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Fanconi anemia core complex-associated protein 20 (FANCA-associated protein of 20 kDa) (Fanconi anemia-associated protein of 20 kDa)

 FAP20_HUMAN             Reviewed;         180 AA.
Q6NZ36; A6PW39; A6PW40; A6PW41; A8MQT6; F2Z2L4; Q6ZT64; Q71M24;
Q96ND7;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 2.
25-OCT-2017, entry version 106.
RecName: Full=Fanconi anemia core complex-associated protein 20 {ECO:0000312|HGNC:HGNC:26428};
AltName: Full=FANCA-associated protein of 20 kDa {ECO:0000303|PubMed:22343915};
AltName: Full=Fanconi anemia-associated protein of 20 kDa {ECO:0000303|PubMed:22343915};
Name=FAAP20 {ECO:0000303|PubMed:22343915,
ECO:0000312|HGNC:HGNC:26428}; Synonyms=C1orf86; ORFNames=FP7162;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Amygdala, and Synovial cell;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 152-180 (ISOFORM 5).
TISSUE=Hypothalamus;
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]
FUNCTION, IDENTIFICATION IN THE FA COMPLEX, SUBCELLULAR LOCATION,
DOMAIN, INTERACTION WITH FANCA, AND MUTAGENESIS OF CYS-170.
PubMed=22343915; DOI=10.1182/blood-2011-10-385963;
Ali A.M., Pradhan A., Singh T.R., Du C., Li J., Wahengbam K.,
Grassman E., Auerbach A.D., Pang Q., Meetei A.R.;
"FAAP20: a novel ubiquitin-binding FA nuclear core-complex protein
required for functional integrity of the FA-BRCA DNA repair pathway.";
Blood 119:3285-3294(2012).
[7]
FUNCTION, IDENTIFICATION IN THE FA COMPLEX, SUBCELLULAR LOCATION,
DOMAIN, INTERACTION WITH FANCA, AND MUTAGENESIS OF CYS-147 AND
ASP-164.
PubMed=22705371; DOI=10.1016/j.molcel.2012.05.026;
Yan Z., Guo R., Paramasivam M., Shen W., Ling C., Fox D. III, Wang Y.,
Oostra A.B., Kuehl J., Lee D.Y., Takata M., Hoatlin M.E.,
Schindler D., Joenje H., de Winter J.P., Li L., Seidman M.M., Wang W.;
"A ubiquitin-binding protein, FAAP20, links RNF8-mediated
ubiquitination to the Fanconi anemia DNA repair network.";
Mol. Cell 47:61-75(2012).
[8]
FUNCTION, IDENTIFICATION IN THE FA COMPLEX, DOMAIN, INTERACTION WITH
REV1, AND MUTAGENESIS OF CYS-147 AND CYS-150.
PubMed=22266823; DOI=10.1038/nsmb.2222;
Kim H., Yang K., Dejsuphong D., D'Andrea A.D.;
"Regulation of Rev1 by the Fanconi anemia core complex.";
Nat. Struct. Mol. Biol. 19:164-170(2012).
[9]
FUNCTION, IDENTIFICATION IN THE FA COMPLEX, DOMAIN, INTERACTION WITH
FANCA, AND MUTAGENESIS OF CYS-147 AND CYS-150.
PubMed=22396592; DOI=10.1073/pnas.1118720109;
Leung J.W., Wang Y., Fong K.W., Huen M.S., Li L., Chen J.;
"Fanconi anemia (FA) binding protein FAAP20 stabilizes FA
complementation group A (FANCA) and participates in interstrand cross-
link repair.";
Proc. Natl. Acad. Sci. U.S.A. 109:4491-4496(2012).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-137, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Component of the Fanconi anemia (FA) complex required to
recruit the FA complex to DNA interstrand cross-links (ICLs) and
promote ICLs repair. Following DNA damage recognizes and binds
'Lys-63'-linked ubiquitin generated by RNF8 at ICLs and recruits
other components of the FA complex. Promotes translesion synthesis
via interaction with REV1. {ECO:0000269|PubMed:22266823,
ECO:0000269|PubMed:22343915, ECO:0000269|PubMed:22396592,
ECO:0000269|PubMed:22705371}.
-!- SUBUNIT: Component of the Fanconi anemia (FA) complex. Interacts
with FANCA; interaction is direct. Interacts with REV1. Reported
to bind monoubiquitinated REV1; however it binds better to non-
ubiquitinated REV1 (PubMed:22266823).
{ECO:0000269|PubMed:22266823, ECO:0000269|PubMed:22343915,
ECO:0000269|PubMed:22396592, ECO:0000269|PubMed:22705371}.
-!- INTERACTION:
O15360:FANCA; NbExp=5; IntAct=EBI-15965017, EBI-81570;
Q9UBZ9:REV1; NbExp=2; IntAct=EBI-2817693, EBI-7353917;
Q920Q2:Rev1 (xeno); NbExp=7; IntAct=EBI-15965017, EBI-2114764;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22343915,
ECO:0000269|PubMed:22705371}. Chromosome
{ECO:0000305|PubMed:22343915, ECO:0000305|PubMed:22705371}.
Note=Following DNA damage, recruited to DNA interstrand cross-
links (ICLs) sites by binding to ubiquitin generated by RNF8.
{ECO:0000269|PubMed:22705371}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q6NZ36-1; Sequence=Displayed;
Name=2;
IsoId=Q6NZ36-2; Sequence=VSP_030812;
Note=Ref.1 (BAC86730) sequence is in conflict in position:
65:R->H. {ECO:0000305};
Name=3;
IsoId=Q6NZ36-3; Sequence=VSP_030813;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q6NZ36-4; Sequence=VSP_030816;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=5;
IsoId=Q6NZ36-5; Sequence=VSP_030814, VSP_030815;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q6NZ36-6; Sequence=VSP_047264;
Note=Gene prediction based on EST data.;
-!- DOMAIN: The UBZ-type zinc finger binds both 'Lys-48'- and 'Lys-
63'-linked polyubiquitin with preference for 'Lys-63'-linked
polyubiquitin. {ECO:0000269|PubMed:22266823,
ECO:0000269|PubMed:22343915, ECO:0000269|PubMed:22396592,
ECO:0000269|PubMed:22705371}.
-!- CAUTION: According to a report, ubiquitin-binding is dispensable
for function (PubMed:22396592). However, such data are not
confirmed by PubMed:22705371. {ECO:0000305|PubMed:22396592}.
-!- SEQUENCE CAUTION:
Sequence=AAH66360.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AK055593; BAB70965.1; -; mRNA.
EMBL; AK126870; BAC86730.1; -; mRNA.
EMBL; AF461903; AAQ04817.1; -; mRNA.
EMBL; AL590822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471183; EAW56125.1; -; Genomic_DNA.
EMBL; BC066360; AAH66360.1; ALT_INIT; mRNA.
EMBL; BC078145; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC103992; AAI03993.1; -; mRNA.
CCDS; CCDS38.2; -. [Q6NZ36-1]
CCDS; CCDS57965.1; -. [Q6NZ36-6]
CCDS; CCDS72687.1; -. [Q6NZ36-5]
RefSeq; NP_001243874.1; NM_001256945.1.
RefSeq; NP_001243875.1; NM_001256946.1.
RefSeq; NP_001243876.1; NM_001256947.1.
RefSeq; NP_001269599.1; NM_001282670.1. [Q6NZ36-2]
RefSeq; NP_001269600.1; NM_001282671.1.
RefSeq; NP_001269601.1; NM_001282672.1.
RefSeq; NP_001269602.1; NM_001282673.1.
RefSeq; NP_872339.2; NM_182533.2.
UniGene; Hs.107101; -.
PDB; 2MUQ; NMR; -; A=140-180.
PDB; 2MUR; NMR; -; A=140-180.
PDB; 3WWQ; X-ray; 1.90 A; C/F/I/L=142-180.
PDBsum; 2MUQ; -.
PDBsum; 2MUR; -.
PDBsum; 3WWQ; -.
ProteinModelPortal; Q6NZ36; -.
SMR; Q6NZ36; -.
BioGrid; 128288; 24.
DIP; DIP-59917N; -.
IntAct; Q6NZ36; 30.
STRING; 9606.ENSP00000367808; -.
iPTMnet; Q6NZ36; -.
BioMuta; FAAP20; -.
DMDM; 166991449; -.
MaxQB; Q6NZ36; -.
PaxDb; Q6NZ36; -.
PeptideAtlas; Q6NZ36; -.
PRIDE; Q6NZ36; -.
Ensembl; ENST00000378543; ENSP00000367804; ENSG00000162585. [Q6NZ36-6]
Ensembl; ENST00000378546; ENSP00000367808; ENSG00000162585. [Q6NZ36-1]
Ensembl; ENST00000400918; ENSP00000383709; ENSG00000162585. [Q6NZ36-5]
Ensembl; ENST00000414253; ENSP00000410450; ENSG00000162585. [Q6NZ36-4]
GeneID; 199990; -.
KEGG; hsa:199990; -.
UCSC; uc001aiy.4; human. [Q6NZ36-1]
CTD; 199990; -.
DisGeNET; 199990; -.
EuPathDB; HostDB:ENSG00000162585.16; -.
GeneCards; FAAP20; -.
HGNC; HGNC:26428; FAAP20.
HPA; HPA038829; -.
MIM; 615183; gene.
neXtProt; NX_Q6NZ36; -.
OpenTargets; ENSG00000162585; -.
PharmGKB; PA142672470; -.
eggNOG; ENOG410J1M8; Eukaryota.
eggNOG; ENOG410Y5B2; LUCA.
HOGENOM; HOG000111230; -.
HOVERGEN; HBG107553; -.
InParanoid; Q6NZ36; -.
OMA; GSKTFSW; -.
PhylomeDB; Q6NZ36; -.
TreeFam; TF336358; -.
Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
ChiTaRS; C1orf86; human.
GenomeRNAi; 199990; -.
PRO; PR:Q6NZ36; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162585; -.
CleanEx; HS_C1orf86; -.
ExpressionAtlas; Q6NZ36; baseline and differential.
Genevisible; Q6NZ36; HS.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005694; C:chromosome; IDA:UniProtKB.
GO; GO:0043240; C:Fanconi anaemia nuclear complex; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
GO; GO:0140036; F:ubiquitin-dependent protein binding; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB.
GO; GO:0019985; P:translesion synthesis; IMP:UniProtKB.
InterPro; IPR031491; FANCA_interact.
InterPro; IPR031490; UBZ_FAAP20.
Pfam; PF15751; FANCA_interact; 1.
Pfam; PF15750; UBZ_FAAP20; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosome; Complete proteome;
DNA damage; DNA repair; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Zinc; Zinc-finger.
CHAIN 1 180 Fanconi anemia core complex-associated
protein 20.
/FTId=PRO_0000316882.
ZN_FING 144 174 UBZ-type.
MOD_RES 113 113 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 21 MEAARRPRLGLSRRRPRPAGG -> MCGPEHLLCCPKDLAM
FPRQLSLTACLPGTPVSHKCHHIWLWVGVPAWHPRASRCGG
AQPSSWLRQKAARAFWLSLPAAKLRHHSSRWLRRSGAFSSG
STLKPPPSPSPAPLCHADNLRTGRTR (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_030812.
VAR_SEQ 1 21 MEAARRPRLGLSRRRPRPAGG -> MNFGLEKTHFHCARVS
PNQKLFSNKAKLRHHSSRWLRRSGAFSSGSTLKPPPSPSPA
PLCHADNLRTGRTR (in isoform 3).
{ECO:0000303|PubMed:15498874}.
/FTId=VSP_030813.
VAR_SEQ 22 180 PSGGRPWFLLGGDERERLWAELLRTVSPELILDHEVPSLPA
FPGQEPRCGPEPTEVFTVGPKTFSWTPFPPDLWGPGRSYRL
LHGAGGHLESPARSLPQRPAPDPCRAPRVEQQPSVEGAAAL
RSCPMCQKEFAPRLTQLDVDSHLAQCLAESTEDVTW -> S
PGAARSPLKSSLSDPRPFPGHPFRRTCGARAVPTGCFTGQE
GTWNPPPGPCPSARHLIPAGPPGWSSSRLWRVPRPCAAAPC
ARRSSPPG (in isoform 6). {ECO:0000305}.
/FTId=VSP_047264.
VAR_SEQ 158 158 L -> YFNSRPHLCPAGS (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030814.
VAR_SEQ 159 180 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030815.
VAR_SEQ 180 180 W -> CLSWMCKTLNDPGSQG (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_030816.
VARIANT 126 126 P -> S (in dbSNP:rs1058411).
/FTId=VAR_038434.
MUTAGEN 147 147 C->A: Abolishes binding to ubiquitin.
Abolishes binding to ubiquitin; when
associated with A-150.
{ECO:0000269|PubMed:22266823,
ECO:0000269|PubMed:22396592,
ECO:0000269|PubMed:22705371}.
MUTAGEN 150 150 C->A: Abolishes binding to ubiquitin;
when associated with A-147.
{ECO:0000269|PubMed:22266823,
ECO:0000269|PubMed:22396592}.
MUTAGEN 164 164 D->A: Abolishes binding to ubiquitin.
{ECO:0000269|PubMed:22705371}.
MUTAGEN 170 170 C->A: Abolishes binding to ubiquitin.
{ECO:0000269|PubMed:22343915}.
CONFLICT 1 1 M -> V (in Ref. 5; AAH66360).
{ECO:0000305}.
CONFLICT 17 17 R -> P (in Ref. 1; BAB70965, 4; EAW56125
and 5; AAH66360/AAI03993). {ECO:0000305}.
CONFLICT 146 146 S -> N (in Ref. 2; AAQ04817).
{ECO:0000305}.
CONFLICT 176 177 ED -> KN (in Ref. 2; AAQ04817).
{ECO:0000305}.
STRAND 145 147 {ECO:0000244|PDB:2MUQ}.
TURN 148 150 {ECO:0000244|PDB:3WWQ}.
HELIX 160 173 {ECO:0000244|PDB:3WWQ}.
STRAND 174 176 {ECO:0000244|PDB:3WWQ}.
SEQUENCE 180 AA; 19869 MW; D8FC889A20AF732F CRC64;
MEAARRPRLG LSRRRPRPAG GPSGGRPWFL LGGDERERLW AELLRTVSPE LILDHEVPSL
PAFPGQEPRC GPEPTEVFTV GPKTFSWTPF PPDLWGPGRS YRLLHGAGGH LESPARSLPQ
RPAPDPCRAP RVEQQPSVEG AAALRSCPMC QKEFAPRLTQ LDVDSHLAQC LAESTEDVTW


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FANCA_MOUSE ELISA Kit FOR Fanconi anemia group A protein homolog; organism: Mouse; gene name: Fanca 96T
EIAAB14412 FAA,FACA,FANCA,FANCH,Fanconi anemia group A protein,Homo sapiens,Human,Protein FACA
FANCC FANCA Gene Fanconi anemia, complementation group A
201-20-1976 FANCA{Fanconi anemia, complementation group A}rabbit.pAb 0.2ml
201-20-1977 FANCA{Homo sapiens Fanconi anemia, complementation group A}rabbit.pAb 0.2ml
GTX25065 Fanconi anemia group C protein 100 µg
GTX30142 Fanconi anemia group D2 protein 50 µl
E3972h Human Fanconi Anemia Associated Protein, 24 kDa EL 96T
GTX25360 Fanconi anemia group D2 protein 100 µl
NB100-411 Fanconi anemia group D2 protein 0.1 ml
GTX70315 Fanconi anemia group C protein 0.1 mg
GTX70299 Fanconi anemia group D2 protein 0.1 mg
AP06115PU-N Fanconi anemia group D2 protein 100 µg
FAP20_RAT Rat ELISA Kit FOR Fanconi anemia-associated protein of 20 kDa 96T
GTX25064 Fanconi anemia group E protein 100 µg
GTX25063 Fanconi anemia group A protein 100 µg
NB100-182 Fanconi anemia group D2 protein 0.05 ml


 

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