNAQQT KAVLDLESER RWVLTGTPIQ NSLKDLWSLL
SFLKLKPFID REWWHRTIQR PVTMGDEGGL RRLQSLIKNI TLRRTKTSKI KGKPVLELPE
RKVFIQHITL SDEERKIYQS VKNEGRATIG RYFNEGTVLA HYADVLGLLL RLRQICCHTY
LLTNAVSSNG PSGNDTPEEL RKKLIRKMKL ILSSGSDEEC AICLDSLTVP VITHCAHVFC
KPCICQVIQN EQPHAKCPLC RNDIHEDNLL ECPPEELARD SEKKSDMEWT SSSKINALMH
ALTDLRKKNP NIKSLVVSQF TTFLSLIEIP LKASGFVFTR LDGSMAQKKR VESIQCFQNT
EAGSPTIMLL SLKAGGVGLN LSAASRVFLM DPAWNPAAED QCFDRCHRLG QKQEVIITKF
IVKDSVEENM LKIQNKKREL AAGAFGTKKP NADEMKQAKI NEIRTLIDL


Related products :

Catalog number Product name Quantity
18-272-196662 SMARCA3 - Rabbit polyclonal to SMARCA3; EC 3.6.1.-; SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3; Sucrose nonfermenting protein 2-like 3; DNA-binding p 0.05 mg
EIAAB38782 Mouse,mSnf2h,Mus musculus,Smarca5,Snf2h,Sucrose nonfermenting protein 2 homolog,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5
EIAAB38735 Bos taurus,Bovine,HARP,HepA-related protein,SMARCAL1,Sucrose nonfermenting protein 2-like 1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
EIAAB38733 Harp,HepA-related protein,Rat,Rattus norvegicus,Smarcal1,Sucrose nonfermenting protein 2-like 1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
EIAAB38732 Harp,HepA-related protein,mharp,Mouse,Mus musculus,Smarcal1,Sucrose nonfermenting protein 2-like 1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
EIAAB38734 HARP,HepA-related protein,hHARP,Homo sapiens,Human,SMARCAL1,Sucrose nonfermenting protein 2-like 1,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
EIAAB38783 Homo sapiens,hSNF2H,Human,SMARCA5,SNF2H,Sucrose nonfermenting protein 2 homolog,SWI_SNF-related matrix-associated actin-dependent regulator of chromatin A5,SWI_SNF-related matrix-associated actin-depe
18-003-43154 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related - SMARCE1-related protein; HMG domain protein HMG20B; Structural DNA-binding protein BRAF35; BRCA2 0.05 mg Aff Pur
18-003-42490 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 - Integrase interactor 1 protein; hSNF5; BAF47 Polyclonal 0.05 mg Aff Pur
PDE12_MOUSE Rat ELISA Kit FOR SWI per SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 96T
E0448Rb Rat ELISA Kit FOR SWI per SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 96T
EIAAB34367 CARP-2,Caspase regulator CARP2,Caspases-8 and -10-associated RING finger protein 2,E3 ubiquitin-protein ligase rififylin,Fring,FYVE-RING finger protein Sakura,Homo sapiens,Human,RFFL,RING finger and F
18-003-43477 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 - BRG1-associated factor 57 Polyclonal 0.05 mg Aff Pur
H3844 SWI SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 (SMARCAL1), Rat, ELISA Kit 96T
20-372-60078 SWI_SNF related. matrix associated. actin dependent regulator of chromatin. subfamily a. member 4 (SMARCA4) - Mouse monoclonal anti-human SMARCA4 antibody; EC 3.6.1.-; ATP-dependent helicase SMARCA4; 0.1 mg
H3843 SWI SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 (SMARCAL1), Mouse, ELISA Kit 96T
CSB-EL021804HU Human SWI per SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1(SMARCAL1) ELISA kit 96T
H3842 SWI SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 (SMARCAL1), Human, ELISA Kit 96T
H3841 SWI SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1 (SMARCAL1), Bovine, ELISA Kit 96T
CSB-EL021804RA Rat SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1(SMARCAL1) ELISA kit 96T
18-272-195641 SMARCA2 - Rabbit polyclonal to SMARCA2; EC 3.6.1.-; ATP-dependent helicase SMARCA2; SNF2-alpha; SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2; hBRM Poly 0.1 ml
18-272-195642 SMARCA2 - Rabbit polyclonal to SMARCA2; EC 3.6.1.-; ATP-dependent helicase SMARCA2; SNF2-alpha; SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2; hBRM Poly 0.1 ml
CSB-EL021804MO Mouse SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1(SMARCAL1) ELISA kit 96T
CSB-EL021804HU Human SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1(SMARCAL1) ELISA kit 96T
SMAL1_RAT ELISA Kit FOR SWI per SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1; organism: Rat; gene name: Smarcal1 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur