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Q16649

- NFIL3_HUMAN

UniProt

Q16649 - NFIL3_HUMAN

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Protein

Nuclear factor interleukin-3-regulated protein

Gene

NFIL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acts as a transcriptional regulator that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many cellular and viral promoters. Represses transcription from promoters with activating transcription factor (ATF) sites. Represses promoter activity in osteoblasts (By similarity). Represses transcriptional activity of PER1 (By similarity). Represses transcriptional activity of PER2 via the B-site on the promoter (By similarity). Activates transcription from the interleukin-3 promoter in T-cells. Competes for the same consensus-binding site with PAR DNA-binding factors (DBP, HLF and TEF) (By similarity). Component of the circadian clock that acts as a negative regulator for the circadian expression of PER2 oscillation in the cell-autonomous core clock (By similarity). Protects pro-B cells from programmed cell death (By similarity).By similarity

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: BHF-UCL
  3. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
  4. RNA polymerase II regulatory region sequence-specific DNA binding Source: BHF-UCL
  5. sequence-specific DNA binding transcription factor activity Source: ProtInc
  6. transcription corepressor activity Source: ProtInc

GO - Biological processi

  1. cellular response to interleukin-4 Source: Ensembl
  2. circadian rhythm Source: InterPro
  3. immune response Source: ProtInc
  4. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  5. positive regulation of gene expression Source: Ensembl
  6. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiQ16649.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear factor interleukin-3-regulated protein
Alternative name(s):
E4 promoter-binding protein 4
Interleukin-3 promoter transcriptional activator
Interleukin-3-binding protein 1
Transcriptional activator NF-IL3A
Gene namesi
Name:NFIL3
Synonyms:E4BP4, IL3BP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:7787. NFIL3.

Subcellular locationi

Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi330 – 3301K → A: Interacts with DR1 and partially affects transcriptional repression; when associated with E-332. 1 Publication
Mutagenesisi330 – 3301K → E: Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-332. 1 Publication
Mutagenesisi332 – 3321K → A: Interacts with DR1 and partially affects transcriptional repression; when associated with E-330. 1 Publication
Mutagenesisi332 – 3321K → E: Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-330. 1 Publication

Organism-specific databases

PharmGKBiPA31593.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Nuclear factor interleukin-3-regulated proteinPRO_0000292667Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei301 – 3011Phosphoserine2 Publications
Modified residuei353 – 3531Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ16649.
PaxDbiQ16649.
PRIDEiQ16649.

PTM databases

PhosphoSiteiQ16649.

Expressioni

Tissue specificityi

Expressed in bladder stomach, thyroid, spinal cord, lymph node, trachea, adrenal gland, bone marrow and muscle.1 Publication

Inductioni

Up-regulated by PHA or TPA.1 Publication

Gene expression databases

BgeeiQ16649.
CleanExiHS_NFIL3.
GenevestigatoriQ16649.

Organism-specific databases

HPAiHPA003261.

Interactioni

Subunit structurei

Homodimer. Binds DNA as a dimer. Interacts with DR1. Interacts with PER2 and CRY2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi110855. 9 interactions.
IntActiQ16649. 5 interactions.
MINTiMINT-268122.
STRINGi9606.ENSP00000297689.

Structurei

3D structure databases

ProteinModelPortaliQ16649.
SMRiQ16649. Positions 61-124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 13664bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 9517Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni99 – 1068Leucine-zipperPROSITE-ProRule annotation
Regioni299 – 36365Necessary for transcriptional repression and sufficient for interaction with DR1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi155 – 21056Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the bZIP family. NFIL3 subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG260819.
GeneTreeiENSGT00530000064087.
HOGENOMiHOG000059596.
HOVERGENiHBG105717.
InParanoidiQ16649.
KOiK09059.
OMAiWHQKELN.
OrthoDBiEOG7GQXWM.
PhylomeDBiQ16649.
TreeFamiTF328374.

Family and domain databases

InterProiIPR004827. bZIP.
IPR016743. NFIL3/E4BP4.
IPR010533. Vert_IL3-reg_TF.
[Graphical view]
PANTHERiPTHR15284:SF1. PTHR15284:SF1. 1 hit.
PfamiPF07716. bZIP_2. 1 hit.
PF06529. Vert_IL3-reg_TF. 1 hit.
[Graphical view]
PIRSFiPIRSF019029. bZIP_E4BP4. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q16649-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQLRKMQTVK KEQASLDASS NVDKMMVLNS ALTEVSEDST TGEELLLSEG
60 70 80 90 100
SVGKNKSSAC RRKREFIPDE KKDAMYWEKR RKNNEAAKRS REKRRLNDLV
110 120 130 140 150
LENKLIALGE ENATLKAELL SLKLKFGLIS STAYAQEIQK LSNSTAVYFQ
160 170 180 190 200
DYQTSKSNVS SFVDEHEPSM VSSSCISVIK HSPQSSLSDV SEVSSVEHTQ
210 220 230 240 250
ESSVQGSCRS PENKFQIIKQ EPMELESYTR EPRDDRGSYT ASIYQNYMGN
260 270 280 290 300
SFSGYSHSPP LLQVNRSSSN SPRTSETDDG VVGKSSDGED EQQVPKGPIH
310 320 330 340 350
SPVELKHVHA TVVKVPEVNS SALPHKLRIK AKAMQIKVEA FDNEFEATQK
360 370 380 390 400
LSSPIDMTSK RHFELEKHSA PSMVHSSLTP FSVQVTNIQD WSLKSEHWHQ
410 420 430 440 450
KELSGKTQNS FKTGVVEMKD SGYKVSDPEN LYLKQGIANL SAEVVSLKRL
460
IATQPISASD SG
Length:462
Mass (Da):51,472
Last modified:June 26, 2007 - v2
Checksum:iD19946AAC774C3E7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 452EL → DV in AAA93067. (PubMed:1620116)Curated
Sequence conflicti44 – 452EL → DV in CAA45597. (PubMed:1620116)Curated
Sequence conflicti44 – 452EL → DV in AAB35410. (PubMed:7565758)Curated
Sequence conflicti149 – 1491F → S in CAG46846. 1 PublicationCurated
Sequence conflicti273 – 2731R → G in AAA93067. (PubMed:1620116)Curated
Sequence conflicti273 – 2731R → G in CAA45597. (PubMed:1620116)Curated
Sequence conflicti273 – 2731R → G in AAB35410. (PubMed:7565758)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U26173 mRNA. Translation: AAA93067.1.
X64318 mRNA. Translation: CAA45597.1.
S79880 mRNA. Translation: AAB35410.1.
EF028070 Genomic DNA. Translation: ABK15691.1.
CR542049 mRNA. Translation: CAG46846.1.
AK313970 mRNA. Translation: BAG36685.1.
AL353764 Genomic DNA. Translation: CAH73854.1.
CH471089 Genomic DNA. Translation: EAW62796.1.
BC008197 mRNA. Translation: AAH08197.1.
CCDSiCCDS6690.1.
PIRiG01804.
RefSeqiNP_001276928.1. NM_001289999.1.
NP_001276929.1. NM_001290000.1.
NP_005375.2. NM_005384.2.
UniGeneiHs.79334.

Genome annotation databases

EnsembliENST00000297689; ENSP00000297689; ENSG00000165030.
GeneIDi4783.
KEGGihsa:4783.
UCSCiuc004arh.3. human.

Polymorphism databases

DMDMi150385077.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U26173 mRNA. Translation: AAA93067.1 .
X64318 mRNA. Translation: CAA45597.1 .
S79880 mRNA. Translation: AAB35410.1 .
EF028070 Genomic DNA. Translation: ABK15691.1 .
CR542049 mRNA. Translation: CAG46846.1 .
AK313970 mRNA. Translation: BAG36685.1 .
AL353764 Genomic DNA. Translation: CAH73854.1 .
CH471089 Genomic DNA. Translation: EAW62796.1 .
BC008197 mRNA. Translation: AAH08197.1 .
CCDSi CCDS6690.1.
PIRi G01804.
RefSeqi NP_001276928.1. NM_001289999.1.
NP_001276929.1. NM_001290000.1.
NP_005375.2. NM_005384.2.
UniGenei Hs.79334.

3D structure databases

ProteinModelPortali Q16649.
SMRi Q16649. Positions 61-124.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110855. 9 interactions.
IntActi Q16649. 5 interactions.
MINTi MINT-268122.
STRINGi 9606.ENSP00000297689.

PTM databases

PhosphoSitei Q16649.

Polymorphism databases

DMDMi 150385077.

Proteomic databases

MaxQBi Q16649.
PaxDbi Q16649.
PRIDEi Q16649.

Protocols and materials databases

DNASUi 4783.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297689 ; ENSP00000297689 ; ENSG00000165030 .
GeneIDi 4783.
KEGGi hsa:4783.
UCSCi uc004arh.3. human.

Organism-specific databases

CTDi 4783.
GeneCardsi GC09M094171.
H-InvDB HIX0169355.
HGNCi HGNC:7787. NFIL3.
HPAi HPA003261.
MIMi 605327. gene.
neXtProti NX_Q16649.
PharmGKBi PA31593.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG260819.
GeneTreei ENSGT00530000064087.
HOGENOMi HOG000059596.
HOVERGENi HBG105717.
InParanoidi Q16649.
KOi K09059.
OMAi WHQKELN.
OrthoDBi EOG7GQXWM.
PhylomeDBi Q16649.
TreeFami TF328374.

Enzyme and pathway databases

SignaLinki Q16649.

Miscellaneous databases

ChiTaRSi NFIL3. human.
GeneWikii NFIL3.
GenomeRNAii 4783.
NextBioi 18446.
PROi Q16649.
SOURCEi Search...

Gene expression databases

Bgeei Q16649.
CleanExi HS_NFIL3.
Genevestigatori Q16649.

Family and domain databases

InterProi IPR004827. bZIP.
IPR016743. NFIL3/E4BP4.
IPR010533. Vert_IL3-reg_TF.
[Graphical view ]
PANTHERi PTHR15284:SF1. PTHR15284:SF1. 1 hit.
Pfami PF07716. bZIP_2. 1 hit.
PF06529. Vert_IL3-reg_TF. 1 hit.
[Graphical view ]
PIRSFi PIRSF019029. bZIP_E4BP4. 1 hit.
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
PROSITEi PS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Transcriptional repression by a novel member of the bZIP family of transcription factors."
    Cowell I.G., Skinner A., Hurst H.C.
    Mol. Cell. Biol. 12:3070-3077(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, DNA-BINDING.
    Tissue: Placenta.
  2. "Molecular cloning and characterization of NF-IL3A, a transcriptional activator of the human interleukin-3 promoter."
    Zhang W., Zhang J., Kornuc M., Kwan K., Frank R., Nimer S.D.
    Mol. Cell. Biol. 15:6055-6063(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, DNA-BINDING.
    Tissue: T-cell.
  3. NHLBI resequencing and genotyping service (RS&G)
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Tissue: Liver.
  6. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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].
    Tissue: Placenta.
  9. "Protein-protein interaction between the transcriptional repressor E4BP4 and the TBP-binding protein Dr1."
    Cowell I.G., Hurst H.C.
    Nucleic Acids Res. 24:3607-3613(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DR1, MUTAGENESIS OF LYS-330 AND LYS-332.
  10. "Exclusion of NFIL3 as the gene causing hereditary sensory neuropathy type I by mutation analysis."
    Hulme D.J., Blair I.P., Dawkins J.L., Nicholson G.A.
    Hum. Genet. 106:594-596(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiNFIL3_HUMAN
AccessioniPrimary (citable) accession number: Q16649
Secondary accession number(s): B2R9Y8
, Q14211, Q6FGQ8, Q96HS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: October 29, 2014
This is version 112 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3