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Q9NW38

- FANCL_HUMAN

UniProt

Q9NW38 - FANCL_HUMAN

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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

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
Complete GO annotation...

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-KW
  2. Fanconi anaemia nuclear complex Source: UniProtKB
  3. nuclear envelope Source: Ensembl
  4. nucleoplasm Source: Reactome
Complete GO annotation...

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. 1 Publication
Mutagenesisi149 – 1491L → A: Does not affect interaction with FANCI and FANCD2; when associatec witt A-166. 1 Publication
Mutagenesisi158 – 1592YP → AA: Abolishes UBE2T charging. 1 Publication
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. 1 Publication
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

BgeeiQ9NW38.
CleanExiHS_FANCL.
ExpressionAtlasiQ9NW38. baseline and differential.
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.
GeneTreeiENSGT00390000005537.
HOGENOMiHOG000007643.
HOVERGENiHBG045632.
InParanoidiQ9NW38.
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

        10         20         30         40         50
MAVTEASLLR QCPLLLPQNR SKTVYEGFIS AQGRDFHLRI VLPEDLQLKN
60 70 80 90 100
ARLLCSWQLR TILSGYHRIV QQRMQHSPDL MSFMMELKML LEVALKNRQE
110 120 130 140 150
LYALPPPPQF YSSLIEEIGT LGWDKLVYAD TCFSTIKLKA EDASGREHLI
160 170 180 190 200
TLKLKAKYPA ESPDYFVDFP VPFCASWTPQ SSLISIYSQF LAAIESLKAF
210 220 230 240 250
WDVMDEIDEK TWVLEPEKPP RSATARRIAL GNNVSINIEV DPRHPTMLPE
260 270 280 290 300
CFFLGADHVV KPLGIKLSRN IHLWDPENSV LQNLKDVLEI DFPARAILEK
310 320 330 340 350
SDFTMDCGIC YAYQLDGTIP DQVCDNSQCG QPFHQICLYE WLRGLLTSRQ
360 370
SFNIIFGECP YCSKPITLKM SGRKH
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.
GeneTreei ENSGT00390000005537.
HOGENOMi HOG000007643.
HOVERGENi HBG045632.
InParanoidi Q9NW38.
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

Bgeei Q9NW38.
CleanExi HS_FANCL.
ExpressionAtlasi Q9NW38. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 127 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