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Protein

Fanconi-associated nuclease 1

Gene

Fan1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity). Not involved in DNA double-strand breaks resection. 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 (PubMed:24981866). Probably keeps excising with 3'-flap annealing until it reaches and unhooks the ICL. 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 (By similarity). Also has endonuclease activity toward 5'-flaps (PubMed:24981866).By similarity1 Publication

Catalytic activityi

Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.1 Publication

Cofactori

Mn2+By similarity, Mg2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi837 – 8371Magnesium or manganese 2By similarity
Metal bindingi963 – 9631Magnesium or manganese 1By similarity
Metal bindingi963 – 9631Magnesium or manganese 2By similarity
Metal bindingi978 – 9781Magnesium or manganese 1By similarity
Metal bindingi979 – 9791Magnesium or manganese 1; via carbonyl oxygenBy similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

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-MMU-6783310. Fanconi Anemia Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Fanconi-associated nuclease 1By similarity (EC:3.1.21.-1 Publication, EC:3.1.4.11 Publication)
Alternative name(s):
FANCD2/FANCI-associated nuclease 1By similarity
Short name:
mFAN11 Publication
Myotubularin-related protein 15
Gene namesi
Name:Fan1Imported
Synonyms:Kiaa10181 Publication, Mtmr15
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:3045266. Fan1.

Subcellular locationi

  • Nucleus By similarity

  • Note: Localizes at sites of DNA damage following recruitment by monoubiquitinated FANCD2. Localizes to stalled replication forks via its UBZ-type zinc finger.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10201020Fanconi-associated nuclease 1PRO_0000311225Add
BLAST

Post-translational modificationi

Ubiquitinated and degraded during mitotic exit by the APC/C-Cdh1 complex.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ69ZT1.
MaxQBiQ69ZT1.
PaxDbiQ69ZT1.
PRIDEiQ69ZT1.

PTM databases

iPTMnetiQ69ZT1.
PhosphoSiteiQ69ZT1.

Expressioni

Gene expression databases

BgeeiQ69ZT1.
CleanExiMM_MTMR15.

Interactioni

Subunit structurei

Interacts with FANCD2 (when monoubiquitinated). Interacts with FANCI, MLH1, MLH3 and PMS2.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000130012.

Structurei

3D structure databases

ProteinModelPortaliQ69ZT1.
SMRiQ69ZT1. Positions 375-1012.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini898 – 1010113VRR-NUCAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili673 – 73765Sequence analysisAdd
BLAST

Motif

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

Domaini

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

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.
HOVERGENiHBG108156.
InParanoidiQ69ZT1.
KOiK15363.
OMAiCFRGEAL.
OrthoDBiEOG7CNZF4.
PhylomeDBiQ69ZT1.
TreeFamiTF312870.

Family and domain databases

InterProiIPR033315. Fan1-like.
IPR014883. VRR_NUC.
[Graphical view]
PANTHERiPTHR15749. PTHR15749. 1 hit.
PfamiPF08774. VRR_NUC. 1 hit.
[Graphical view]
SMARTiSM00990. VRR_NUC. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q69ZT1-1) [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
MPSQRKSPDQ KRPRRSLSTS KTAKSQCHSI TSYFNSAPPA KLACSTCHKM
60 70 80 90 100
VPRYDLIRHL DESCANNGVG DDVQVEPAQA GLMSPTVPTS DLPSGPLENV
110 120 130 140 150
TPQKLSPPKR SLISVQCGSK LGIQQQTSPY FKDALVSKDQ NELPNQSVEI
160 170 180 190 200
MPLGSLTSKL SRRYLNAKKS LAKNEGLASQ CPQTSPSTPG TSLTDNCPEM
210 220 230 240 250
EDKDEVLNSS QKENIYSCAP LKEENASEQK VKNNKITGDE SQKASCGEPA
260 270 280 290 300
LTPASAEHAS ILLSSDSTLV SNTKSSPGDT LVKQESARRA DVGLAEPLEV
310 320 330 340 350
RSHKEVQMTF DAAAKTLVSG EAESNGPTDV DMSDMTTWSN NQELVREAGS
360 370 380 390 400
VLHCPLEQGS SCGGPSETAQ LALSHPYYLR SFLVVLQALL GNEEDMKLFD
410 420 430 440 450
EQEKAIITRF YQLSASGQKL YVRLFQRKLT WIKMSKLEYE EIASDLTPVV
460 470 480 490 500
EELKDSGFLQ TESELQELSD VLELLSAPEL KALAKTFHLV SPGGQKQQLV
510 520 530 540 550
DAFHKLAKQR SVCTWGKTQP GIRAVILKRA KDLAGRSLRV CKGPRAVFAR
560 570 580 590 600
ILLLFSLTDS MEDEEAACGG QGQLSTVLLV NLGRMEFPQY TICRKTQIFR
610 620 630 640 650
DREDLIRYAA AAHMLSDISA AMASGNWEDA KELARSAKRD WEQLKSHPSL
660 670 680 690 700
RYHEALPPFL RCFTVGWIYT RISSRAVEVL ERLHMYEEAV KELENLLSQK
710 720 730 740 750
IYCPDSRGRW WDRLALNLHQ HLKRLEEAIR CIREGLADPH VRTGHRLSLY
760 770 780 790 800
QRAVRLRESP SCRKYKHLFS RLPEVAVGDV KHVTITGRLC PQHGMGKSVF
810 820 830 840 850
VMESGDGANP TTVLCSVEEL ALGYYRQSGF DQGIHGEGST FSTLCGLLLW
860 870 880 890 900
DIIFMDGIPD VFRNAYQASP LDLLTDSFFA SREQALEARL QLIHSAPAES
910 920 930 940 950
LRAWVGEAWQ AQQGRVASLV SWDRFTSLQQ AQDLVSCLGG PVLSGVCRRL
960 970 980 990 1000
AADFRHCRGG LPDLVVWNSQ SHHCKLVEVK GPSDRLSCKQ MIWLYELQKL
1010 1020
GADVEVCHVV AVGAKSKGLG
Length:1,020
Mass (Da):112,925
Last modified:November 13, 2007 - v2
Checksum:iA887731CD19DBF93
GO
Isoform 2 (identifier: Q69ZT1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     728-743: AIRCIREGLADPHVRT → VLAAYPAAYLVLNGKL
     744-1020: Missing.

Note: No experimental confirmation available.
Show »
Length:743
Mass (Da):82,316
Checksum:iCD2E7516C695D88D
GO
Isoform 3 (identifier: Q69ZT1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     462-468: ESELQEL → GTVRRRT
     469-1020: Missing.

Note: No experimental confirmation available.
Show »
Length:468
Mass (Da):51,103
Checksum:i7607F809E2A3E5F2
GO
Isoform 4 (identifier: Q69ZT1-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     415-469: ASGQKLYVRL...QTESELQELS → GTFGLLAFRA...GPFKTSSCAW
     470-1020: Missing.

Note: No experimental confirmation available.
Show »
Length:469
Mass (Da):50,415
Checksum:i74205382B373310F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei415 – 46955ASGQK…LQELS → GTFGLLAFRASSSGLCAMGG PVSSLMTTTRSHCGSTAGWL SVSRRGPFKTSSCAW in isoform 4. 1 PublicationVSP_029431Add
BLAST
Alternative sequencei462 – 4687ESELQEL → GTVRRRT in isoform 3. 1 PublicationVSP_029432
Alternative sequencei469 – 1020552Missing in isoform 3. 1 PublicationVSP_029433Add
BLAST
Alternative sequencei470 – 1020551Missing in isoform 4. 1 PublicationVSP_029434Add
BLAST
Alternative sequencei728 – 74316AIRCI…PHVRT → VLAAYPAAYLVLNGKL in isoform 2. 1 PublicationVSP_029435Add
BLAST
Alternative sequencei744 – 1020277Missing in isoform 2. 1 PublicationVSP_029436Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077918 mRNA. Translation: BAC37062.1.
AC129199 Genomic DNA. No translation available.
AC139849 Genomic DNA. No translation available.
BC116270 mRNA. Translation: AAI16271.1.
BC116271 mRNA. Translation: AAI16272.1.
AK173087 mRNA. Translation: BAD32365.1.
CCDSiCCDS52265.1. [Q69ZT1-1]
RefSeqiNP_808561.2. NM_177893.3. [Q69ZT1-1]
XP_006541021.1. XM_006540958.2. [Q69ZT1-1]
UniGeneiMm.236510.

Genome annotation databases

EnsembliENSMUST00000163289; ENSMUSP00000130012; ENSMUSG00000033458. [Q69ZT1-1]
GeneIDi330554.
KEGGimmu:330554.
UCSCiuc009hge.1. mouse. [Q69ZT1-2]
uc009hgf.2. mouse. [Q69ZT1-3]
uc012fmp.1. mouse. [Q69ZT1-1]
uc029wgg.1. mouse. [Q69ZT1-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077918 mRNA. Translation: BAC37062.1.
AC129199 Genomic DNA. No translation available.
AC139849 Genomic DNA. No translation available.
BC116270 mRNA. Translation: AAI16271.1.
BC116271 mRNA. Translation: AAI16272.1.
AK173087 mRNA. Translation: BAD32365.1.
CCDSiCCDS52265.1. [Q69ZT1-1]
RefSeqiNP_808561.2. NM_177893.3. [Q69ZT1-1]
XP_006541021.1. XM_006540958.2. [Q69ZT1-1]
UniGeneiMm.236510.

3D structure databases

ProteinModelPortaliQ69ZT1.
SMRiQ69ZT1. Positions 375-1012.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000130012.

PTM databases

iPTMnetiQ69ZT1.
PhosphoSiteiQ69ZT1.

Proteomic databases

EPDiQ69ZT1.
MaxQBiQ69ZT1.
PaxDbiQ69ZT1.
PRIDEiQ69ZT1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000163289; ENSMUSP00000130012; ENSMUSG00000033458. [Q69ZT1-1]
GeneIDi330554.
KEGGimmu:330554.
UCSCiuc009hge.1. mouse. [Q69ZT1-2]
uc009hgf.2. mouse. [Q69ZT1-3]
uc012fmp.1. mouse. [Q69ZT1-1]
uc029wgg.1. mouse. [Q69ZT1-4]

Organism-specific databases

CTDi22909.
MGIiMGI:3045266. Fan1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG2143. Eukaryota.
ENOG410XRN3. LUCA.
GeneTreeiENSGT00390000018637.
HOVERGENiHBG108156.
InParanoidiQ69ZT1.
KOiK15363.
OMAiCFRGEAL.
OrthoDBiEOG7CNZF4.
PhylomeDBiQ69ZT1.
TreeFamiTF312870.

Enzyme and pathway databases

ReactomeiR-MMU-6783310. Fanconi Anemia Pathway.

Miscellaneous databases

NextBioi399454.
PROiQ69ZT1.
SOURCEiSearch...

Gene expression databases

BgeeiQ69ZT1.
CleanExiMM_MTMR15.

Family and domain databases

InterProiIPR033315. Fan1-like.
IPR014883. VRR_NUC.
[Graphical view]
PANTHERiPTHR15749. PTHR15749. 1 hit.
PfamiPF08774. VRR_NUC. 1 hit.
[Graphical view]
SMARTiSM00990. VRR_NUC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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 4).
  4. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-1020 (ISOFORM 2).
    Tissue: Pancreatic islet.
  5. "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.

Entry informationi

Entry nameiFAN1_MOUSE
AccessioniPrimary (citable) accession number: Q69ZT1
Secondary accession number(s): Q14B88, Q8BVK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: May 11, 2016
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.