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Q9NW38

- FANCL_HUMAN

UniProt

Q9NW38 - FANCL_HUMAN

Protein

E3 ubiquitin-protein ligase FANCL

Gene

FANCL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Ubiquitin ligase protein that mediates monoubiquitination of FANCD2, a key step in the DNA damage pathway. Also mediates monoubiquitination of FANCI. May stimulate the ubiquitin release from UBE2W. May be required for proper primordial germ cell proliferation in the embryonic stage, whereas it is probably not needed for spermatogonial proliferation after birth.5 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri307 – 36559RING-typeAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. ubiquitin protein ligase binding Source: UniProtKB
    3. ubiquitin-protein transferase activity Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: UniProtKB
    2. DNA repair Source: UniProtKB
    3. gamete generation Source: Ensembl
    4. protein monoubiquitination Source: UniProtKB
    5. regulation of cell proliferation Source: Ensembl

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_18410. Fanconi Anemia pathway.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase FANCL (EC:6.3.2.-)
    Alternative name(s):
    Fanconi anemia group L protein
    Fanconi anemia-associated polypeptide of 43 kDa
    Short name:
    FAAP43
    Gene namesi
    Name:FANCL
    Synonyms:PHF9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:20748. FANCL.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. Fanconi anaemia nuclear complex Source: UniProtKB
    3. nuclear envelope Source: Ensembl
    4. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Fanconi anemia complementation group L (FANCL) [MIM:614083]: 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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi127 – 1282VY → AA: Does not affect interaction with FANCI and FANCD2.
    Mutagenesisi149 – 1491L → A: Does not affect interaction with FANCI and FANCD2; when associatec witt A-166. 1 Publication
    Mutagenesisi158 – 1592YP → AA: Abolishes UBE2T charging.
    Mutagenesisi166 – 1661F → A: Does not affect interaction with FANCI and FANCD2; when associatec witt A-149. 1 Publication
    Mutagenesisi212 – 2143WVL → AVA: Impairs interaction with FANCI and FANCD2.
    Mutagenesisi248 – 2481L → A: Impairs interaction with FANCI and FANCD2; when associatec witt A-252. 1 Publication
    Mutagenesisi252 – 2521F → A: Impairs interaction with FANCI and FANCD2; when associatec witt A-248. 1 Publication
    Mutagenesisi254 – 2541L → A: Impairs interaction with FANCI and FANCD2; when associatec witt A-265. 1 Publication
    Mutagenesisi265 – 2651I → A: Impairs interaction with FANCI and FANCD2; when associatec witt A-254. 1 Publication
    Mutagenesisi307 – 3071C → A: Abolishes ubiquitin ligase activity. 5 Publications
    Mutagenesisi310 – 3101C → A: Abolishes ubiquitin ligase activity. 2 Publications
    Mutagenesisi341 – 3411W → G: Abolishes interaction with UBE2T and ubiquitin ligase activity. 1 Publication
    Mutagenesisi359 – 3591C → A: Abolishes ubiquitin ligase activity. 1 Publication

    Keywords - Diseasei

    Fanconi anemia

    Organism-specific databases

    MIMi614083. phenotype.
    Orphaneti84. Fanconi anemia.
    PharmGKBiPA134887656.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 375374E3 ubiquitin-protein ligase FANCLPRO_0000055908Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Post-translational modificationi

    The RING-type zinc finger domain is monoubiquitinated in the presence of UBE2T and UBE2W.

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NW38.
    PaxDbiQ9NW38.
    PRIDEiQ9NW38.

    PTM databases

    PhosphoSiteiQ9NW38.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NW38.
    BgeeiQ9NW38.
    CleanExiHS_FANCL.
    GenevestigatoriQ9NW38.

    Organism-specific databases

    HPAiCAB033842.
    HPA036685.
    HPA036686.

    Interactioni

    Subunit structurei

    Interacts with GGN By similarity. Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. The complex is not found in FA patients. In complex with FANCF, FANCA and FANCG, but not with FANCC, nor FANCE, interacts with HES1; this interaction may be essential for the stability and nuclear localization of FA core complex proteins. Interacts with FANCI. Interacts (via the RING-type zinc finger) with UBE2T and UBE2W.By similarity9 Publications

    Protein-protein interaction databases

    BioGridi120429. 24 interactions.
    DIPiDIP-43975N.
    IntActiQ9NW38. 4 interactions.
    MINTiMINT-2819517.
    STRINGi9606.ENSP00000385021.

    Structurei

    Secondary structure

    1
    375
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi114 – 1218
    Helixi123 – 1253
    Beta strandi126 – 1294
    Beta strandi133 – 1419
    Beta strandi147 – 1537
    Turni156 – 1605
    Beta strandi164 – 1663
    Helixi183 – 19614
    Helixi198 – 21013
    Beta strandi213 – 2186
    Beta strandi225 – 2317
    Beta strandi234 – 2396
    Beta strandi250 – 2556
    Helixi257 – 27014
    Helixi271 – 2733
    Helixi280 – 2889
    Turni308 – 3103
    Turni327 – 3293
    Helixi335 – 3428
    Beta strandi349 – 3513
    Beta strandi354 – 3585
    Turni360 – 3623
    Beta strandi365 – 3695

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZQSX-ray2.00A/B109-294[»]
    4CCGX-ray2.40X/Y288-375[»]
    ProteinModelPortaliQ9NW38.
    SMRiQ9NW38. Positions 109-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni104 – 294191UBC-RWD region (URD)Add
    BLAST

    Domaini

    The UBC-RWD region (URD) region mediates interaction with FANCI and FANCD2.1 Publication

    Sequence similaritiesi

    Contains 1 RING-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri307 – 36559RING-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG311231.
    HOGENOMiHOG000007643.
    HOVERGENiHBG045632.
    KOiK10606.
    OMAiWTPQSSL.
    PhylomeDBiQ9NW38.
    TreeFamiTF323571.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR026848. Fancl.
    IPR019162. FancL_WD-rpt_cont_dom.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PANTHERiPTHR13206:SF0. PTHR13206:SF0. 1 hit.
    PfamiPF09765. WD-3. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NW38-1) [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

    MAVTEASLLR QCPLLLPQNR SKTVYEGFIS AQGRDFHLRI VLPEDLQLKN    50
    ARLLCSWQLR TILSGYHRIV QQRMQHSPDL MSFMMELKML LEVALKNRQE 100
    LYALPPPPQF YSSLIEEIGT LGWDKLVYAD TCFSTIKLKA EDASGREHLI 150
    TLKLKAKYPA ESPDYFVDFP VPFCASWTPQ SSLISIYSQF LAAIESLKAF 200
    WDVMDEIDEK TWVLEPEKPP RSATARRIAL GNNVSINIEV DPRHPTMLPE 250
    CFFLGADHVV KPLGIKLSRN IHLWDPENSV LQNLKDVLEI DFPARAILEK 300
    SDFTMDCGIC YAYQLDGTIP DQVCDNSQCG QPFHQICLYE WLRGLLTSRQ 350
    SFNIIFGECP YCSKPITLKM SGRKH 375
    Length:375
    Mass (Da):42,905
    Last modified:October 17, 2006 - v2
    Checksum:iE217DF9D64587E5E
    GO
    Isoform 2 (identifier: Q9NW38-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         178-178: T → TPQVNS

    Show »
    Length:380
    Mass (Da):43,430
    Checksum:iA5FA331CCC1C9C1E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771S → P in BAA91548. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti144 – 1441S → F.
    Corresponds to variant rs36059257 [ dbSNP | Ensembl ].
    VAR_052082

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei178 – 1781T → TPQVNS in isoform 2. 1 PublicationVSP_041727

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK001197 mRNA. Translation: BAA91548.1.
    AC007250 Genomic DNA. Translation: AAY15020.1.
    BC009042 mRNA. Translation: AAH09042.1.
    BC054517 mRNA. Translation: AAH54517.1.
    BC037570 mRNA. No translation available.
    CCDSiCCDS1860.1. [Q9NW38-1]
    CCDS46294.1. [Q9NW38-2]
    RefSeqiNP_001108108.1. NM_001114636.1. [Q9NW38-2]
    NP_060532.2. NM_018062.3. [Q9NW38-1]
    UniGeneiHs.631890.

    Genome annotation databases

    EnsembliENST00000233741; ENSP00000233741; ENSG00000115392. [Q9NW38-1]
    ENST00000402135; ENSP00000385021; ENSG00000115392. [Q9NW38-2]
    GeneIDi55120.
    KEGGihsa:55120.
    UCSCiuc002rzw.4. human. [Q9NW38-1]
    uc002rzx.4. human. [Q9NW38-2]

    Polymorphism databases

    DMDMi116241360.

    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
    AK001197 mRNA. Translation: BAA91548.1 .
    AC007250 Genomic DNA. Translation: AAY15020.1 .
    BC009042 mRNA. Translation: AAH09042.1 .
    BC054517 mRNA. Translation: AAH54517.1 .
    BC037570 mRNA. No translation available.
    CCDSi CCDS1860.1. [Q9NW38-1 ]
    CCDS46294.1. [Q9NW38-2 ]
    RefSeqi NP_001108108.1. NM_001114636.1. [Q9NW38-2 ]
    NP_060532.2. NM_018062.3. [Q9NW38-1 ]
    UniGenei Hs.631890.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZQS X-ray 2.00 A/B 109-294 [» ]
    4CCG X-ray 2.40 X/Y 288-375 [» ]
    ProteinModelPortali Q9NW38.
    SMRi Q9NW38. Positions 109-373.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120429. 24 interactions.
    DIPi DIP-43975N.
    IntActi Q9NW38. 4 interactions.
    MINTi MINT-2819517.
    STRINGi 9606.ENSP00000385021.

    PTM databases

    PhosphoSitei Q9NW38.

    Polymorphism databases

    DMDMi 116241360.

    Proteomic databases

    MaxQBi Q9NW38.
    PaxDbi Q9NW38.
    PRIDEi Q9NW38.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233741 ; ENSP00000233741 ; ENSG00000115392 . [Q9NW38-1 ]
    ENST00000402135 ; ENSP00000385021 ; ENSG00000115392 . [Q9NW38-2 ]
    GeneIDi 55120.
    KEGGi hsa:55120.
    UCSCi uc002rzw.4. human. [Q9NW38-1 ]
    uc002rzx.4. human. [Q9NW38-2 ]

    Organism-specific databases

    CTDi 55120.
    GeneCardsi GC02M058298.
    GeneReviewsi FANCL.
    HGNCi HGNC:20748. FANCL.
    HPAi CAB033842.
    HPA036685.
    HPA036686.
    MIMi 608111. gene.
    614083. phenotype.
    neXtProti NX_Q9NW38.
    Orphaneti 84. Fanconi anemia.
    PharmGKBi PA134887656.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG311231.
    HOGENOMi HOG000007643.
    HOVERGENi HBG045632.
    KOi K10606.
    OMAi WTPQSSL.
    PhylomeDBi Q9NW38.
    TreeFami TF323571.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_18410. Fanconi Anemia pathway.

    Miscellaneous databases

    ChiTaRSi Fancl. human.
    GeneWikii FANCL.
    GenomeRNAii 55120.
    NextBioi 58768.
    PROi Q9NW38.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NW38.
    Bgeei Q9NW38.
    CleanExi HS_FANCL.
    Genevestigatori Q9NW38.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR026848. Fancl.
    IPR019162. FancL_WD-rpt_cont_dom.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    PANTHERi PTHR13206:SF0. PTHR13206:SF0. 1 hit.
    Pfami PF09765. WD-3. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 1).
      Tissue: Teratocarcinoma.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Eye.
    4. "A multiprotein nuclear complex connects Fanconi anemia and Bloom syndrome."
      Meetei A.R., Sechi S., Wallisch M., Yang D., Young M.K., Joenje H., Hoatlin M.E., Wang W.
      Mol. Cell. Biol. 23:3417-3426(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY IN A BRAFT COMPLEX WITH FANCA; FANCC; FANCE; FANCF AND FANCG.
    5. Cited for: FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN FANCL, INTERACTION WITH FANCA; FANCC; FANCF AND FANCG, MUTAGENESIS OF CYS-307 AND CYS-310.
    6. Cited for: IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCC; FANCE; FANCF AND FANCLG.
    7. "A human ortholog of archaeal DNA repair protein Hef is defective in Fanconi anemia complementation group M."
      Meetei A.R., Medhurst A.L., Ling C., Xue Y., Singh T.R., Bier P., Steltenpool J., Stone S., Dokal I., Mathew C.G., Hoatlin M., Joenje H., de Winter J.P., Wang W.
      Nat. Genet. 37:958-963(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH FANCA; FANCB; FANCC; FANCE; FANCF; FANCG AND FANCM.
    8. "UBE2T is the E2 in the Fanconi anemia pathway and undergoes negative autoregulation."
      Machida Y.J., Machida Y., Chen Y., Gurtan A.M., Kupfer G.M., D'Andrea A.D., Dutta A.
      Mol. Cell 23:589-596(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UBE2T, UBIQUITINATION, MUTAGENESIS OF CYS-307 AND TRP-341.
    9. "UBE2T, the Fanconi anemia core complex, and FANCD2 are recruited independently to chromatin: a basis for the regulation of FANCD2 monoubiquitination."
      Alpi A., Langevin F., Mosedale G., Machida Y.J., Dutta A., Patel K.J.
      Mol. Cell. Biol. 27:8421-8430(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UBE2T, MUTAGENESIS OF CYS-307 AND CYS-310.
    10. "HES1 is a novel interactor of the Fanconi anemia core complex."
      Tremblay C.S., Huang F.F., Habi O., Huard C.C., Godin C., Levesque G., Carreau M.
      Blood 112:2062-2070(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HES1, SUBCELLULAR LOCATION.
    11. "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, INTERACTION WITH UBE2T AND UBE2W, MUTAGENESIS OF 158-TYR-PRO-159; CYS-307 AND CYS-359.
    12. "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: FUNCTION, MUTAGENESIS OF CYS-307.
    13. "FAAP20: a novel ubiquitin-binding FA nuclear core-complex protein required for functional integrity of the FA-BRCA DNA repair pathway."
      Ali A.M., Pradhan A., Singh T.R., Du C., Li J., Wahengbam K., Grassman E., Auerbach A.D., Pang Q., Meetei A.R.
      Blood 119:3285-3294(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE FA COMPLEX.
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. "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: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 109-294, INTERACTION WITH FANCI AND UBE2T, MUTAGENESIS OF 127-VAL-TYR-128; LEU-149; PHE-166; 212-TRP--LEU-214; LEU-248; PHE-252; LEU-254 AND ILE-265.

    Entry informationi

    Entry nameiFANCL_HUMAN
    AccessioniPrimary (citable) accession number: Q9NW38
    Secondary accession number(s): Q6GU60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 10, 2003
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 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

    Caution

    Although PubMed:12724401 reports that it contains a PHD-type zinc finger, it contains a RING-type zinc finger. Moreover, PHD-type zinc fingers do not have any ubiquitin ligase activity.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3