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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)DescriptionActionsGraphical viewLength
Metal bindingi834Magnesium or manganese 2By similarity1
Metal bindingi960Magnesium or manganese 11 Publication1
Metal bindingi960Magnesium or manganese 21 Publication1
Metal bindingi975Magnesium or manganese 11 Publication1
Metal bindingi976Magnesium or manganese 1; via carbonyl oxygenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri41 – 67UBZ-typeAdd BLAST27

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

BioCyciZFISH:G66-31269-MONOMER.
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_068958871C → R in KMIN; partially complement cell survival upon exposure to mitomycin C. 1 Publication1
Natural variantiVAR_068959929Q → P in KMIN. 1 Publication1
Natural variantiVAR_068960937G → D in KMIN. 1 Publication1
Natural variantiVAR_068961960D → N in KMIN. 1 PublicationCorresponds to variant rs751703979dbSNPEnsembl.1

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)DescriptionActionsGraphical viewLength
Mutagenesisi44C → A: Abolishes interaction with monoubiquitinated FANCD2; when associated with A-47. 3 Publications1
Mutagenesisi47C → A: Abolishes interaction with monoubiquitinated FANCD2; when associated with A-44. 2 Publications1
Mutagenesisi477L → P: Still localized to sites of DNA damage but the strength of the signal is diminished. 1 Publication1
Mutagenesisi706R → 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 Publication1
Mutagenesisi864Q → A: Loss of nuclease activity; when associated with A-960; A-975 and A-977. 1 Publication1
Mutagenesisi952R → 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 Publication1
Mutagenesisi960D → A: Loss of nuclease activity. Loss of nuclease activity; when associated with A-864; A-975 and A-977. 3 Publications1
Mutagenesisi975E → A: Loss of nuclease activity; when associated with A-864; A-960 and A-977. 1 Publication1
Mutagenesisi977K → A: Loss of nuclease activity; when associated with A-864; A-960 and A-975. 2 Publications1
Mutagenesisi981 – 982DR → AA: Loss of nuclease activity. 1 Publication2

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi22909.
MalaCardsiFAN1.
MIMi614817. phenotype.
OpenTargetsiENSG00000198690.
ENSG00000276787.
Orphaneti401996. Karyomegalic interstitial nephritis.
PharmGKBiPA165478601.

Polymorphism and mutation databases

BioMutaiFAN1.
DMDMi160410012.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003112241 – 1017Fanconi-associated nuclease 1Add BLAST1017

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei180PhosphoserineCombined sources1

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y2M0.
PaxDbiQ9Y2M0.
PeptideAtlasiQ9Y2M0.
PRIDEiQ9Y2M0.

PTM databases

DEPODiQ9Y2M0.
iPTMnetiQ9Y2M0.
PhosphoSitePlusiQ9Y2M0.

Expressioni

Gene expression databases

BgeeiENSG00000198690.
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 interactors.
IntActiQ9Y2M0. 23 interactors.
STRINGi9606.ENSP00000354497.

Structurei

Secondary structure

11017
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi374 – 388Combined sources15
Helixi390 – 393Combined sources4
Helixi398 – 408Combined sources11
Helixi412 – 422Combined sources11
Helixi431 – 433Combined sources3
Turni437 – 439Combined sources3
Helixi444 – 452Combined sources9
Beta strandi455 – 458Combined sources4
Helixi459 – 461Combined sources3
Helixi465 – 471Combined sources7
Helixi474 – 483Combined sources10
Helixi493 – 503Combined sources11
Helixi520 – 531Combined sources12
Beta strandi533 – 537Combined sources5
Helixi539 – 552Combined sources14
Helixi554 – 556Combined sources3
Turni557 – 559Combined sources3
Turni563 – 565Combined sources3
Helixi566 – 568Combined sources3
Helixi573 – 575Combined sources3
Helixi577 – 580Combined sources4
Beta strandi595 – 598Combined sources4
Helixi599 – 620Combined sources22
Helixi624 – 639Combined sources16
Turni640 – 643Combined sources4
Helixi645 – 651Combined sources7
Helixi655 – 658Combined sources4
Helixi662 – 679Combined sources18
Helixi683 – 695Combined sources13
Beta strandi697 – 699Combined sources3
Helixi701 – 703Combined sources3
Helixi704 – 716Combined sources13
Helixi722 – 734Combined sources13
Helixi740 – 754Combined sources15
Helixi757 – 759Combined sources3
Helixi761 – 765Combined sources5
Beta strandi778 – 783Combined sources6
Beta strandi786 – 788Combined sources3
Beta strandi796 – 798Combined sources3
Beta strandi804 – 806Combined sources3
Beta strandi811 – 813Combined sources3
Helixi814 – 824Combined sources11
Beta strandi829 – 832Combined sources4
Helixi835 – 850Combined sources16
Beta strandi861 – 863Combined sources3
Turni868 – 871Combined sources4
Helixi874 – 877Combined sources4
Helixi880 – 891Combined sources12
Helixi895 – 909Combined sources15
Beta strandi921 – 924Combined sources4
Helixi925 – 949Combined sources25
Helixi951 – 955Combined sources5
Beta strandi960 – 964Combined sources5
Turni966 – 968Combined sources3
Beta strandi971 – 977Combined sources7
Helixi985 – 996Combined sources12
Beta strandi1001 – 1007Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini895 – 1007VRR-NUCAdd BLAST113

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili671 – 696Sequence analysisAdd BLAST26

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi14 – 22D-boxCurated9
Motifi212 – 214KEN boxCurated3

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)DescriptionActionsGraphical viewLength
Zinc fingeri41 – 67UBZ-typeAdd BLAST27

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG2143. Eukaryota.
ENOG410XRN3. LUCA.
GeneTreeiENSGT00390000018637.
HOGENOMiHOG000113686.
HOVERGENiHBG108156.
InParanoidiQ9Y2M0.
KOiK15363.
OMAiCFRGEAL.
OrthoDBiEOG091G033P.
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA76862 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9D → DK in AAH47882 (PubMed:15489334).Curated1
Sequence conflicti319S → P in BAF83676 (PubMed:14702039).Curated1
Sequence conflicti487V → A in BAA76862 (PubMed:10231032).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_037167233G → E.1 PublicationCorresponds to variant rs4779794dbSNPEnsembl.1
Natural variantiVAR_068958871C → R in KMIN; partially complement cell survival upon exposure to mitomycin C. 1 Publication1
Natural variantiVAR_068959929Q → P in KMIN. 1 Publication1
Natural variantiVAR_068960937G → D in KMIN. 1 Publication1
Natural variantiVAR_068961960D → N in KMIN. 1 PublicationCorresponds to variant rs751703979dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_029429527 – 533AKALAGQ → FCWLLLQ in isoform 2. 2 Publications7
Alternative sequenceiVSP_029430534 – 1017Missing in isoform 2. 2 PublicationsAdd BLAST484

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_005254232.4. [Q9Y2M0-1]
XP_005254291.1. XM_005254234.4. [Q9Y2M0-1]
XP_005254292.1. XM_005254235.3. [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_005254232.4. [Q9Y2M0-1]
XP_005254291.1. XM_005254234.4. [Q9Y2M0-1]
XP_005254292.1. XM_005254235.3. [Q9Y2M0-1]
UniGeneiHs.584863.
Hs.734213.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116573. 35 interactors.
IntActiQ9Y2M0. 23 interactors.
STRINGi9606.ENSP00000354497.

PTM databases

DEPODiQ9Y2M0.
iPTMnetiQ9Y2M0.
PhosphoSitePlusiQ9Y2M0.

Polymorphism and mutation databases

BioMutaiFAN1.
DMDMi160410012.

Proteomic databases

EPDiQ9Y2M0.
PaxDbiQ9Y2M0.
PeptideAtlasiQ9Y2M0.
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.
DisGeNETi22909.
GeneCardsiFAN1.
H-InvDBHIX0012068.
HGNCiHGNC:29170. FAN1.
HPAiHPA041383.
HPA048198.
MalaCardsiFAN1.
MIMi613534. gene.
614817. phenotype.
neXtProtiNX_Q9Y2M0.
OpenTargetsiENSG00000198690.
ENSG00000276787.
Orphaneti401996. Karyomegalic interstitial nephritis.
PharmGKBiPA165478601.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2143. Eukaryota.
ENOG410XRN3. LUCA.
GeneTreeiENSGT00390000018637.
HOGENOMiHOG000113686.
HOVERGENiHBG108156.
InParanoidiQ9Y2M0.
KOiK15363.
OMAiCFRGEAL.
OrthoDBiEOG091G033P.
PhylomeDBiQ9Y2M0.
TreeFamiTF312870.

Enzyme and pathway databases

BioCyciZFISH:G66-31269-MONOMER.
ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000198690.
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...

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: November 2, 2016
This is version 113 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.