FAP20_HUMAN
ID FAP20_HUMAN Reviewed; 180 AA.
AC Q6NZ36; A6PW39; A6PW40; A6PW41; A8MQT6; F2Z2L4; Q6ZT64; Q71M24; Q96ND7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Fanconi anemia core complex-associated protein 20 {ECO:0000312|HGNC:HGNC:26428};
DE AltName: Full=FANCA-associated protein of 20 kDa {ECO:0000303|PubMed:22343915};
DE AltName: Full=Fanconi anemia-associated protein of 20 kDa {ECO:0000303|PubMed:22343915};
GN Name=FAAP20 {ECO:0000303|PubMed:22343915, ECO:0000312|HGNC:HGNC:26428};
GN Synonyms=C1orf86; ORFNames=FP7162;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Amygdala, and Synovial cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 152-180 (ISOFORM 5).
RC TISSUE=Hypothalamus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE FA COMPLEX, SUBCELLULAR LOCATION, DOMAIN,
RP INTERACTION WITH FANCA, AND MUTAGENESIS OF CYS-170.
RX PubMed=22343915; DOI=10.1182/blood-2011-10-385963;
RA Ali A.M., Pradhan A., Singh T.R., Du C., Li J., Wahengbam K., Grassman E.,
RA Auerbach A.D., Pang Q., Meetei A.R.;
RT "FAAP20: a novel ubiquitin-binding FA nuclear core-complex protein required
RT for functional integrity of the FA-BRCA DNA repair pathway.";
RL Blood 119:3285-3294(2012).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE FA COMPLEX, SUBCELLULAR LOCATION, DOMAIN,
RP INTERACTION WITH FANCA, AND MUTAGENESIS OF CYS-147 AND ASP-164.
RX PubMed=22705371; DOI=10.1016/j.molcel.2012.05.026;
RA Yan Z., Guo R., Paramasivam M., Shen W., Ling C., Fox D. III, Wang Y.,
RA Oostra A.B., Kuehl J., Lee D.Y., Takata M., Hoatlin M.E., Schindler D.,
RA Joenje H., de Winter J.P., Li L., Seidman M.M., Wang W.;
RT "A ubiquitin-binding protein, FAAP20, links RNF8-mediated ubiquitination to
RT the Fanconi anemia DNA repair network.";
RL Mol. Cell 47:61-75(2012).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE FA COMPLEX, DOMAIN, INTERACTION WITH REV1,
RP AND MUTAGENESIS OF CYS-147 AND CYS-150.
RX PubMed=22266823; DOI=10.1038/nsmb.2222;
RA Kim H., Yang K., Dejsuphong D., D'Andrea A.D.;
RT "Regulation of Rev1 by the Fanconi anemia core complex.";
RL Nat. Struct. Mol. Biol. 19:164-170(2012).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE FA COMPLEX, DOMAIN, INTERACTION WITH FANCA,
RP AND MUTAGENESIS OF CYS-147 AND CYS-150.
RX PubMed=22396592; DOI=10.1073/pnas.1118720109;
RA Leung J.W., Wang Y., Fong K.W., Huen M.S., Li L., Chen J.;
RT "Fanconi anemia (FA) binding protein FAAP20 stabilizes FA complementation
RT group A (FANCA) and participates in interstrand cross-link repair.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:4491-4496(2012).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-137, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Component of the Fanconi anemia (FA) complex required to
CC recruit the FA complex to DNA interstrand cross-links (ICLs) and
CC promote ICLs repair. Following DNA damage recognizes and binds 'Lys-
CC 63'-linked ubiquitin generated by RNF8 at ICLs and recruits other
CC components of the FA complex. Promotes translesion synthesis via
CC interaction with REV1. {ECO:0000269|PubMed:22266823,
CC ECO:0000269|PubMed:22343915, ECO:0000269|PubMed:22396592,
CC ECO:0000269|PubMed:22705371}.
CC -!- SUBUNIT: Component of the Fanconi anemia (FA) complex. Interacts with
CC FANCA; interaction is direct. Interacts with REV1. Reported to bind
CC monoubiquitinated REV1; however it binds better to non-ubiquitinated
CC REV1 (PubMed:22266823). {ECO:0000269|PubMed:22266823,
CC ECO:0000269|PubMed:22343915, ECO:0000269|PubMed:22396592,
CC ECO:0000269|PubMed:22705371}.
CC -!- INTERACTION:
CC Q6NZ36; Q9UBZ9: REV1; NbExp=2; IntAct=EBI-2817693, EBI-7353917;
CC Q6NZ36-1; O15360: FANCA; NbExp=5; IntAct=EBI-15965017, EBI-81570;
CC Q6NZ36-1; Q920Q2: Rev1; Xeno; NbExp=7; IntAct=EBI-15965017, EBI-2114764;
CC Q6NZ36-4; A0A087WVE9: ARNT2; NbExp=3; IntAct=EBI-12013806, EBI-12808086;
CC Q6NZ36-4; Q86V38: ATN1; NbExp=3; IntAct=EBI-12013806, EBI-11954292;
CC Q6NZ36-4; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-12013806, EBI-953896;
CC Q6NZ36-4; O43186: CRX; NbExp=3; IntAct=EBI-12013806, EBI-748171;
CC Q6NZ36-4; P02489: CRYAA; NbExp=3; IntAct=EBI-12013806, EBI-6875961;
CC Q6NZ36-4; Q8WUE5: CT55; NbExp=3; IntAct=EBI-12013806, EBI-6873363;
CC Q6NZ36-4; Q9GZU7: CTDSP1; NbExp=3; IntAct=EBI-12013806, EBI-751587;
CC Q6NZ36-4; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12013806, EBI-742054;
CC Q6NZ36-4; Q9H596: DUSP21; NbExp=3; IntAct=EBI-12013806, EBI-7357329;
CC Q6NZ36-4; O14908-2: GIPC1; NbExp=3; IntAct=EBI-12013806, EBI-25913156;
CC Q6NZ36-4; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-12013806, EBI-5916454;
CC Q6NZ36-4; Q0VD86: INCA1; NbExp=3; IntAct=EBI-12013806, EBI-6509505;
CC Q6NZ36-4; Q92876: KLK6; NbExp=3; IntAct=EBI-12013806, EBI-2432309;
CC Q6NZ36-4; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-12013806, EBI-11962084;
CC Q6NZ36-4; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-12013806, EBI-10261141;
CC Q6NZ36-4; P80188: LCN2; NbExp=3; IntAct=EBI-12013806, EBI-11911016;
CC Q6NZ36-4; P25791-3: LMO2; NbExp=3; IntAct=EBI-12013806, EBI-11959475;
CC Q6NZ36-4; Q9P2M1: LRP2BP; NbExp=3; IntAct=EBI-12013806, EBI-18273118;
CC Q6NZ36-4; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12013806, EBI-16439278;
CC Q6NZ36-4; Q70IA6: MOB2; NbExp=3; IntAct=EBI-12013806, EBI-2558739;
CC Q6NZ36-4; Q8NI38: NFKBID; NbExp=6; IntAct=EBI-12013806, EBI-10271199;
CC Q6NZ36-4; Q13153: PAK1; NbExp=3; IntAct=EBI-12013806, EBI-1307;
CC Q6NZ36-4; Q99471: PFDN5; NbExp=3; IntAct=EBI-12013806, EBI-357275;
CC Q6NZ36-4; Q9NQX1-2: PRDM5; NbExp=3; IntAct=EBI-12013806, EBI-12859340;
CC Q6NZ36-4; Q04864-2: REL; NbExp=3; IntAct=EBI-12013806, EBI-10829018;
CC Q6NZ36-4; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-12013806, EBI-748601;
CC Q6NZ36-4; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-12013806, EBI-748621;
CC Q6NZ36-4; Q8IYF3-3: TEX11; NbExp=3; IntAct=EBI-12013806, EBI-11523345;
CC Q6NZ36-4; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-12013806, EBI-492476;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22343915,
CC ECO:0000269|PubMed:22705371}. Chromosome {ECO:0000305|PubMed:22343915,
CC ECO:0000305|PubMed:22705371}. Note=Following DNA damage, recruited to
CC DNA interstrand cross-links (ICLs) sites by binding to ubiquitin
CC generated by RNF8. {ECO:0000269|PubMed:22705371}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q6NZ36-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6NZ36-2; Sequence=VSP_030812;
CC Name=3;
CC IsoId=Q6NZ36-3; Sequence=VSP_030813;
CC Name=4;
CC IsoId=Q6NZ36-4; Sequence=VSP_030816;
CC Name=5;
CC IsoId=Q6NZ36-5; Sequence=VSP_030814, VSP_030815;
CC Name=6;
CC IsoId=Q6NZ36-6; Sequence=VSP_047264;
CC -!- DOMAIN: The UBZ2-type zinc finger binds both 'Lys-48'- and 'Lys-63'-
CC linked polyubiquitin with preference for 'Lys-63'-linked polyubiquitin.
CC {ECO:0000255|PROSITE-ProRule:PRU01254, ECO:0000269|PubMed:22266823,
CC ECO:0000269|PubMed:22343915, ECO:0000269|PubMed:22396592,
CC ECO:0000269|PubMed:22705371}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- CAUTION: According to a report, ubiquitin-binding is dispensable for
CC function (PubMed:22396592). However, such data are not confirmed by
CC PubMed:22705371. {ECO:0000305|PubMed:22396592}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH66360.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK055593; BAB70965.1; -; mRNA.
DR EMBL; AK126870; BAC86730.1; -; mRNA.
DR EMBL; AF461903; AAQ04817.1; -; mRNA.
DR EMBL; AL590822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56125.1; -; Genomic_DNA.
DR EMBL; BC066360; AAH66360.1; ALT_INIT; mRNA.
DR EMBL; BC078145; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC103992; AAI03993.1; -; mRNA.
DR CCDS; CCDS38.2; -. [Q6NZ36-1]
DR CCDS; CCDS57965.1; -. [Q6NZ36-6]
DR CCDS; CCDS72687.1; -. [Q6NZ36-5]
DR RefSeq; NP_001243874.1; NM_001256945.1.
DR RefSeq; NP_001243875.1; NM_001256946.1.
DR RefSeq; NP_001243876.1; NM_001256947.1. [Q6NZ36-6]
DR RefSeq; NP_001269599.1; NM_001282670.1. [Q6NZ36-2]
DR RefSeq; NP_001269600.1; NM_001282671.1.
DR RefSeq; NP_001269601.1; NM_001282672.1.
DR RefSeq; NP_001269602.1; NM_001282673.1. [Q6NZ36-5]
DR RefSeq; NP_872339.2; NM_182533.2. [Q6NZ36-1]
DR PDB; 2MUQ; NMR; -; A=140-180.
DR PDB; 2MUR; NMR; -; A=140-180.
DR PDB; 3WWQ; X-ray; 1.90 A; C/F/I/L=142-180.
DR PDBsum; 2MUQ; -.
DR PDBsum; 2MUR; -.
DR PDBsum; 3WWQ; -.
DR AlphaFoldDB; Q6NZ36; -.
DR SMR; Q6NZ36; -.
DR BioGRID; 128288; 71.
DR ComplexPortal; CPX-6263; Fanconi anemia ubiquitin ligase complex.
DR DIP; DIP-59917N; -.
DR IntAct; Q6NZ36; 42.
DR MINT; Q6NZ36; -.
DR iPTMnet; Q6NZ36; -.
DR BioMuta; FAAP20; -.
DR DMDM; 166991449; -.
DR EPD; Q6NZ36; -.
DR jPOST; Q6NZ36; -.
DR MassIVE; Q6NZ36; -.
DR MaxQB; Q6NZ36; -.
DR PaxDb; Q6NZ36; -.
DR PeptideAtlas; Q6NZ36; -.
DR PRIDE; Q6NZ36; -.
DR ProteomicsDB; 23749; -.
DR ProteomicsDB; 66786; -. [Q6NZ36-1]
DR ProteomicsDB; 66787; -. [Q6NZ36-2]
DR ProteomicsDB; 66788; -. [Q6NZ36-3]
DR ProteomicsDB; 66789; -. [Q6NZ36-4]
DR ProteomicsDB; 66790; -. [Q6NZ36-5]
DR Antibodypedia; 52488; 60 antibodies from 14 providers.
DR DNASU; 199990; -.
DR Ensembl; ENST00000378543.2; ENSP00000367804.2; ENSG00000162585.17. [Q6NZ36-6]
DR Ensembl; ENST00000378546.9; ENSP00000367808.4; ENSG00000162585.17. [Q6NZ36-1]
DR Ensembl; ENST00000400918.7; ENSP00000383709.3; ENSG00000162585.17. [Q6NZ36-5]
DR Ensembl; ENST00000414253.5; ENSP00000410450.1; ENSG00000162585.17. [Q6NZ36-4]
DR GeneID; 199990; -.
DR KEGG; hsa:199990; -.
DR MANE-Select; ENST00000378546.9; ENSP00000367808.4; NM_182533.4; NP_872339.3.
DR UCSC; uc001aiy.4; human. [Q6NZ36-1]
DR CTD; 199990; -.
DR DisGeNET; 199990; -.
DR GeneCards; FAAP20; -.
DR HGNC; HGNC:26428; FAAP20.
DR HPA; ENSG00000162585; Low tissue specificity.
DR MIM; 615183; gene.
DR neXtProt; NX_Q6NZ36; -.
DR OpenTargets; ENSG00000162585; -.
DR PharmGKB; PA142672470; -.
DR VEuPathDB; HostDB:ENSG00000162585; -.
DR GeneTree; ENSGT00390000010531; -.
DR HOGENOM; CLU_2145000_0_0_1; -.
DR InParanoid; Q6NZ36; -.
DR OMA; CARPWAE; -.
DR OrthoDB; 1051670at2759; -.
DR PhylomeDB; Q6NZ36; -.
DR TreeFam; TF336358; -.
DR PathwayCommons; Q6NZ36; -.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR SignaLink; Q6NZ36; -.
DR BioGRID-ORCS; 199990; 110 hits in 1052 CRISPR screens.
DR ChiTaRS; FAAP20; human.
DR GenomeRNAi; 199990; -.
DR Pharos; Q6NZ36; Tbio.
DR PRO; PR:Q6NZ36; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6NZ36; protein.
DR Bgee; ENSG00000162585; Expressed in adenohypophysis and 169 other tissues.
DR ExpressionAtlas; Q6NZ36; baseline and differential.
DR Genevisible; Q6NZ36; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0140036; F:ubiquitin-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:ComplexPortal.
DR GO; GO:0019985; P:translesion synthesis; IMP:UniProtKB.
DR InterPro; IPR031491; FANCA_interact.
DR InterPro; IPR031490; UBZ2_FAAP20.
DR Pfam; PF15751; FANCA_interact; 1.
DR Pfam; PF15750; UBZ_FAAP20; 1.
DR PROSITE; PS51906; ZF_UBZ2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; DNA damage; DNA repair;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..180
FT /note="Fanconi anemia core complex-associated protein 20"
FT /id="PRO_0000316882"
FT ZN_FING 144..180
FT /note="UBZ2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01254"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..21
FT /note="MEAARRPRLGLSRRRPRPAGG -> MCGPEHLLCCPKDLAMFPRQLSLTACL
FT PGTPVSHKCHHIWLWVGVPAWHPRASRCGGAQPSSWLRQKAARAFWLSLPAAKLRHHSS
FT RWLRRSGAFSSGSTLKPPPSPSPAPLCHADNLRTGRTR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_030812"
FT VAR_SEQ 1..21
FT /note="MEAARRPRLGLSRRRPRPAGG -> MNFGLEKTHFHCARVSPNQKLFSNKAK
FT LRHHSSRWLRRSGAFSSGSTLKPPPSPSPAPLCHADNLRTGRTR (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_030813"
FT VAR_SEQ 22..180
FT /note="PSGGRPWFLLGGDERERLWAELLRTVSPELILDHEVPSLPAFPGQEPRCGPE
FT PTEVFTVGPKTFSWTPFPPDLWGPGRSYRLLHGAGGHLESPARSLPQRPAPDPCRAPRV
FT EQQPSVEGAAALRSCPMCQKEFAPRLTQLDVDSHLAQCLAESTEDVTW -> SPGAARS
FT PLKSSLSDPRPFPGHPFRRTCGARAVPTGCFTGQEGTWNPPPGPCPSARHLIPAGPPGW
FT SSSRLWRVPRPCAAAPCARRSSPPG (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_047264"
FT VAR_SEQ 158
FT /note="L -> YFNSRPHLCPAGS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030814"
FT VAR_SEQ 159..180
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030815"
FT VAR_SEQ 180
FT /note="W -> CLSWMCKTLNDPGSQG (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030816"
FT VARIANT 126
FT /note="P -> S (in dbSNP:rs1058411)"
FT /id="VAR_038434"
FT MUTAGEN 147
FT /note="C->A: Abolishes binding to ubiquitin. Abolishes
FT binding to ubiquitin; when associated with A-150."
FT /evidence="ECO:0000269|PubMed:22266823,
FT ECO:0000269|PubMed:22396592, ECO:0000269|PubMed:22705371"
FT MUTAGEN 150
FT /note="C->A: Abolishes binding to ubiquitin; when
FT associated with A-147."
FT /evidence="ECO:0000269|PubMed:22266823,
FT ECO:0000269|PubMed:22396592"
FT MUTAGEN 164
FT /note="D->A: Abolishes binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:22705371"
FT MUTAGEN 170
FT /note="C->A: Abolishes binding to ubiquitin."
FT /evidence="ECO:0000269|PubMed:22343915"
FT CONFLICT 1
FT /note="M -> V (in Ref. 5; AAH66360)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="R -> P (in Ref. 1; BAB70965, 4; EAW56125 and 5;
FT AAH66360/AAI03993)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="S -> N (in Ref. 2; AAQ04817)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..177
FT /note="ED -> KN (in Ref. 2; AAQ04817)"
FT /evidence="ECO:0000305"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2MUQ"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:3WWQ"
FT HELIX 160..173
FT /evidence="ECO:0007829|PDB:3WWQ"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3WWQ"
FT CONFLICT Q6NZ36-2:65
FT /note="R -> H (in Ref. 1; BAC86730)"
FT /evidence="ECO:0000305"
SQ 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
