Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fanconi-associated nuclease 1

Gene

FAN1

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

Functioni

Nuclease required for the repair of DNA interstrand cross-links (ICL) recruited at sites of DNA damage by monoubiquitinated FANCD2. Specifically involved in repair of ICL-induced DNA breaks by being required for efficient homologous recombination, probably in the resolution of homologous recombination intermediates (PubMed:20603015, PubMed:20603016, PubMed:20603073, PubMed:20671156, PubMed:24981866, PubMed:25430771). Not involved in DNA double-strand breaks resection (PubMed:20603015, PubMed:20603016). Acts as a 5'-3' exonuclease that anchors at a cut end of DNA and cleaves DNA successively at every third nucleotide, allowing to excise an ICL from one strand through flanking incisions. Probably keeps excising with 3'-flap annealing until it reaches and unhooks the ICL (PubMed:25430771). Acts at sites that have a 5'-terminal phosphate anchor at a nick or a 1- or 2-nucleotide flap and is augmented by a 3' flap (PubMed:25430771). Also has endonuclease activity toward 5'-flaps (PubMed:20603015, PubMed:20603016, PubMed:24981866).7 Publications

Catalytic activityi

Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.2 Publications

Cofactori

Mn2+1 Publication, Mg2+1 PublicationNote: Binds 2 magnesium or manganese ions per subunit.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi834 – 8341Magnesium or manganese 2By similarity
Metal bindingi960 – 9601Magnesium or manganese 11 Publication
Metal bindingi960 – 9601Magnesium or manganese 21 Publication
Metal bindingi975 – 9751Magnesium or manganese 11 Publication
Metal bindingi976 – 9761Magnesium or manganese 1; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri41 – 6727UBZ-typeAdd
BLAST

GO - Molecular functioni

  • 5'-3' exonuclease activity Source: UniProtKB
  • 5'-flap endonuclease activity Source: UniProtKB
  • flap-structured DNA binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • phosphodiesterase I activity Source: UniProtKB-EC
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

  • DNA repair Source: UniProtKB
  • double-strand break repair via homologous recombination Source: UniProtKB
  • interstrand cross-link repair Source: UniProtKB
  • nucleotide-excision repair Source: UniProtKB
  • nucleotide-excision repair, DNA incision Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Fanconi-associated nuclease 13 Publications (EC:3.1.21.-3 Publications, EC:3.1.4.12 Publications)
Alternative name(s):
FANCD2/FANCI-associated nuclease 13 Publications
Short name:
hFAN11 Publication
Myotubularin-related protein 15
Gene namesi
Name:FAN11 Publication
Synonyms:KIAA10181 Publication, MTMR15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:29170. FAN1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • intercellular bridge Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Interstitial nephritis, karyomegalic (KMIN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare kidney disease characterized by chronic tubulointerstitial nephritis associated with massively enlarged tubular epithelial cell nuclei. The clinical picture is associated with recurrent upper respiratory tract infections in addition to chronic kidney disease beginning in the third decade of life.
See also OMIM:614817
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti871 – 8711C → R in KMIN; partially complement cell survival upon exposure to mitomycin C. 1 Publication
VAR_068958
Natural varianti929 – 9291Q → P in KMIN. 1 Publication
VAR_068959
Natural varianti937 – 9371G → D in KMIN. 1 Publication
VAR_068960
Natural varianti960 – 9601D → N in KMIN. 1 Publication
VAR_068961

Schizophrenia and autism. Schizophrenia is a severe psychiatric disorder characterized by positive, negative, and cognitive symptoms, and it is associated with increased mortality and severely reduced fecundity. Autim is a complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation.Disease susceptibility may be associated with variations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441C → A: Abolishes interaction with monoubiquitinated FANCD2; when associated with A-47. 3 Publications
Mutagenesisi47 – 471C → A: Abolishes interaction with monoubiquitinated FANCD2; when associated with A-44. 2 Publications
Mutagenesisi477 – 4771L → P: Still localized to sites of DNA damage but the strength of the signal is diminished. 1 Publication
Mutagenesisi706 – 7061R → A: Strongly reduced affinity for sites that have a 5'-terminal phosphate anchor at a flap of 1 nucleotide; when associated with A-952. 1 Publication
Mutagenesisi864 – 8641Q → A: Loss of nuclease activity; when associated with A-960; A-975 and A-977. 1 Publication
Mutagenesisi952 – 9521R → A: Strongly reduced affinity for sites that have a 5'-terminal phosphate anchor at a flap of 1 nucleotide; when associated with A-706. 1 Publication
Mutagenesisi960 – 9601D → A: Loss of nuclease activity. Loss of nuclease activity; when associated with A-864; A-975 and A-977. 3 Publications
Mutagenesisi975 – 9751E → A: Loss of nuclease activity; when associated with A-864; A-960 and A-977. 1 Publication
Mutagenesisi977 – 9771K → A: Loss of nuclease activity; when associated with A-864; A-960 and A-975. 2 Publications
Mutagenesisi981 – 9822DR → AA: Loss of nuclease activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiFAN1.
MIMi614817. phenotype.
Orphaneti401996. Karyomegalic interstitial nephritis.
PharmGKBiPA165478601.

Polymorphism and mutation databases

BioMutaiFAN1.
DMDMi160410012.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10171017Fanconi-associated nuclease 1PRO_0000311224Add
BLAST

Post-translational modificationi

Ubiquitinated and degraded during mitotic exit by the APC/C-Cdh1 complex.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ9Y2M0.
PaxDbiQ9Y2M0.
PRIDEiQ9Y2M0.

PTM databases

DEPODiQ9Y2M0.
PhosphoSiteiQ9Y2M0.

Expressioni

Gene expression databases

BgeeiQ9Y2M0.
CleanExiHS_MTMR15.
ExpressionAtlasiQ9Y2M0. baseline and differential.
GenevisibleiQ9Y2M0. HS.

Organism-specific databases

HPAiHPA041383.
HPA048198.

Interactioni

Subunit structurei

Interacts with FANCD2 (when monoubiquitinated). Interacts with FANCI, MLH1, MLH3 and PMS2.4 Publications

GO - Molecular functioni

  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116573. 35 interactions.
IntActiQ9Y2M0. 23 interactions.
STRINGi9606.ENSP00000354497.

Structurei

Secondary structure

1
1017
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi374 – 38815Combined sources
Helixi390 – 3934Combined sources
Helixi398 – 40811Combined sources
Helixi412 – 42211Combined sources
Helixi431 – 4333Combined sources
Turni437 – 4393Combined sources
Helixi444 – 4529Combined sources
Beta strandi455 – 4584Combined sources
Helixi459 – 4613Combined sources
Helixi465 – 4717Combined sources
Helixi474 – 48310Combined sources
Helixi493 – 50311Combined sources
Helixi520 – 53112Combined sources
Beta strandi533 – 5375Combined sources
Helixi539 – 55214Combined sources
Helixi554 – 5563Combined sources
Turni557 – 5593Combined sources
Turni563 – 5653Combined sources
Helixi566 – 5683Combined sources
Helixi573 – 5753Combined sources
Helixi577 – 5804Combined sources
Beta strandi595 – 5984Combined sources
Helixi599 – 62022Combined sources
Helixi624 – 63916Combined sources
Turni640 – 6434Combined sources
Helixi645 – 6517Combined sources
Helixi655 – 6584Combined sources
Helixi662 – 67918Combined sources
Helixi683 – 69513Combined sources
Beta strandi697 – 6993Combined sources
Helixi701 – 7033Combined sources
Helixi704 – 71613Combined sources
Helixi722 – 73413Combined sources
Helixi740 – 75415Combined sources
Helixi757 – 7593Combined sources
Helixi761 – 7655Combined sources
Beta strandi778 – 7836Combined sources
Beta strandi786 – 7883Combined sources
Beta strandi796 – 7983Combined sources
Beta strandi804 – 8063Combined sources
Beta strandi811 – 8133Combined sources
Helixi814 – 82411Combined sources
Beta strandi829 – 8324Combined sources
Helixi835 – 85016Combined sources
Beta strandi861 – 8633Combined sources
Turni868 – 8714Combined sources
Helixi874 – 8774Combined sources
Helixi880 – 89112Combined sources
Helixi895 – 90915Combined sources
Beta strandi921 – 9244Combined sources
Helixi925 – 94925Combined sources
Helixi951 – 9555Combined sources
Beta strandi960 – 9645Combined sources
Turni966 – 9683Combined sources
Beta strandi971 – 9777Combined sources
Helixi985 – 99612Combined sources
Beta strandi1001 – 10077Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4REAX-ray3.81A/B373-1017[»]
4REBX-ray4.20A/H373-1017[»]
4RECX-ray2.20A373-1017[»]
4RI8X-ray2.90A/B370-1017[»]
4RI9X-ray2.90A/B370-1017[»]
4RIAX-ray3.00A/B370-1017[»]
4RIBX-ray3.25A/B364-1017[»]
4RICX-ray2.80A/B370-1009[»]
4RIDX-ray3.30A/B370-1009[»]
4RY3X-ray2.80A371-1010[»]
ProteinModelPortaliQ9Y2M0.
SMRiQ9Y2M0. Positions 370-1009.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini895 – 1007113VRR-NUCAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili671 – 69626Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi14 – 229D-boxCurated
Motifi212 – 2143KEN boxCurated

Domaini

The UBZ-type zinc finger specifically binds monoubiquitinated FANCD2.4 Publications
The KEN box and D-box are required for interaction with FZR1/CDH1 and essential for APC(CDH1)-mediated ubiquitination.1 Publication

Sequence similaritiesi

Belongs to the FAN1 family.Curated
Contains 1 UBZ-type zinc finger.Curated
Contains 1 VRR-NUC domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri41 – 6727UBZ-typeAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2143. Eukaryota.
ENOG410XRN3. LUCA.
GeneTreeiENSGT00390000018637.
HOGENOMiHOG000113686.
HOVERGENiHBG108156.
InParanoidiQ9Y2M0.
KOiK15363.
OMAiCFRGEAL.
OrthoDBiEOG7CNZF4.
PhylomeDBiQ9Y2M0.
TreeFamiTF312870.

Family and domain databases

InterProiIPR014883. VRR_NUC.
IPR006642. Znf_Rad18_put.
[Graphical view]
PfamiPF08774. VRR_NUC. 1 hit.
[Graphical view]
SMARTiSM00990. VRR_NUC. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y2M0-1) [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
MMSEGKPPDK KRPRRSLSIS KNKKKASNSI ISCFNNAPPA KLACPVCSKM
60 70 80 90 100
VPRYDLNRHL DEMCANNDFV QVDPGQVGLI NSNVSMVDLT SVTLEDVTPK
110 120 130 140 150
KSPPPKTNLT PGQSDSAKRE VKQKISPYFK SNDVVCKNQD ELRNRSVKVI
160 170 180 190 200
CLGSLASKLS RKYVKAKKSI DKDEEFAGSS PQSSKSTVVK SLIDNSSEIE
210 220 230 240 250
DEDQILENSS QKENVFKCDS LKEECIPEHM VRGSKIMEAE SQKATRECEK
260 270 280 290 300
SALTPGFSDN AIMLFSPDFT LRNTLKSTSE DSLVKQECIK EVVEKREACH
310 320 330 340 350
CEEVKMTVAS EAKIQLSDSE AKSHSSADDA SAWSNIQEAP LQDDSCLNND
360 370 380 390 400
IPHSIPLEQG SSCNGPGQTT GHPYYLRSFL VVLKTVLENE DDMLLFDEQE
410 420 430 440 450
KGIVTKFYQL SATGQKLYVR LFQRKLSWIK MTKLEYEEIA LDLTPVIEEL
460 470 480 490 500
TNAGFLQTES ELQELSEVLE LLSAPELKSL AKTFHLVNPN GQKQQLVDAF
510 520 530 540 550
LKLAKQRSVC TWGKNKPGIG AVILKRAKAL AGQSVRICKG PRAVFSRILL
560 570 580 590 600
LFSLTDSMED EDAACGGQGQ LSTVLLVNLG RMEFPSYTIN RKTHIFQDRD
610 620 630 640 650
DLIRYAAATH MLSDISSAMA NGNWEEAKEL AQCAKRDWNR LKNHPSLRCH
660 670 680 690 700
EDLPLFLRCF TVGWIYTRIL SRFVEILQRL HMYEEAVREL ESLLSQRIYC
710 720 730 740 750
PDSRGRWWDR LALNLHQHLK RLEPTIKCIT EGLADPEVRT GHRLSLYQRA
760 770 780 790 800
VRLRESPSCK KFKHLFQQLP EMAVQDVKHV TITGRLCPQR GMCKSVFVME
810 820 830 840 850
AGEAADPTTV LCSVEELALA HYRRSGFDQG IHGEGSTFST LYGLLLWDII
860 870 880 890 900
FMDGIPDVFR NACQAFPLDL CTDSFFTSRR PALEARLQLI HDAPEESLRA
910 920 930 940 950
WVAATWHEQE GRVASLVSWD RFTSLQQAQD LVSCLGGPVL SGVCRHLAAD
960 970 980 990 1000
FRHCRGGLPD LVVWNSQSRH FKLVEVKGPN DRLSHKQMIW LAELQKLGAE
1010
VEVCHVVAVG AKSQSLS
Length:1,017
Mass (Da):114,225
Last modified:November 13, 2007 - v4
Checksum:i5E4E0A8A1A158F50
GO
Isoform 2 (identifier: Q9Y2M0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     527-533: AKALAGQ → FCWLLLQ
     534-1017: Missing.

Show »
Length:533
Mass (Da):59,498
Checksum:i016E3FDB6C031F95
GO

Sequence cautioni

The sequence AAH47882.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA76862.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91D → DK in AAH47882 (PubMed:15489334).Curated
Sequence conflicti319 – 3191S → P in BAF83676 (PubMed:14702039).Curated
Sequence conflicti487 – 4871V → A in BAA76862 (PubMed:10231032).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti233 – 2331G → E.1 Publication
Corresponds to variant rs4779794 [ dbSNP | Ensembl ].
VAR_037167
Natural varianti871 – 8711C → R in KMIN; partially complement cell survival upon exposure to mitomycin C. 1 Publication
VAR_068958
Natural varianti929 – 9291Q → P in KMIN. 1 Publication
VAR_068959
Natural varianti937 – 9371G → D in KMIN. 1 Publication
VAR_068960
Natural varianti960 – 9601D → N in KMIN. 1 Publication
VAR_068961

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei527 – 5337AKALAGQ → FCWLLLQ in isoform 2. 2 PublicationsVSP_029429
Alternative sequencei534 – 1017484Missing in isoform 2. 2 PublicationsVSP_029430Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023235 mRNA. Translation: BAA76862.3. Different initiation.
AK290987 mRNA. Translation: BAF83676.1.
AC087481 Genomic DNA. No translation available.
BC047882 mRNA. Translation: AAH47882.1. Different initiation.
CCDSiCCDS32186.1. [Q9Y2M0-1]
CCDS58344.1. [Q9Y2M0-2]
RefSeqiNP_001139566.1. NM_001146094.1. [Q9Y2M0-2]
NP_001139567.1. NM_001146095.1. [Q9Y2M0-2]
NP_001139568.1. NM_001146096.1. [Q9Y2M0-2]
NP_055782.3. NM_014967.4. [Q9Y2M0-1]
XP_005254289.1. XM_005254232.3. [Q9Y2M0-1]
XP_005254291.1. XM_005254234.3. [Q9Y2M0-1]
XP_005254292.1. XM_005254235.3. [Q9Y2M0-1]
XP_006725601.1. XM_006725538.2. [Q9Y2M0-1]
XP_006725602.1. XM_006725539.2. [Q9Y2M0-1]
XP_006725603.1. XM_006725540.2. [Q9Y2M0-1]
XP_011547200.1. XM_011548898.1. [Q9Y2M0-1]
XP_011547201.1. XM_011548899.1. [Q9Y2M0-1]
XP_011547202.1. XM_011548900.1. [Q9Y2M0-1]
UniGeneiHs.584863.
Hs.734213.

Genome annotation databases

EnsembliENST00000362065; ENSP00000354497; ENSG00000198690. [Q9Y2M0-1]
ENST00000561594; ENSP00000455983; ENSG00000198690. [Q9Y2M0-2]
ENST00000561607; ENSP00000454223; ENSG00000198690. [Q9Y2M0-2]
ENST00000565466; ENSP00000454544; ENSG00000198690. [Q9Y2M0-2]
ENST00000621063; ENSP00000484956; ENSG00000276787. [Q9Y2M0-1]
GeneIDi22909.
KEGGihsa:22909.
UCSCiuc001zfc.3. human. [Q9Y2M0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023235 mRNA. Translation: BAA76862.3. Different initiation.
AK290987 mRNA. Translation: BAF83676.1.
AC087481 Genomic DNA. No translation available.
BC047882 mRNA. Translation: AAH47882.1. Different initiation.
CCDSiCCDS32186.1. [Q9Y2M0-1]
CCDS58344.1. [Q9Y2M0-2]
RefSeqiNP_001139566.1. NM_001146094.1. [Q9Y2M0-2]
NP_001139567.1. NM_001146095.1. [Q9Y2M0-2]
NP_001139568.1. NM_001146096.1. [Q9Y2M0-2]
NP_055782.3. NM_014967.4. [Q9Y2M0-1]
XP_005254289.1. XM_005254232.3. [Q9Y2M0-1]
XP_005254291.1. XM_005254234.3. [Q9Y2M0-1]
XP_005254292.1. XM_005254235.3. [Q9Y2M0-1]
XP_006725601.1. XM_006725538.2. [Q9Y2M0-1]
XP_006725602.1. XM_006725539.2. [Q9Y2M0-1]
XP_006725603.1. XM_006725540.2. [Q9Y2M0-1]
XP_011547200.1. XM_011548898.1. [Q9Y2M0-1]
XP_011547201.1. XM_011548899.1. [Q9Y2M0-1]
XP_011547202.1. XM_011548900.1. [Q9Y2M0-1]
UniGeneiHs.584863.
Hs.734213.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4REAX-ray3.81A/B373-1017[»]
4REBX-ray4.20A/H373-1017[»]
4RECX-ray2.20A373-1017[»]
4RI8X-ray2.90A/B370-1017[»]
4RI9X-ray2.90A/B370-1017[»]
4RIAX-ray3.00A/B370-1017[»]
4RIBX-ray3.25A/B364-1017[»]
4RICX-ray2.80A/B370-1009[»]
4RIDX-ray3.30A/B370-1009[»]
4RY3X-ray2.80A371-1010[»]
ProteinModelPortaliQ9Y2M0.
SMRiQ9Y2M0. Positions 370-1009.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116573. 35 interactions.
IntActiQ9Y2M0. 23 interactions.
STRINGi9606.ENSP00000354497.

PTM databases

DEPODiQ9Y2M0.
PhosphoSiteiQ9Y2M0.

Polymorphism and mutation databases

BioMutaiFAN1.
DMDMi160410012.

Proteomic databases

MaxQBiQ9Y2M0.
PaxDbiQ9Y2M0.
PRIDEiQ9Y2M0.

Protocols and materials databases

DNASUi22909.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000362065; ENSP00000354497; ENSG00000198690. [Q9Y2M0-1]
ENST00000561594; ENSP00000455983; ENSG00000198690. [Q9Y2M0-2]
ENST00000561607; ENSP00000454223; ENSG00000198690. [Q9Y2M0-2]
ENST00000565466; ENSP00000454544; ENSG00000198690. [Q9Y2M0-2]
ENST00000621063; ENSP00000484956; ENSG00000276787. [Q9Y2M0-1]
GeneIDi22909.
KEGGihsa:22909.
UCSCiuc001zfc.3. human. [Q9Y2M0-1]

Organism-specific databases

CTDi22909.
GeneCardsiFAN1.
H-InvDBHIX0012068.
HGNCiHGNC:29170. FAN1.
HPAiHPA041383.
HPA048198.
MalaCardsiFAN1.
MIMi613534. gene.
614817. phenotype.
neXtProtiNX_Q9Y2M0.
Orphaneti401996. Karyomegalic interstitial nephritis.
PharmGKBiPA165478601.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2143. Eukaryota.
ENOG410XRN3. LUCA.
GeneTreeiENSGT00390000018637.
HOGENOMiHOG000113686.
HOVERGENiHBG108156.
InParanoidiQ9Y2M0.
KOiK15363.
OMAiCFRGEAL.
OrthoDBiEOG7CNZF4.
PhylomeDBiQ9Y2M0.
TreeFamiTF312870.

Enzyme and pathway databases

ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.

Miscellaneous databases

ChiTaRSiFAN1. human.
GenomeRNAii22909.
NextBioi43581.
PROiQ9Y2M0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2M0.
CleanExiHS_MTMR15.
ExpressionAtlasiQ9Y2M0. baseline and differential.
GenevisibleiQ9Y2M0. HS.

Family and domain databases

InterProiIPR014883. VRR_NUC.
IPR006642. Znf_Rad18_put.
[Graphical view]
PfamiPF08774. VRR_NUC. 1 hit.
[Graphical view]
SMARTiSM00990. VRR_NUC. 1 hit.
SM00734. ZnF_Rad18. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. Ohara O., Nagase T., Kikuno R.
    Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "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] (ISOFORM 2).
    Tissue: Teratocarcinoma.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 2), VARIANT GLU-233.
    Tissue: Lung.
  6. "Identification of KIAA1018/FAN1, a DNA repair nuclease recruited to DNA damage by monoubiquitinated FANCD2."
    MacKay C., Declais A.C., Lundin C., Agostinho A., Deans A.J., MacArtney T.J., Hofmann K., Gartner A., West S.C., Helleday T., Lilley D.M., Rouse J.
    Cell 142:65-76(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN UBZ-TYPE, INTERACTION WITH FANCD2 AND FANCI, MUTAGENESIS OF 981-ASP-ARG-982.
  7. "Deficiency of FANCD2-associated nuclease KIAA1018/FAN1 sensitizes cells to interstrand crosslinking agents."
    Kratz K., Schopf B., Kaden S., Sendoel A., Eberhard R., Lademann C., Cannavo E., Sartori A.A., Hengartner M.O., Jiricny J.
    Cell 142:77-88(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, DOMAIN UBZ-TYPE, INTERACTION WITH FANCD2, MUTAGENESIS OF CYS-44; CYS-47 AND ASP-960.
  8. "Human KIAA1018/FAN1 localizes to stalled replication forks via its ubiquitin-binding domain."
    Shereda R.D., Machida Y., Machida Y.J.
    Cell Cycle 9:3977-3983(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DOMAIN UBZ-TYPE.
  9. "A genetic screen identifies FAN1, a Fanconi anemia-associated nuclease necessary for DNA interstrand crosslink repair."
    Smogorzewska A., Desetty R., Saito T.T., Schlabach M., Lach F.P., Sowa M.E., Clark A.B., Kunkel T.A., Harper J.W., Colaiacovo M.P., Elledge S.J.
    Mol. Cell 39:36-47(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FANCD2; MLH1; MLH3 AND PMS2, MUTAGENESIS OF CYS-44; CYS-47; LEU-477; GLN-864; ASP-960; GLU-975 AND LYS-977.
  10. "FAN1 acts with FANCI-FANCD2 to promote DNA interstrand cross-link repair."
    Liu T., Ghosal G., Yuan J., Chen J., Huang J.
    Science 329:693-696(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DOMAIN UBZ-TYPE, INTERACTION WITH FANCD2 AND FANCI, MUTAGENESIS OF CYS-44; ASP-960 AND LYS-977.
  11. "KIAA1018/FAN1 nuclease protects cells against genomic instability induced by interstrand cross-linking agents."
    Yoshikiyo K., Kratz K., Hirota K., Nishihara K., Takata M., Kurumizaka H., Horimoto S., Takeda S., Jiricny J.
    Proc. Natl. Acad. Sci. U.S.A. 107:21553-21557(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Human KIAA1018/FAN1 nuclease is a new mitotic substrate of APC/C(Cdh1)."
    Lai F., Hu K., Wu Y., Tang J., Sang Y., Cao J., Kang T.
    Ai Zheng 31:440-448(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, PROTEASOMAL DEGRADATION, IDENTIFICATION OF D-BOX AND KEN BOX MOTIFS.
  13. "FAN1 activity on asymmetric repair intermediates is mediated by an atypical monomeric virus-type replication-repair nuclease domain."
    Pennell S., Declais A.C., Li J., Haire L.F., Berg W., Saldanha J.W., Taylor I.A., Rouse J., Lilley D.M., Smerdon S.J.
    Cell Rep. 8:84-93(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "FANCD2-controlled chromatin access of the Fanconi-associated nuclease FAN1 is crucial for the recovery of stalled replication forks."
    Chaudhury I., Stroik D.R., Sobeck A.
    Mol. Cell. Biol. 34:3939-3954(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Scan statistic-based analysis of exome sequencing data identifies FAN1 at 15q13.3 as a susceptibility gene for schizophrenia and autism."
    Ionita-Laza I., Xu B., Makarov V., Buxbaum J.D., Roos J.L., Gogos J.A., Karayiorgou M.
    Proc. Natl. Acad. Sci. U.S.A. 111:343-348(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN SCHIZOPHRENIA AND AUTISM.
  16. "DNA repair. Mechanism of DNA interstrand cross-link processing by repair nuclease FAN1."
    Wang R., Persky N.S., Yoo B., Ouerfelli O., Smogorzewska A., Elledge S.J., Pavletich N.P.
    Science 346:1127-1130(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 364-1017 IN COMPLEX WITH TARGET DNA AND CALCIUM, FUNCTION, MUTAGENESIS OF ARG-706 AND ARG-952.
  17. Cited for: VARIANTS KMIN ARG-871; PRO-929; ASP-937 AND ASN-960.

Entry informationi

Entry nameiFAN1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2M0
Secondary accession number(s): A8K4M2, Q86WU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: April 13, 2016
This is version 108 of the entry and version 4 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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.