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Protein

Fanconi anemia core complex-associated protein 20

Gene

FAAP20

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 REV1.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri144 – 17431UBZ-typeAdd
BLAST

GO - Molecular functioni

  • K63-linked polyubiquitin binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • polyubiquitin binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • interstrand cross-link repair Source: UniProtKB
  • translesion synthesis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Fanconi anemia core complex-associated protein 20Imported
Alternative name(s):
FANCA-associated protein of 20 kDa1 Publication
Fanconi anemia-associated protein of 20 kDa1 Publication
Gene namesi
Name:FAAP201 PublicationImported
Synonyms:C1orf86
ORF Names:FP7162
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:26428. FAAP20.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: HPA
  • chromosome Source: UniProtKB
  • Fanconi anaemia nuclear complex Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi147 – 1471C → A: Abolishes binding to ubiquitin. Abolishes binding to ubiquitin; when associated with A-150. 3 Publications
Mutagenesisi150 – 1501C → A: Abolishes binding to ubiquitin; when associated with A-147. 2 Publications
Mutagenesisi164 – 1641D → A: Abolishes binding to ubiquitin. 1 Publication
Mutagenesisi170 – 1701C → A: Abolishes binding to ubiquitin. 1 Publication

Organism-specific databases

PharmGKBiPA142672470.

Polymorphism and mutation databases

BioMutaiFAAP20.
DMDMi166991449.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 180180Fanconi anemia core complex-associated protein 20PRO_0000316882Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei113 – 1131PhosphoserineCombined sources
Modified residuei137 – 1371PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6NZ36.
PaxDbiQ6NZ36.
PeptideAtlasiQ6NZ36.
PRIDEiQ6NZ36.

PTM databases

iPTMnetiQ6NZ36.

Expressioni

Gene expression databases

BgeeiQ6NZ36.
CleanExiHS_C1orf86.
ExpressionAtlasiQ6NZ36. baseline and differential.
GenevisibleiQ6NZ36. HS.

Organism-specific databases

HPAiHPA038829.

Interactioni

Subunit structurei

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).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
REV1Q9UBZ92EBI-2817693,EBI-7353917

GO - Molecular functioni

  • K63-linked polyubiquitin binding Source: UniProtKB
  • polyubiquitin binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi128288. 23 interactions.
DIPiDIP-59917N.
IntActiQ6NZ36. 5 interactions.
STRINGi9606.ENSP00000367808.

Structurei

Secondary structure

1
180
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi145 – 1473Combined sources
Turni148 – 1503Combined sources
Helixi160 – 17314Combined sources
Beta strandi174 – 1763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MUQNMR-A140-180[»]
2MURNMR-A140-180[»]
3WWQX-ray1.90C/F/I/L142-180[»]
ProteinModelPortaliQ6NZ36.
SMRiQ6NZ36. Positions 140-180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The UBZ-type zinc finger binds both 'Lys-48'- and 'Lys-63'-linked polyubiquitin with preference for 'Lys-63'-linked polyubiquitin.4 Publications

Sequence similaritiesi

Contains 1 UBZ-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri144 – 17431UBZ-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410J1M8. Eukaryota.
ENOG410Y5B2. LUCA.
HOGENOMiHOG000111230.
HOVERGENiHBG107553.
InParanoidiQ6NZ36.
OMAiGSKTFSW.
PhylomeDBiQ6NZ36.
TreeFamiTF336358.

Family and domain databases

InterProiIPR031491. FANCA_interact.
IPR031490. UBZ_FAAP20.
[Graphical view]
PfamiPF15751. FANCA_interact. 1 hit.
PF15750. UBZ_FAAP20. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6NZ36-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEAARRPRLG LSRRRPRPAG GPSGGRPWFL LGGDERERLW AELLRTVSPE
60 70 80 90 100
LILDHEVPSL PAFPGQEPRC GPEPTEVFTV GPKTFSWTPF PPDLWGPGRS
110 120 130 140 150
YRLLHGAGGH LESPARSLPQ RPAPDPCRAP RVEQQPSVEG AAALRSCPMC
160 170 180
QKEFAPRLTQ LDVDSHLAQC LAESTEDVTW
Length:180
Mass (Da):19,869
Last modified:February 5, 2008 - v2
Checksum:iD8FC889A20AF732F
GO
Isoform 2 (identifier: Q6NZ36-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEAARRPRLGLSRRRPRPAGG → MCGPEHLLCC...ADNLRTGRTR

Show »
Length:283
Mass (Da):31,209
Checksum:i8FF8997665B31D6C
GO
Isoform 3 (identifier: Q6NZ36-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MEAARRPRLGLSRRRPRPAGG → MNFGLEKTHF...ADNLRTGRTR

Note: No experimental confirmation available.
Show »
Length:230
Mass (Da):25,473
Checksum:i2727C4B213BE0838
GO
Isoform 4 (identifier: Q6NZ36-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     180-180: W → CLSWMCKTLNDPGSQG

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:195
Mass (Da):21,404
Checksum:i365E26323B5A7EDB
GO
Isoform 5 (identifier: Q6NZ36-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     158-158: L → YFNSRPHLCPAGS
     159-180: Missing.

Note: No experimental confirmation available.
Show »
Length:170
Mass (Da):18,742
Checksum:i12370B74D47CFB68
GO
Isoform 6 (identifier: Q6NZ36-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     22-180: PSGGRPWFLL...LAESTEDVTW → SPGAARSPLK...PCARRSSPPG

Note: Gene prediction based on EST data.
Show »
Length:112
Mass (Da):11,834
Checksum:i71D4D88F8542A1BD
GO

Sequence cautioni

The sequence AAH66360.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 11M → V in AAH66360 (PubMed:15489334).Curated
Sequence conflicti17 – 171R → P in BAB70965 (PubMed:14702039).Curated
Sequence conflicti17 – 171R → P in EAW56125 (Ref. 4) Curated
Sequence conflicti17 – 171R → P in AAH66360 (PubMed:15489334).Curated
Sequence conflicti17 – 171R → P in AAI03993 (PubMed:15489334).Curated
Sequence conflicti146 – 1461S → N in AAQ04817 (PubMed:15498874).Curated
Sequence conflicti176 – 1772ED → KN in AAQ04817 (PubMed:15498874).Curated
Isoform 2 (identifier: Q6NZ36-2)
Sequence conflicti65 – 651R → H in BAC86730 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti126 – 1261P → S.
Corresponds to variant rs1058411 [ dbSNP | Ensembl ].
VAR_038434

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121MEAAR…RPAGG → MCGPEHLLCCPKDLAMFPRQ LSLTACLPGTPVSHKCHHIW LWVGVPAWHPRASRCGGAQP SSWLRQKAARAFWLSLPAAK LRHHSSRWLRRSGAFSSGST LKPPPSPSPAPLCHADNLRT GRTR in isoform 2. 1 PublicationVSP_030812Add
BLAST
Alternative sequencei1 – 2121MEAAR…RPAGG → MNFGLEKTHFHCARVSPNQK LFSNKAKLRHHSSRWLRRSG AFSSGSTLKPPPSPSPAPLC HADNLRTGRTR in isoform 3. 1 PublicationVSP_030813Add
BLAST
Alternative sequencei22 – 180159PSGGR…EDVTW → SPGAARSPLKSSLSDPRPFP GHPFRRTCGARAVPTGCFTG QEGTWNPPPGPCPSARHLIP AGPPGWSSSRLWRVPRPCAA APCARRSSPPG in isoform 6. CuratedVSP_047264Add
BLAST
Alternative sequencei158 – 1581L → YFNSRPHLCPAGS in isoform 5. 1 PublicationVSP_030814
Alternative sequencei159 – 18022Missing in isoform 5. 1 PublicationVSP_030815Add
BLAST
Alternative sequencei180 – 1801W → CLSWMCKTLNDPGSQG in isoform 4. 2 PublicationsVSP_030816

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055593 mRNA. Translation: BAB70965.1.
AK126870 mRNA. Translation: BAC86730.1.
AF461903 mRNA. Translation: AAQ04817.1.
AL590822 Genomic DNA. No translation available.
CH471183 Genomic DNA. Translation: EAW56125.1.
BC066360 mRNA. Translation: AAH66360.1. Different initiation.
BC078145 mRNA. No translation available.
BC103992 mRNA. Translation: AAI03993.1.
CCDSiCCDS38.2. [Q6NZ36-1]
CCDS57965.1. [Q6NZ36-6]
CCDS72687.1. [Q6NZ36-5]
RefSeqiNP_001243874.1. NM_001256945.1.
NP_001243875.1. NM_001256946.1.
NP_001243876.1. NM_001256947.1.
NP_001269599.1. NM_001282670.1. [Q6NZ36-2]
NP_001269600.1. NM_001282671.1.
NP_001269601.1. NM_001282672.1.
NP_001269602.1. NM_001282673.1.
NP_872339.2. NM_182533.2.
UniGeneiHs.107101.

Genome annotation databases

EnsembliENST00000378543; ENSP00000367804; ENSG00000162585. [Q6NZ36-6]
ENST00000378546; ENSP00000367808; ENSG00000162585. [Q6NZ36-1]
ENST00000400918; ENSP00000383709; ENSG00000162585. [Q6NZ36-5]
ENST00000414253; ENSP00000410450; ENSG00000162585. [Q6NZ36-4]
GeneIDi199990.
KEGGihsa:199990.
UCSCiuc001aiy.4. human. [Q6NZ36-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055593 mRNA. Translation: BAB70965.1.
AK126870 mRNA. Translation: BAC86730.1.
AF461903 mRNA. Translation: AAQ04817.1.
AL590822 Genomic DNA. No translation available.
CH471183 Genomic DNA. Translation: EAW56125.1.
BC066360 mRNA. Translation: AAH66360.1. Different initiation.
BC078145 mRNA. No translation available.
BC103992 mRNA. Translation: AAI03993.1.
CCDSiCCDS38.2. [Q6NZ36-1]
CCDS57965.1. [Q6NZ36-6]
CCDS72687.1. [Q6NZ36-5]
RefSeqiNP_001243874.1. NM_001256945.1.
NP_001243875.1. NM_001256946.1.
NP_001243876.1. NM_001256947.1.
NP_001269599.1. NM_001282670.1. [Q6NZ36-2]
NP_001269600.1. NM_001282671.1.
NP_001269601.1. NM_001282672.1.
NP_001269602.1. NM_001282673.1.
NP_872339.2. NM_182533.2.
UniGeneiHs.107101.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MUQNMR-A140-180[»]
2MURNMR-A140-180[»]
3WWQX-ray1.90C/F/I/L142-180[»]
ProteinModelPortaliQ6NZ36.
SMRiQ6NZ36. Positions 140-180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128288. 23 interactions.
DIPiDIP-59917N.
IntActiQ6NZ36. 5 interactions.
STRINGi9606.ENSP00000367808.

PTM databases

iPTMnetiQ6NZ36.

Polymorphism and mutation databases

BioMutaiFAAP20.
DMDMi166991449.

Proteomic databases

MaxQBiQ6NZ36.
PaxDbiQ6NZ36.
PeptideAtlasiQ6NZ36.
PRIDEiQ6NZ36.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378543; ENSP00000367804; ENSG00000162585. [Q6NZ36-6]
ENST00000378546; ENSP00000367808; ENSG00000162585. [Q6NZ36-1]
ENST00000400918; ENSP00000383709; ENSG00000162585. [Q6NZ36-5]
ENST00000414253; ENSP00000410450; ENSG00000162585. [Q6NZ36-4]
GeneIDi199990.
KEGGihsa:199990.
UCSCiuc001aiy.4. human. [Q6NZ36-1]

Organism-specific databases

CTDi199990.
GeneCardsiC1orf86.
HGNCiHGNC:26428. FAAP20.
HPAiHPA038829.
MIMi615183. gene.
neXtProtiNX_Q6NZ36.
PharmGKBiPA142672470.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J1M8. Eukaryota.
ENOG410Y5B2. LUCA.
HOGENOMiHOG000111230.
HOVERGENiHBG107553.
InParanoidiQ6NZ36.
OMAiGSKTFSW.
PhylomeDBiQ6NZ36.
TreeFamiTF336358.

Enzyme and pathway databases

ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.

Miscellaneous databases

ChiTaRSiC1orf86. human.
GenomeRNAii199990.
PROiQ6NZ36.
SOURCEiSearch...

Gene expression databases

BgeeiQ6NZ36.
CleanExiHS_C1orf86.
ExpressionAtlasiQ6NZ36. baseline and differential.
GenevisibleiQ6NZ36. HS.

Family and domain databases

InterProiIPR031491. FANCA_interact.
IPR031490. UBZ_FAAP20.
[Graphical view]
PfamiPF15751. FANCA_interact. 1 hit.
PF15750. UBZ_FAAP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
    Tissue: Amygdala and Synovial cell.
  2. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  3. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 152-180 (ISOFORM 5).
    Tissue: Hypothalamus.
  6. "FAAP20: a novel ubiquitin-binding FA nuclear core-complex protein required for functional integrity of the FA-BRCA DNA repair pathway."
    Ali A.M., Pradhan A., Singh T.R., Du C., Li J., Wahengbam K., Grassman E., Auerbach A.D., Pang Q., Meetei A.R.
    Blood 119:3285-3294(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE FA COMPLEX, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH FANCA, MUTAGENESIS OF CYS-170.
  7. "A ubiquitin-binding protein, FAAP20, links RNF8-mediated ubiquitination to the Fanconi anemia DNA repair network."
    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.
    Mol. Cell 47:61-75(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE FA COMPLEX, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH FANCA, MUTAGENESIS OF CYS-147 AND ASP-164.
  8. "Regulation of Rev1 by the Fanconi anemia core complex."
    Kim H., Yang K., Dejsuphong D., D'Andrea A.D.
    Nat. Struct. Mol. Biol. 19:164-170(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE FA COMPLEX, DOMAIN, INTERACTION WITH REV1, MUTAGENESIS OF CYS-147 AND CYS-150.
  9. "Fanconi anemia (FA) binding protein FAAP20 stabilizes FA complementation group A (FANCA) and participates in interstrand cross-link repair."
    Leung J.W., Wang Y., Fong K.W., Huen M.S., Li L., Chen J.
    Proc. Natl. Acad. Sci. U.S.A. 109:4491-4496(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE FA COMPLEX, DOMAIN, INTERACTION WITH FANCA, MUTAGENESIS OF CYS-147 AND CYS-150.
  10. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiFAP20_HUMAN
AccessioniPrimary (citable) accession number: Q6NZ36
Secondary accession number(s): A6PW39
, A6PW40, A6PW41, A8MQT6, F2Z2L4, Q6ZT64, Q71M24, Q96ND7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 5, 2008
Last modified: July 6, 2016
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

According to a report, ubiquitin-binding is dispensable for function (PubMed:22396592). However, such data are not confirmed by PubMed:22705371.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.