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Q9NVI1

- FANCI_HUMAN

UniProt

Q9NVI1 - FANCI_HUMAN

Protein

Fanconi anemia group I protein

Gene

FANCI

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 4 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    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.4 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. DNA polymerase binding Source: UniProt
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. DNA repair Source: Reactome
    3. positive regulation of protein ubiquitination Source: MGI

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_18265. Regulation of the Fanconi anemia pathway.
    REACT_18410. Fanconi Anemia pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fanconi anemia group I protein
    Short name:
    Protein FACI
    Gene namesi
    Name:FANCI
    Synonyms:KIAA1794
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:25568. FANCI.

    Subcellular locationi

    Nucleus 3 Publications
    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.

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Fanconi anemia complementation group I (FANCI) [MIM:609053]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1285 – 12851R → Q in FA/FANCI; abolishes function in DNA repair. 2 Publications
    VAR_032692

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi523 – 5231K → R: Abolishes monoubiquitination by FANCL and UBE2T. 1 Publication

    Keywords - Diseasei

    Disease mutation, Fanconi anemia

    Organism-specific databases

    MIMi227650. phenotype.
    609053. phenotype.
    Orphaneti84. Fanconi anemia.
    PharmGKBiPA162387928.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13281328Fanconi anemia group I proteinPRO_0000248376Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei407 – 4071Phosphoserine2 Publications
    Cross-linki523 – 523Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)3 Publications
    Modified residuei556 – 5561PhosphoserineBy similarity
    Modified residuei730 – 7301Phosphoserine1 Publication
    Modified residuei952 – 9521Phosphothreonine1 Publication
    Modified residuei1121 – 11211Phosphoserine1 Publication

    Post-translational modificationi

    Monoubiquitinated by FANCL on Lys-523 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.3 Publications
    Phosphorylated in response to DNA damage by ATM and/or ATR.3 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NVI1.
    PaxDbiQ9NVI1.
    PRIDEiQ9NVI1.

    PTM databases

    PhosphoSiteiQ9NVI1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NVI1.
    BgeeiQ9NVI1.
    CleanExiHS_FANCI.
    GenevestigatoriQ9NVI1.

    Organism-specific databases

    HPAiHPA039972.

    Interactioni

    Subunit structurei

    Interacts with FANCD2; the interaction is direct. Interacts with FANCL. Interacts with MTMR15/FAN1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FANCD2Q9BXW92EBI-1013291,EBI-359343

    Protein-protein interaction databases

    BioGridi120511. 30 interactions.
    DIPiDIP-29381N.
    IntActiQ9NVI1. 11 interactions.
    MINTiMINT-1138578.
    STRINGi9606.ENSP00000310842.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NVI1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

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

    Phylogenomic databases

    eggNOGiNOG324185.
    HOVERGENiHBG106622.
    InParanoidiQ9NVI1.
    KOiK10895.
    OMAiSQEEDFN.
    PhylomeDBiQ9NVI1.
    TreeFamiTF323694.

    Family and domain databases

    InterProiIPR026171. FANCI.
    IPR029310. FANCI_HD1.
    IPR029312. FANCI_HD2.
    IPR029308. FANCI_S1.
    IPR029305. FANCI_S1-cap.
    IPR029315. FANCI_S2.
    IPR029313. FANCI_S3.
    IPR029314. FANCI_S4.
    [Graphical view]
    PANTHERiPTHR21818:SF0. PTHR21818:SF0. 1 hit.
    PfamiPF14679. FANCI_HD1. 1 hit.
    PF14680. FANCI_HD2. 1 hit.
    PF14675. FANCI_S1. 1 hit.
    PF14674. FANCI_S1-cap. 1 hit.
    PF14676. FANCI_S2. 1 hit.
    PF14677. FANCI_S3. 1 hit.
    PF14678. FANCI_S4. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 3 (identifier: Q9NVI1-3) [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

    MDQKILSLAA EKTADKLQEF LQTLREGDLT NLLQNQAVKG KVAGALLRAI     50
    FKGSPCSEEA GTLRRRKIYT CCIQLVESGD LQKEIASEII GLLMLEAHHF 100
    PGPLLVELAN EFISAVREGS LVNGKSLELL PIILTALATK KENLAYGKGV 150
    LSGEECKKQL INTLCSGRWD QQYVIQLTSM FKDVPLTAEE VEFVVEKALS 200
    MFSKMNLQEI PPLVYQLLVL SSKGSRKSVL EGIIAFFSAL DKQHNEEQSG 250
    DELLDVVTVP SGELRHVEGT IILHIVFAIK LDYELGRELV KHLKVGQQGD 300
    SNNNLSPFSI ALLLSVTRIQ RFQDQVLDLL KTSVVKSFKD LQLLQGSKFL 350
    QNLVPHRSYV STMILEVVKN SVHSWDHVTQ GLVELGFILM DSYGPKKVLD 400
    GKTIETSPSL SRMPNQHACK LGANILLETF KIHEMIRQEI LEQVLNRVVT 450
    RASSPISHFL DLLSNIVMYA PLVLQSCSSK VTEAFDYLSF LPLQTVQRLL 500
    KAVQPLLKVS MSMRDCLILV LRKAMFANQL DARKSAVAGF LLLLKNFKVL 550
    GSLSSSQCSQ SLSVSQVHVD VHSHYNSVAN ETFCLEIMDS LRRCLSQQAD 600
    VRLMLYEGFY DVLRRNSQLA NSVMQTLLSQ LKQFYEPKPD LLPPLKLEAC 650
    ILTQGDKISL QEPLDYLLCC IQHCLAWYKN TVIPLQQGEE EEEEEEAFYE 700
    DLDDILESIT NRMIKSELED FELDKSADFS QSTSIGIKNN ICAFLVMGVC 750
    EVLIEYNFSI SSFSKNRFED ILSLFMCYKK LSDILNEKAG KAKTKMANKT 800
    SDSLLSMKFV SSLLTALFRD SIQSHQESLS VLRSSNEFMR YAVNVALQKV 850
    QQLKETGHVS GPDGQNPEKI FQNLCDITRV LLWRYTSIPT SVEESGKKEK 900
    GKSISLLCLE GLQKIFSAVQ QFYQPKIQQF LRALDVTDKE GEEREDADVS 950
    VTQRTAFQIR QFQRSLLNLL SSQEEDFNSK EALLLVTVLT SLSKLLEPSS 1000
    PQFVQMLSWT SKICKENSRE DALFCKSLMN LLFSLHVSYK SPVILLRDLS 1050
    QDIHGHLGDI DQDVEVEKTN HFAIVNLRTA APTVCLLVLS QAEKVLEEVD 1100
    WLITKLKGQV SQETLSEEAS SQATLPNQPV EKAIIMQLGT LLTFFHELVQ 1150
    TALPSGSCVD TLLKDLCKMY TTLTALVRYY LQVCQSSGGI PKNMEKLVKL 1200
    SGSHLTPLCY SFISYVQNKS KSLNYTGEKK EKPAAVATAM ARVLRETKPI 1250
    PNLIFAIEQY EKFLIHLSKK SKVNLMQHMK LSTSRDFKIK GNILDMVLRE 1300
    DGEDENEEGT ASEHGGQNKE PAKKKRKK 1328
    Length:1,328
    Mass (Da):149,324
    Last modified:November 4, 2008 - v4
    Checksum:i07E80FD2F0BCCB32
    GO
    Isoform 2 (identifier: Q9NVI1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         819-878: Missing.
         1117-1117: Missing.

    Show »
    Length:1,267
    Mass (Da):142,440
    Checksum:iAD13BB6692A0D812
    GO
    Isoform 1 (identifier: Q9NVI1-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         819-878: Missing.

    Show »
    Length:1,268
    Mass (Da):142,569
    Checksum:i7D3A1A04E97FE80C
    GO
    Isoform 4 (identifier: Q9NVI1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         253-1328: Missing.

    Show »
    Length:252
    Mass (Da):27,824
    Checksum:i8C0E5CC711546A8B
    GO

    Sequence cautioni

    The sequence AAH04277.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA91770.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB55200.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti528 – 5281N → S in BAB47423. (PubMed:11347906)Curated
    Sequence conflicti604 – 6041M → T in BAA91770. (PubMed:14702039)Curated
    Sequence conflicti877 – 8771I → L in BAB47423. (PubMed:11347906)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551P → L in FA; unknown pathological significance; no effect on ubiquitination and DNA repair. 2 Publications
    Corresponds to variant rs62020347 [ dbSNP | Ensembl ].
    VAR_032689
    Natural varianti86 – 861A → V.1 Publication
    Corresponds to variant rs17803620 [ dbSNP | Ensembl ].
    VAR_032690
    Natural varianti686 – 6861Q → K.
    Corresponds to variant rs28378332 [ dbSNP | Ensembl ].
    VAR_027278
    Natural varianti742 – 7421C → S.2 Publications
    Corresponds to variant rs2283432 [ dbSNP | Ensembl ].
    VAR_027279
    Natural varianti858 – 8581H → Y in FA. 1 Publication
    VAR_032691
    Natural varianti1285 – 12851R → Q in FA/FANCI; abolishes function in DNA repair. 2 Publications
    VAR_032692

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei253 – 13281076Missing in isoform 4. 1 PublicationVSP_035606Add
    BLAST
    Alternative sequencei819 – 87860Missing in isoform 1 and isoform 2. 1 PublicationVSP_026069Add
    BLAST
    Alternative sequencei1117 – 11171Missing in isoform 2. 1 PublicationVSP_020257

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF469766 mRNA. Translation: ABP88002.1.
    EF567077 mRNA. Translation: ABQ63084.1.
    AC124068 Genomic DNA. No translation available.
    BC004277 mRNA. Translation: AAH04277.1. Different initiation.
    BC140769 mRNA. Translation: AAI40770.1.
    AK001581 mRNA. Translation: BAA91770.1. Different initiation.
    AK027564 mRNA. Translation: BAB55200.1. Different initiation.
    AB058697 mRNA. Translation: BAB47423.1.
    CCDSiCCDS10349.2. [Q9NVI1-1]
    CCDS45346.1. [Q9NVI1-3]
    RefSeqiNP_001106849.1. NM_001113378.1. [Q9NVI1-3]
    NP_060663.2. NM_018193.2. [Q9NVI1-1]
    UniGeneiHs.513126.

    Genome annotation databases

    EnsembliENST00000300027; ENSP00000300027; ENSG00000140525. [Q9NVI1-1]
    ENST00000310775; ENSP00000310842; ENSG00000140525. [Q9NVI1-3]
    ENST00000567996; ENSP00000458024; ENSG00000140525. [Q9NVI1-4]
    GeneIDi55215.
    KEGGihsa:55215.
    UCSCiuc002bnm.1. human. [Q9NVI1-1]
    uc002bno.3. human. [Q9NVI1-4]
    uc002bnp.1. human. [Q9NVI1-2]
    uc002bnq.1. human. [Q9NVI1-3]

    Polymorphism databases

    DMDMi212276518.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Fanconi Anemia Mutation Database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF469766 mRNA. Translation: ABP88002.1 .
    EF567077 mRNA. Translation: ABQ63084.1 .
    AC124068 Genomic DNA. No translation available.
    BC004277 mRNA. Translation: AAH04277.1 . Different initiation.
    BC140769 mRNA. Translation: AAI40770.1 .
    AK001581 mRNA. Translation: BAA91770.1 . Different initiation.
    AK027564 mRNA. Translation: BAB55200.1 . Different initiation.
    AB058697 mRNA. Translation: BAB47423.1 .
    CCDSi CCDS10349.2. [Q9NVI1-1 ]
    CCDS45346.1. [Q9NVI1-3 ]
    RefSeqi NP_001106849.1. NM_001113378.1. [Q9NVI1-3 ]
    NP_060663.2. NM_018193.2. [Q9NVI1-1 ]
    UniGenei Hs.513126.

    3D structure databases

    ProteinModelPortali Q9NVI1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120511. 30 interactions.
    DIPi DIP-29381N.
    IntActi Q9NVI1. 11 interactions.
    MINTi MINT-1138578.
    STRINGi 9606.ENSP00000310842.

    PTM databases

    PhosphoSitei Q9NVI1.

    Polymorphism databases

    DMDMi 212276518.

    Proteomic databases

    MaxQBi Q9NVI1.
    PaxDbi Q9NVI1.
    PRIDEi Q9NVI1.

    Protocols and materials databases

    DNASUi 55215.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300027 ; ENSP00000300027 ; ENSG00000140525 . [Q9NVI1-1 ]
    ENST00000310775 ; ENSP00000310842 ; ENSG00000140525 . [Q9NVI1-3 ]
    ENST00000567996 ; ENSP00000458024 ; ENSG00000140525 . [Q9NVI1-4 ]
    GeneIDi 55215.
    KEGGi hsa:55215.
    UCSCi uc002bnm.1. human. [Q9NVI1-1 ]
    uc002bno.3. human. [Q9NVI1-4 ]
    uc002bnp.1. human. [Q9NVI1-2 ]
    uc002bnq.1. human. [Q9NVI1-3 ]

    Organism-specific databases

    CTDi 55215.
    GeneCardsi GC15P089787.
    GeneReviewsi FANCI.
    H-InvDB HIX0012562.
    HGNCi HGNC:25568. FANCI.
    HPAi HPA039972.
    MIMi 227650. phenotype.
    609053. phenotype.
    611360. gene.
    neXtProti NX_Q9NVI1.
    Orphaneti 84. Fanconi anemia.
    PharmGKBi PA162387928.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG324185.
    HOVERGENi HBG106622.
    InParanoidi Q9NVI1.
    KOi K10895.
    OMAi SQEEDFN.
    PhylomeDBi Q9NVI1.
    TreeFami TF323694.

    Enzyme and pathway databases

    Reactomei REACT_18265. Regulation of the Fanconi anemia pathway.
    REACT_18410. Fanconi Anemia pathway.

    Miscellaneous databases

    GeneWikii FANCI.
    GenomeRNAii 55215.
    NextBioi 59172.
    PROi Q9NVI1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NVI1.
    Bgeei Q9NVI1.
    CleanExi HS_FANCI.
    Genevestigatori Q9NVI1.

    Family and domain databases

    InterProi IPR026171. FANCI.
    IPR029310. FANCI_HD1.
    IPR029312. FANCI_HD2.
    IPR029308. FANCI_S1.
    IPR029305. FANCI_S1-cap.
    IPR029315. FANCI_S2.
    IPR029313. FANCI_S3.
    IPR029314. FANCI_S4.
    [Graphical view ]
    PANTHERi PTHR21818:SF0. PTHR21818:SF0. 1 hit.
    Pfami PF14679. FANCI_HD1. 1 hit.
    PF14680. FANCI_HD2. 1 hit.
    PF14675. FANCI_S1. 1 hit.
    PF14674. FANCI_S1-cap. 1 hit.
    PF14676. FANCI_S2. 1 hit.
    PF14677. FANCI_S3. 1 hit.
    PF14678. FANCI_S4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, UBIQUITINATION AT LYS-523, PHOSPHORYLATION AT SER-730; THR-952 AND SER-1121, SUBCELLULAR LOCATION, INTERACTION WITH FANCD2, VARIANTS FA LEU-55 AND GLN-1285, CHARACTERIZATION OF VARIANTS FA LEU-55 AND GLN-1285.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, UBIQUITINATION AT LYS-523, SUBCELLULAR LOCATION, INTERACTION WITH FANCD2, VARIANT FA TYR-858.
    3. "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].
    4. "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 3 AND 4), VARIANT VAL-86.
      Tissue: Brain and Skin.
    5. "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] OF 175-1324 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 342-1328 (ISOFORM 1), VARIANT SER-742.
      Tissue: Teratocarcinoma.
    6. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
      DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 527-1328 (ISOFORM 3), VARIANT SER-742.
      Tissue: Brain.
    7. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 438-447; 781-788; 809-819; 885-897; 965-994 AND 1079-1094, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Identification of the Fanconi anemia complementation group I gene, FANCI."
      Dorsman J.C., Levitus M., Rockx D., Rooimans M.A., Oostra A.B., Haitjema A., Bakker S.T., Steltenpool J., Schuler D., Mohan S., Schindler D., Arwert F., Pals G., Mathew C.G., Waisfisz Q., de Winter J.P., Joenje H.
      Cell. Oncol. 29:211-218(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, VARIANT FANCI GLN-1285, VARIANT LEU-55.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Mechanistic insight into site-restricted monoubiquitination of FANCD2 by Ube2t, FANCL, and FANCI."
      Alpi A.F., Pace P.E., Babu M.M., Patel K.J.
      Mol. Cell 32:767-777(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "FANCI binds branched DNA and is monoubiquitinated by UBE2T-FANCL."
      Longerich S., San Filippo J., Liu D., Sung P.
      J. Biol. Chem. 284:23182-23186(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, UBIQUITINATION AT LYS-523, MUTAGENESIS OF LYS-523.
    15. "Replication stress induces sister-chromatid bridging at fragile site loci in mitosis."
      Chan K.L., Palmai-Pallag T., Ying S., Hickson I.D.
      Nat. Cell Biol. 11:753-760(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    16. "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: INTERACTION WITH MTMR15.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Structural analysis of human FANCL, the E3 ligase in the Fanconi anemia pathway."
      Hodson C., Cole A.R., Lewis L.P., Miles J.A., Purkiss A., Walden H.
      J. Biol. Chem. 286:32628-32637(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FANCL.

    Entry informationi

    Entry nameiFANCI_HUMAN
    AccessioniPrimary (citable) accession number: Q9NVI1
    Secondary accession number(s): A4ZVE4
    , A5YMH4, A6NJZ0, Q96JN1, Q96ST0, Q9BT96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 106 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

    Complete proteome, Direct protein sequencing, 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

    External Data

    Dasty 3