Q99732 (LITAF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipopolysaccharide-induced tumor necrosis factor-alpha factor
Short name=LPS-induced TNF-alpha factor

Alternative name(s):
Small integral membrane protein of lysosome/late endosome
p53-induced gene 7 protein

Gene names

Name:	LITAF
Synonyms:	PIG7, SIMPLE

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	161 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable role in regulating transcription of specific genes. May regulate through NFKB1 the expression of the CCL2/MCP-1 chemokine. May play a role in tumor necrosis factor alpha (TNF-alpha) gene expression.
Subunit structure	Interacts with NEDD4 By similarity. Interacts with WWOX. Isoform 2 may interact with STAT6. Ref.9 Ref.10
Subcellular location	Lysosome membrane; Peripheral membrane protein; Cytoplasmic side. Note: Associated with membranes of lysosomes. Ref.3
Tissue specificity	Ubiquitously and abundantly expressed. Expressed predominantly in the placenta, peripheral blood leukocytes, lymph nodes and spleen. Ref.2 Ref.3
Induction	By bacterial lipopolysaccharides (LPS) or p53/TP53. In monocytes by the Bacillus Calmette-Guerin (BCG). Ref.1 Ref.2 Ref.3
Domain	The WW-binding motif mediates interaction with WWOX and, probably NEDD4. Ref.9
Involvement in disease	Charcot-Marie-Tooth disease 1C (CMT1C) [MIM:601098]: A dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.13 Ref.14 Defects in LITAF may be involved in extramammary Paget disease (EMPD) carcinogenesis. EMPD is a cancerous disease representing about 8% of all malignant skin cancers; it usually appears in the anogenital area and can be fatal by metastasizing to internal organs when left untreated for a long time. The clinical features are usually those of eczematous eruptions with weeping and crust formation. Ref.12

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation
Cellular component	Lysosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Charcot-Marie-Tooth disease Disease mutation Neuropathy Proto-oncogene
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular response to lipopolysaccharide Inferred from electronic annotation. Source: Compara negative regulation of NF-kappaB import into nucleus Inferred from electronic annotation. Source: Compara positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB regulation of cytokine production Inferred from electronic annotation. Source: Compara regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.2. Source: ProtInc transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay Ref.9. Source: UniProtKB lysosomal membrane Inferred from direct assay Ref.3. Source: MGI plasma membrane Inferred from mutant phenotype PubMed 16118794. Source: UniProtKB
Molecular_function	signal transducer activity Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NEDD4	P46934	4	EBI-725647,EBI-726944
TSG101	Q99816	3	EBI-725647,EBI-346882
WWOX	Q9NZC7	5	EBI-725647,EBI-4320739

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q99732-1)

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: Q99732-2)

The sequence of this isoform differs from the canonical sequence as follows:
     127-161: CIAGCCFIPFCVDALQDVDHYCPNCRALLGTYKRL → VHSGLLLHPL...TPEIAAWSRA

Note: May be due to a frameshift that creates an unconventional splicing site. Data inferred from this isoform must be interpreted with caution.

Isoform 3 (identifier: Q99732-3)

The sequence of this isoform differs from the canonical sequence as follows:
     127-161: CIAGCCFIPFCVDALQDVDHYCPNCRALLGTYKRL → QECSGTIVALRSFDLLGSCNPPSSAS

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 161	161	Lipopolysaccharide-induced tumor necrosis factor-alpha factor		PRO_0000084440
Regions
	Motif	20 – 23	4	WW-binding
Natural variations
	Alternative sequence	127 – 161	35	CIAGC…TYKRL → VHSGLLLHPLLRGCPAGRGP LLSQLQSSPGHLQAFVGLSQ TWREPGAAGSPFHLSSSFTP GGGSALVVSPLQGAHLHVFF WGEYVAKLTNLQTPEIAAWS RA in isoform 2.		VSP_016461
	Alternative sequence	127 – 161	35	CIAGC…TYKRL → QECSGTIVALRSFDLLGSCN PPSSAS in isoform 3.		VSP_045701
	Natural variant	23	1	Y → H in one EMPD primary tumor; somatic mutation. Ref.12		VAR_024014
	Natural variant	49	1	T → M in CMT1C. Ref.14		VAR_024015
	Natural variant	92	1	I → V. Ref.13 Ref.14 Corresponds to variant rs4280262 [ dbSNP | Ensembl ].		VAR_024016
	Natural variant	112	1	G → S in CMT1C. Ref.11 Ref.13 Ref.14		VAR_024017
	Natural variant	115	1	T → N in CMT1C. Ref.11		VAR_024018
	Natural variant	116	1	W → G in CMT1C. Ref.11		VAR_024019
	Natural variant	122	1	L → V in CMT1C. Ref.14		VAR_024020
Isoform 2:
	Natural variant	174	1	A → S Found as a somatic mutation in a EMPD primary tumor.
Experimental info
	Mutagenesis	23	1	Y → A: Abolishes interactions with WWOX. Ref.9
	Mutagenesis	61	1	Y → A: No effect on interaction with WWOX. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: 08D15BF1FDCA16F0	FASTA	161	17,107
	10 20 30 40 50 60 MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS 70 80 90 100 110 120 YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG 130 140 150 160 SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L
	Isoform 2 [UniParc]. Checksum: 2672B55AD96FC4B5	FASTA	228	23,903
	10 20 30 40 50 60 MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS 70 80 90 100 110 120 YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG 130 140 150 160 170 180 SLCLLGVHSG LLLHPLLRGC PAGRGPLLSQ LQSSPGHLQA FVGLSQTWRE PGAAGSPFHL 190 200 210 220 SSSFTPGGGS ALVVSPLQGA HLHVFFWGEY VAKLTNLQTP EIAAWSRA
	Isoform 3 [UniParc]. Checksum: E2270BD322D63344	FASTA	152	15,824
	10 20 30 40 50 60 MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS 70 80 90 100 110 120 YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG 130 140 150 SLCLLGQECS GTIVALRSFD LLGSCNPPSS AS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A model for p53-induced apoptosis." Polyak K., Xia Y., Zweier J.L., Kinzler K.W., Vogelstein B. Nature 389:300-306(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION BY TP53. Tissue: Colon cancer.
[2]	"A novel lipopolysaccharide-induced transcription factor regulating tumor necrosis factor alpha gene expression: molecular cloning, sequencing, characterization, and chromosomal assignment." Myokai F., Takashiba S., Lebo R., Amar S. Proc. Natl. Acad. Sci. U.S.A. 96:4518-4523(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, TISSUE SPECIFICITY. Tissue: Monocyte.
[3]	"Mycobacterium bovis Bacillus Calmette-Guerin and its cell wall complex induce a novel lysosomal membrane protein, SIMPLE, that bridges the missing link between lipopolysaccharide and p53-inducible gene, LITAF(PIG7), and estrogen-inducible gene, EET-1." Moriwaki Y., Begum N.A., Kobayashi M., Matsumoto M., Toyoshima K., Seya T. J. Biol. Chem. 276:23065-23076(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION. Tissue: Monocyte.
[4]	"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 3). Tissue: Hair follicle dermal papilla.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Esophageal carcinoma.
[6]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Kidney, Pancreas, PNS and Skin.
[9]	"WWOX binds the specific proline-rich ligand PPXY: identification of candidate interacting proteins." Ludes-Meyers J.H., Kil H., Bednarek A.K., Drake J., Bedford M.T., Aldaz C.M. Oncogene 23:5049-5055(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WWOX, DOMAIN, MUTAGENESIS OF TYR-23 AND TYR-61.
[10]	"LPS induces the interaction of a transcription factor, LPS-induced TNF-alpha factor, and STAT6(B) with effects on multiple cytokines." Tang X., Marciano D.L., Leeman S.E., Amar S. Proc. Natl. Acad. Sci. U.S.A. 102:5132-5137(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH STAT6.
[11]	"Mutation of a putative protein degradation gene LITAF/SIMPLE in Charcot-Marie-Tooth disease 1C." Street V.A., Bennett C.L., Goldy J.D., Shirk A.J., Kleopa K.A., Tempel B.L., Lipe H.P., Scherer S.S., Bird T.D., Chance P.F. Neurology 60:22-26(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMT1C SER-112; ASN-115 AND GLY-116.
[12]	"PIG7/LITAF gene mutation and overexpression of its gene product in extramammary Paget's disease." Matsumura Y., Matsumura Y., Nishigori C., Horio T., Miyachi Y. Int. J. Cancer 111:218-223(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT EMPD HIS-23.
[13]	"Early onset neuropathy in a compound form of Charcot-Marie-Tooth disease." Meggouh F., de Visser M., Arts W.F.M., De Coo R.I.F.M., van Schaik I.N., Baas F. Ann. Neurol. 57:589-591(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CMT1C SER-112, VARIANT VAL-92.
[14]	"SIMPLE mutations in Charcot-Marie-Tooth disease and the potential role of its protein product in protein degradation." Saifi G.M., Szigeti K., Wiszniewski W., Shy M.E., Krajewski K., Hausmanowa-Petrusewicz I., Kochanski A., Reeser S., Mancias P., Butler I., Lupski J.R. Hum. Mutat. 25:372-383(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMT1C MET-49; SER-112 AND VAL-122, VARIANT VAL-92.
+	Additional computationally mapped references.

Web resources

Inherited peripheral neuropathies mutation db

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF010312 mRNA. Translation: AAC39530.1. U77396 mRNA. Translation: AAB36550.1. AB034747 mRNA. Translation: BAB32547.1. AK095955 mRNA. No translation available. BX537543 mRNA. Translation: CAD97778.1. AC007616 Genomic DNA. No translation available. AC099489 Genomic DNA. No translation available. CH471112 Genomic DNA. Translation: EAW85150.1. CH471112 Genomic DNA. Translation: EAW85151.1. CH471112 Genomic DNA. Translation: EAW85152.1. CH471112 Genomic DNA. Translation: EAW85153.1. BC000053 mRNA. Translation: AAH00053.1. BC008309 mRNA. Translation: AAH08309.1. BC016491 mRNA. Translation: AAH16491.1. BC039840 mRNA. Translation: AAH39840.1. BC046154 mRNA. Translation: AAH46154.1. BC096063 mRNA. Translation: AAH96063.1. BC096065 mRNA. Translation: AAH96065.1. BC096066 mRNA. Translation: AAH96066.1. BC101401 mRNA. Translation: AAI01402.1. BC101402 mRNA. Translation: AAI01403.1. BC101969 mRNA. Translation: AAI01970.1.
IPI	IPI00017762. IPI00645256.
RefSeq	NP_001129944.1. NM_001136472.1. NP_001129945.1. NM_001136473.1. NP_004853.2. NM_004862.3.
UniGene	Hs.459940.
3D structure databases
ProteinModelPortal	Q99732.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99732. 6 interactions.
MINT	MINT-1391850.
STRING	9606.ENSP00000340118.
PTM databases
PhosphoSite	Q99732.
Polymorphism databases
DMDM	83304387.
Proteomic databases
PRIDE	Q99732.
Protocols and materials databases
DNASU	9516.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000339430; ENSP00000340118; ENSG00000189067. ENST00000381810; ENSP00000371231; ENSG00000189067. ENST00000413364; ENSP00000397958; ENSG00000189067. ENST00000570904; ENSP00000459138; ENSG00000189067. ENST00000571688; ENSP00000459533; ENSG00000189067. ENST00000574763; ENSP00000461813; ENSG00000189067. ENST00000576036; ENSP00000461667; ENSG00000189067.
GeneID	9516.
KEGG	hsa:9516.
UCSC	uc002daz.3. human.
Organism-specific databases
CTD	9516.
GeneCards	GC16M011641.
H-InvDB	HIX0134387.
HGNC	HGNC:16841. LITAF.
HPA	HPA006960.
MIM	601098. phenotype. 603795. gene.
neXtProt	NX_Q99732.
Orphanet	101083. Charcot-Marie-Tooth disease type 1C.
PharmGKB	PA134879224.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG41852.
HOGENOM	HOG000039585.
HOVERGEN	HBG006272.
PhylomeDB	Q99732.
Gene expression databases
ArrayExpress	Q99732.
Bgee	Q99732.
CleanEx	HS_LITAF.
Genevestigator	Q99732.
GermOnline	ENSG00000189067. Homo sapiens.
Family and domain databases
InterPro	IPR006629. LITAF. [Graphical view]
Pfam	PF10601. zf-LITAF-like. 1 hit. [Graphical view]
SMART	SM00714. LITAF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q99732.
ChiTaRS	LITAF. human.
GenomeRNAi	9516.
NextBio	35662.
SOURCE	Search...

Entry information

Entry name

LITAF_HUMAN

Accession

Primary (citable) accession number: Q99732
Secondary accession number(s): D3DUG1 , G5E9K0, Q05DW0, Q9C0L6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 6, 2005
Last modified:	May 1, 2013
This is version 115 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.