Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8K368 (FANCI_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fanconi anemia group I protein homolog

Short name=Protein FACI
Gene names
Name:Fanci
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1330 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an essential role in the repair of DNA double-strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and participating in recruitment to DNA repair sites. Required for maintenance of chromosomal stability. Specifically binds branched DNA: binds both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). Participates in S phase and G2 phase checkpoint activation upon DNA damage.

Subunit structure

Interacts with FANCD2; the interaction is direct. Interacts with FANCL. Interacts with MTMR15/FAN1 By similarity.

Subcellular location

Nucleus By similarity. Note: Observed in spots localized in pairs on the sister chromatids of mitotic chromosome arms and not centromeres, one on each chromatids. These foci coincide with common fragile sites. They are frequently interlinked through BLM-associated ultra-fine DNA bridges By similarity.

Domain

The C-terminal 30 residues are probably required for function in DNA repair By similarity.

Post-translational modification

Monoubiquitinated by FANCL on Lys-522 during S phase and upon genotoxic stress. Deubiquitinated by USP1 as cells enter G2/M, or once DNA repair is completed. Monoubiquitination requires the FANCA-FANCB-FANCC-FANCE-FANCF-FANCG-FANCM complex. Ubiquitination is required for binding to chromatin, DNA repair, and normal cell cycle progression. Monoubiquitination is stimulated by DNA-binding By similarity.

Phosphorylated in response to DNA damage by ATM and/or ATR. Ref.4

Sequence caution

The sequence BAC39475.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8K368-1)

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.
Isoform 2 (identifier: Q8K368-2)

The sequence of this isoform differs from the canonical sequence as follows:
     371-394: SVHSWDHVTQGLIEFGFILMDSYG → RLVFRYHHVCTFNSSELFKSHGNF
     395-1330: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.
Isoform 4 (identifier: Q8K368-4)

The sequence of this isoform differs from the canonical sequence as follows:
     879-1330: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13301330Fanconi anemia group I protein homolog
PRO_0000289977

Amino acid modifications

Modified residue5551Phosphoserine Ref.4
Modified residue5581Phosphothreonine Ref.4
Modified residue7291Phosphoserine By similarity
Modified residue9481Phosphothreonine By similarity
Modified residue11221Phosphoserine By similarity
Cross-link522Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence371 – 39424SVHSW…MDSYG → RLVFRYHHVCTFNSSELFKS HGNF in isoform 2.
VSP_026072
Alternative sequence395 – 1330936Missing in isoform 2.
VSP_026073
Alternative sequence879 – 1330452Missing in isoform 4.
VSP_026074

Experimental info

Sequence conflict5401L → W in BAC39475. Ref.3

Secondary structure

.................................................................................................................................................................... 1330
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 12, 2007. Version 2.
Checksum: 68A0580B54E20CBB

FASTA1,330149,326
        10         20         30         40         50         60 
MDLKILSLAT DKTTDKLQEF LQTLKDDDLA SLLQNQAVKG RAVGTLLRAV LKGSPCSEED 

        70         80         90        100        110        120 
GALRRYKIYS CCIQLVESGD LQQDVASEII GLLMLEVHHF PGPLLVDLAS DFVGAVREDR 

       130        140        150        160        170        180 
LVNGKSLELL PIILTALATK KEVLACGKGD LNGEEYKRQL IDTLCSVRWP QRYMIQLTSV 

       190        200        210        220        230        240 
FKDVCLTPEE MNLVVAKVLT MFSKLNLQEI PPLVYQLLVL SSKGSRRSVL DGIIAFFREL 

       250        260        270        280        290        300 
DKQHREEQSS DELSELITAP ADELYHVEGT VILHIVFAIK LDCELGRELL KHLKAGQQGD 

       310        320        330        340        350        360 
PSKCLCPFSI ALLLSLTRIQ RFEEQVFDLL KTSVVKSFKD LQLLQGSKFL QTLVPQRTCV 

       370        380        390        400        410        420 
STMILEVVRN SVHSWDHVTQ GLIEFGFILM DSYGPKKILD GKAVEIGTSL SKMTNQHACK 

       430        440        450        460        470        480 
LGANILLETF KIHEMIRQEI LEQVLNRVVT RTSSPINHFL DLFSDIIMYA PLILQNCSKV 

       490        500        510        520        530        540 
TETFDYLTFL PLQTVQGLLK AVQPLLKISM SMRDSLILVL RKAMFASQLD ARKSAVAGFL 

       550        560        570        580        590        600 
LLLKNFKVLG SLPSSQCTQS IGVTQVRVDV HSRYSAVANE TFCLEIIDSL KRSLGQQADI 

       610        620        630        640        650        660 
RLMLYDGFYD VLRRNSQLAS SIMQTLFSQL KQFYEPEPDL LPPLKLGACV LTQGSQIFLQ 

       670        680        690        700        710        720 
EPLDHLLSCI QHCLAWYKSR VVPLQQGDEG EEEEEELYSE LDDMLESITV RMIKSELEDF 

       730        740        750        760        770        780 
ELDKSADFSQ NTNVGIKNNI CACLIMGVCE VLMEYNFSIS NFSKSKFEEI LSLFTCYKKF 

       790        800        810        820        830        840 
SDILSEKAGK GKAKMTSKVS DSLLSLKFVS DLLTALFRDS IQSHEESLSV LRSSGEFMHY 

       850        860        870        880        890        900 
AVNVTLQKIQ QLIRTGHVSG PDGQNPDKIF QNLCDITRVL LWRYTSIPTS VEESGKKEKG 

       910        920        930        940        950        960 
KSISLLCLEG LQKTFSVVLQ FYQPKVQQFL QALDVMGTEE EEAGVTVTQR ASFQIRQFQR 

       970        980        990       1000       1010       1020 
SLLNLLSSEE DDFNSKEALL LIAVLSTLSR LLEPTSPQFV QMLSWTSKIC KEYSQEDASF 

      1030       1040       1050       1060       1070       1080 
CKSLMNLFFS LHVLYKSPVT LLRDLSQDIH GQLGDIDQDV EIEKTDHFAV VNLRTAAPTV 

      1090       1100       1110       1120       1130       1140 
CLLVLSQAEK VLEEVDWLIA KIKGSANQET LSDKVTPEDA SSQAVPPTLL IEKAIVMQLG 

      1150       1160       1170       1180       1190       1200 
TLVTFFHELV QTALPSGSCV DTLLKGLSKI YSTLTAFVKY YLQVCQSSRG IPNTVEKLVK 

      1210       1220       1230       1240       1250       1260 
LSGSHLTPVC YSFISYVQNK SSDAPKCSEK EKAAVSTTMA KVLRETKPIP NLVFAIEQYE 

      1270       1280       1290       1300       1310       1320 
KFLIQLSKKS KVNLMQHMKL STSRDFKIKG SVLDMVLRED EEDENEEGTA SAHTQQDREP 

      1330 
AKKRRKKCLS 

« Hide

Isoform 2 [UniParc].

Checksum: 71530D576E81F23B
Show »

FASTA39444,333
Isoform 4 [UniParc].

Checksum: BC9A79AED797F624
Show »

FASTA87898,663

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"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).
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"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. expand/collapse author list , 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] OF 27-1330 (ISOFORM 4).
Strain: C57BL/6J.
Tissue: Kidney.
[4]"Identification of the FANCI protein, a monoubiquitinated FANCD2 paralog required for DNA repair."
Smogorzewska A., Matsuoka S., Vinciguerra P., McDonald E.R. III, Hurov K.E., Luo J., Ballif B.A., Gygi S.P., Hofmann K., D'Andrea A.D., Elledge S.J.
Cell 129:289-301(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-555 AND THR-558.
[5]"FANCI is a second monoubiquitinated member of the Fanconi anemia pathway."
Sims A.E., Spiteri E., Sims R.J. III, Arita A.G., Lach F.P., Landers T., Wurm M., Freund M., Neveling K., Hanenberg H., Auerbach A.D., Huang T.T.
Nat. Struct. Mol. Biol. 14:564-567(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC110909 Genomic DNA. No translation available.
BC027836 mRNA. No translation available.
AK085572 mRNA. Translation: BAC39475.1. Different initiation.
RefSeqNP_666058.2. NM_145946.2.
UniGeneMm.349493.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3S4WX-ray3.41A1-1302[»]
3S4ZX-ray7.80A/B/C1-1302[»]
3S51X-ray3.30A/B/C/D1-1302[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229017. 2 interactions.
STRING10090.ENSMUSP00000044931.

PTM databases

PhosphoSiteQ8K368.

Proteomic databases

PaxDbQ8K368.
PRIDEQ8K368.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000036865; ENSMUSP00000044931; ENSMUSG00000039187. [Q8K368-1]
ENSMUST00000132091; ENSMUSP00000122113; ENSMUSG00000039187. [Q8K368-2]
GeneID208836.
KEGGmmu:208836.
UCSCuc009hyh.1. mouse. [Q8K368-1]

Organism-specific databases

CTD55215.
MGIMGI:2384790. Fanci.

Phylogenomic databases

eggNOGNOG324185.
GeneTreeENSGT00390000005855.
HOGENOMHOG000112497.
HOVERGENHBG106622.
InParanoidQ8K368.
KOK10895.
OMASQEEDFN.
PhylomeDBQ8K368.
TreeFamTF323694.

Gene expression databases

ArrayExpressQ8K368.
BgeeQ8K368.
CleanExMM_FANCI.
GenevestigatorQ8K368.

Family and domain databases

InterProIPR026171. FANCI.
[Graphical view]
PANTHERPTHR21818:SF0. PTHR21818:SF0. 1 hit.
PfamPF14676. FANCI_S2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio372429.
PROQ8K368.
SOURCESearch...

Entry information

Entry nameFANCI_MOUSE
AccessionPrimary (citable) accession number: Q8K368
Secondary accession number(s): Q8BUE9, Q8R3G8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 12, 2007
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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