Q9NW38 (FANCL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	FANCL
Synonyms:	PHF9

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5 Ref.8 Ref.9 Ref.11 Ref.12
Pathway	Protein modification; protein ubiquitination.
Subunit structure	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. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14
Subcellular location	Cytoplasm. Nucleus Ref.5 Ref.10.
Domain	The UBC-RWD region (URD) region mediates interaction with FANCI and FANCD2 (Ref.14).
Post-translational modification	The RING-type zinc finger domain is monoubiquitinated in the presence of UBE2T and UBE2W.
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.6
Sequence similarities	Contains 1 RING-type zinc finger.
Caution	Although Ref.4 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.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Fanconi anemia
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from mutant phenotype Ref.8. Source: UniProtKB gamete generation Inferred from electronic annotation. Source: Compara protein monoubiquitination Inferred from direct assay Ref.8. Source: UniProtKB regulation of cell proliferation Inferred from electronic annotation. Source: Compara
Cellular_component	Fanconi anaemia nuclear complex Inferred from direct assay PubMed 20347428Ref.13. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear envelope Inferred from electronic annotation. Source: Compara
Molecular_function	ubiquitin-protein ligase activity Inferred from direct assay Ref.8Ref.11. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NW38-1)

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: Q9NW38-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 375

375

E3 ubiquitin-protein ligase FANCL

PRO_0000055908

Regions

Zinc finger

307 – 365

59

RING-type

Region

104 – 294

191

UBC-RWD region (URD)

Natural variations

Alternative sequence

178

1

T → TPQVNS in isoform 2.

VSP_041727

Natural variant

144

1

S → F.
Corresponds to variant rs36059257 [ dbSNP | Ensembl ].

VAR_052082

Experimental info

Mutagenesis

127 – 128

2

VY → AA: Does not affect interaction with FANCI and FANCD2.

Mutagenesis

149

1

L → A: Does not affect interaction with FANCI and FANCD2; when associatec witt A-166. Ref.14

Mutagenesis

158 – 159

2

YP → AA: Abolishes UBE2T charging.

Mutagenesis

166

1

F → A: Does not affect interaction with FANCI and FANCD2; when associatec witt A-149. Ref.14

Mutagenesis

212 – 214

3

WVL → AVA: Impairs interaction with FANCI and FANCD2. Ref.14

Mutagenesis

248

1

L → A: Impairs interaction with FANCI and FANCD2; when associatec witt A-252. Ref.14

Mutagenesis

252

1

F → A: Impairs interaction with FANCI and FANCD2; when associatec witt A-248. Ref.14

Mutagenesis

254

1

L → A: Impairs interaction with FANCI and FANCD2; when associatec witt A-265. Ref.14

Mutagenesis

265

1

I → A: Impairs interaction with FANCI and FANCD2; when associatec witt A-254. Ref.14

Mutagenesis

307

1

C → A: Abolishes ubiquitin ligase activity. Ref.5 Ref.8 Ref.9 Ref.11 Ref.12

Mutagenesis

310

1

C → A: Abolishes ubiquitin ligase activity. Ref.5 Ref.9

Mutagenesis

341

1

W → G: Abolishes interaction with UBE2T and ubiquitin ligase activity. Ref.8

Mutagenesis

359

1

C → A: Abolishes ubiquitin ligase activity. Ref.11

Sequence conflict

77

1

S → P in BAA91548. Ref.1

Secondary structure

1

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375

Helix Strand Turn

Details...

Helix

114 – 121

8

Helix

123 – 125

3

Beta strand

126 – 129

4

Beta strand

133 – 141

9

Beta strand

147 – 153

7

Turn

156 – 160

5

Beta strand

164 – 166

3

Helix

183 – 196

14

Helix

198 – 210

13

Beta strand

213 – 218

6

Beta strand

225 – 231

7

Beta strand

234 – 239

6

Beta strand

250 – 255

6

Helix

257 – 270

14

Helix

271 – 273

3

Helix

280 – 288

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: E217DF9D64587E5E	FASTA	375	42,905
	10 20 30 40 50 60 MAVTEASLLR QCPLLLPQNR SKTVYEGFIS AQGRDFHLRI VLPEDLQLKN ARLLCSWQLR 70 80 90 100 110 120 TILSGYHRIV QQRMQHSPDL MSFMMELKML LEVALKNRQE LYALPPPPQF YSSLIEEIGT 130 140 150 160 170 180 LGWDKLVYAD TCFSTIKLKA EDASGREHLI TLKLKAKYPA ESPDYFVDFP VPFCASWTPQ 190 200 210 220 230 240 SSLISIYSQF LAAIESLKAF WDVMDEIDEK TWVLEPEKPP RSATARRIAL GNNVSINIEV 250 260 270 280 290 300 DPRHPTMLPE CFFLGADHVV KPLGIKLSRN IHLWDPENSV LQNLKDVLEI DFPARAILEK 310 320 330 340 350 360 SDFTMDCGIC YAYQLDGTIP DQVCDNSQCG QPFHQICLYE WLRGLLTSRQ SFNIIFGECP 370 YCSKPITLKM SGRKH
	Isoform 2 [UniParc]. Checksum: A5FA331CCC1C9C1E	FASTA	380	43,430
	10 20 30 40 50 60 MAVTEASLLR QCPLLLPQNR SKTVYEGFIS AQGRDFHLRI VLPEDLQLKN ARLLCSWQLR 70 80 90 100 110 120 TILSGYHRIV QQRMQHSPDL MSFMMELKML LEVALKNRQE LYALPPPPQF YSSLIEEIGT 130 140 150 160 170 180 LGWDKLVYAD TCFSTIKLKA EDASGREHLI TLKLKAKYPA ESPDYFVDFP VPFCASWTPQ 190 200 210 220 230 240 VNSPQSSLIS IYSQFLAAIE SLKAFWDVMD EIDEKTWVLE PEKPPRSATA RRIALGNNVS 250 260 270 280 290 300 INIEVDPRHP TMLPECFFLG ADHVVKPLGI KLSRNIHLWD PENSVLQNLK DVLEIDFPAR 310 320 330 340 350 360 AILEKSDFTM DCGICYAYQL DGTIPDQVCD NSQCGQPFHQ ICLYEWLRGL LTSRQSFNII 370 380 FGECPYCSKP ITLKMSGRKH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"A novel ubiquitin ligase is deficient in Fanconi anemia." Meetei A.R., de Winter J.P., Medhurst A.L., Wallisch M., Waisfisz Q., van de Vrugt H.J., Oostra A.B., Yan Z., Ling C., Bishop C.E., Hoatlin M.E., Joenje H., Wang W. Nat. Genet. 35:165-170(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN FANCL, INTERACTION WITH FANCA; FANCC; FANCF AND FANCG, MUTAGENESIS OF CYS-307 AND CYS-310.
[6]	"X-linked inheritance of Fanconi anemia complementation group B." Meetei A.R., Levitus M., Xue Y., Medhurst A.L., Zwaan M., Ling C., Rooimans M.A., Bier P., Hoatlin M., Pals G., de Winter J.P., Wang W., Joenje H. Nat. Genet. 36:1219-1224(2004) [PubMed] [Europe PMC] [Abstract] 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]	"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.
+	Additional computationally mapped references.

Web resources

Fanconi Anemia Mutation Database

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00018099.
IPI00885015.

RefSeq

NP_001108108.1. NM_001114636.1.
NP_060532.2. NM_018062.3.

UniGene

Hs.741421.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ZQS	X-ray	2.00	A/B	109-294	[»]

ProteinModelPortal

Q9NW38.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NW38. 1 interaction.

MINT

MINT-2819517.

STRING

9606.ENSP00000385021.

PTM databases

PhosphoSite

Q9NW38.

Polymorphism databases

DMDM

116241360.

Proteomic databases

PaxDb

Q9NW38.

PRIDE

Q9NW38.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000233741; ENSP00000233741; ENSG00000115392.
ENST00000402135; ENSP00000385021; ENSG00000115392.

GeneID

55120.

KEGG

hsa:55120.

UCSC

uc002rzw.4. human.
uc002rzx.4. human.

Organism-specific databases

CTD

55120.

GeneCards

GC02M058298.

HGNC

HGNC:20748. FANCL.

HPA

CAB033842.
HPA036685.
HPA036686.

MIM

608111. gene.
614083. phenotype.

neXtProt

NX_Q9NW38.

Orphanet

84. Fanconi anemia.

PharmGKB

PA134887656.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG311231.

HOGENOM

HOG000007643.

HOVERGEN

HBG045632.

KO

K10606.

OMA

CFVDFPV.

PhylomeDB

Q9NW38.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway. BARD1 signaling events.

Reactome

REACT_216. DNA Repair.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q9NW38.

Bgee

Q9NW38.

CleanEx

HS_FANCL.

Genevestigator

Q9NW38.

GermOnline

ENSG00000115392. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR026848. Fancl.
IPR019162. FancL_WD-rpt_cont_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

PANTHER

PTHR13206:SF0. PTHR13206:SF0. 1 hit.

Pfam

PF09765. WD-3. 1 hit.
[Graphical view]

SMART

SM00184. RING. 1 hit.
[Graphical view]

PROSITE

PS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

Fancl. human.

GenomeRNAi

55120.

NextBio

58768.

SOURCE

Search...

Entry information

Entry name

FANCL_HUMAN

Accession

Primary (citable) accession number: Q9NW38
Secondary accession number(s): Q6GU60

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2003
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.