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O00712 (NFIB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear factor 1 B-type

Short name=NF1-B
Short name=Nuclear factor 1/B
Alternative name(s):
CCAAT-box-binding transcription factor
Short name=CTF
Nuclear factor I/B
Short name=NF-I/B
Short name=NFI-B
TGGCA-binding protein
Gene names
Name:NFIB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.

Subunit structure

Binds DNA as a homodimer.

Subcellular location

Nucleus.

Sequence similarities

Belongs to the CTF/NF-I family.

Contains 1 CTF/NF-I DNA-binding domain.

Ontologies

Keywords
   Biological processDNA replication
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processClara cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

Type I pneumocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

Type II pneumocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

anterior commissure morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

chondrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

commissural neuron axon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

glial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

hindbrain development

Inferred from electronic annotation. Source: Ensembl

lung ciliated cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of DNA binding

Inferred from direct assay Ref.2. Source: UniProtKB

negative regulation of epithelial cell proliferation involved in lung morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of mesenchymal cell proliferation involved in lung development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19540848Ref.2. Source: UniProtKB

principal sensory nucleus of trigeminal nerve development

Inferred from sequence or structural similarity. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19540848Ref.2. Source: GOC

   Cellular_componentcerebellar mossy fiber

Inferred from sequence or structural similarity. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 19540848Ref.2. Source: UniProtKB

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II transcription corepressor activity

Inferred from direct assay Ref.2. Source: UniProtKB

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 19540848Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: O00712-1)

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: O00712-3)

The sequence of this isoform is not available.
Isoform 3 (identifier: O00712-2)

Also known as: NFI-B3;

The sequence of this isoform differs from the canonical sequence as follows:
     187-188: QD → AR
     189-420: Missing.
Isoform 4 (identifier: O00712-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MMYSPICLTQ → MERIPVSVDFWVVCCAVLKCNPGIPMERIPVSVDFWVVCCAVLKCNPGIPKRMSTLCFGFS
Note: No experimental confirmation available.
Isoform 5 (identifier: O00712-5)

The sequence of this isoform differs from the canonical sequence as follows:
     416-416: S → PNGSGQVVGK...DPSFLHQQQS
Note: No experimental confirmation available.
Isoform 6 (identifier: O00712-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-252: Missing.
     416-420: SWYLG → PNGSGQVVGK...EPFLQAETSN
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Nuclear factor 1 B-type
PRO_0000100195

Regions

DNA binding1 – 195195CTF/NF-I

Amino acid modifications

Modified residue2641Phosphoserine Ref.10
Modified residue2921Phosphoserine By similarity
Modified residue2951Phosphoserine By similarity
Modified residue3121Phosphoserine Ref.11
Modified residue3281Phosphoserine Ref.10 Ref.11
Modified residue3331Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 252252Missing in isoform 6.
VSP_054713
Alternative sequence1 – 1010MMYSPICLTQ → MERIPVSVDFWVVCCAVLKC NPGIPMERIPVSVDFWVVCC AVLKCNPGIPKRMSTLCFGF S in isoform 4.
VSP_044462
Alternative sequence187 – 1882QD → AR in isoform 3.
VSP_003545
Alternative sequence189 – 420232Missing in isoform 3.
VSP_003546
Alternative sequence416 – 4205SWYLG → PNGSGQVVGKVPGHFTPVLA PSPHPSAVRPVTLSMTDTKP ITTSTEAYTASGTSQANRYV GLSPRDPSFLHQQQLRICDW TMNQNGRHLYPSTSEDTLGI TWQSPGTWASLVPFQVSNRT PILPANVQNYGLNIIGEPFL QAETSN in isoform 6.
VSP_054714
Alternative sequence4161S → PNGSGQVVGKVPGHFTPVLA PSPHPSAVRPVTLSMTDTKP ITTSTEAYTASGTSQANRYV GLSPRDPSFLHQQQS in isoform 5.
VSP_045065

Experimental info

Sequence conflict171I → M in AAB41899. Ref.1
Sequence conflict371R → G in BAD18416. Ref.4
Sequence conflict741S → F in BX648845. Ref.5
Sequence conflict1981N → S in BAD18416. Ref.4
Sequence conflict2841S → R in BX648845. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 15, 2004. Version 2.
Checksum: 0F71635FE9D64FA4

FASTA42047,442
        10         20         30         40         50         60 
MMYSPICLTQ DEFHPFIEAL LPHVRAIAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE 

        70         80         90        100        110        120 
LLSEKPEIKQ KWASRLLAKL RKDIRQEYRE DFVLTVTGKK HPCCVLSNPD QKGKIRRIDC 

       130        140        150        160        170        180 
LRQADKVWRL DLVMVILFKG IPLESTDGER LMKSPHCTNP ALCVQPHHIT VSVKELDLFL 

       190        200        210        220        230        240 
AYYVQEQDSG QSGSPSHNDP AKNPPGYLED SFVKSGVFNV SELVRVSRTP ITQGTGVNFP 

       250        260        270        280        290        300 
IGEIPSQPYY HDMNSGVNLQ RSLSSPPSSK RPKTISIDEN MEPSPTGDFY PSPSSPAAGS 

       310        320        330        340        350        360 
RTWHERDQDM SSPTTMKKPE KPLFSSASPQ DSSPRLSTFP QHHHPGIPGV AHSVISTRTP 

       370        380        390        400        410        420 
PPPSPLPFPT QAILPPAPSS YFSHPTIRYP PHLNPQDTLK NYVPSYDPSS PQTSQSWYLG 

« Hide

Isoform 2 (Sequence not available).
Isoform 3 (NFI-B3) [UniParc].

Checksum: C718698597C13336
Show »

FASTA18822,251
Isoform 4 [UniParc].

Checksum: D2797FFB1527C066
Show »

FASTA47153,049
Isoform 5 [UniParc].

Checksum: 55BE3377EEEA2C07
Show »

FASTA49455,181
Isoform 6 [UniParc].

Checksum: 8DA70FF7F8A8CEEF
Show »

FASTA30933,525

References

« Hide 'large scale' references
[1]"Identification of NFIB as recurrent translocation partner gene of HMGIC in pleomorphic adenomas."
Geurts J.M.W., Schoenmakers E.F.P.M., Roijer E., Astroem A.-K., Stenman G., van de Ven W.J.M.
Oncogene 16:865-872(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"NFI-B3, a novel transcriptional repressor of the nuclear factor I family, is generated by alternative RNA processing."
Liu Y., Bernard H.U., Apt D.
J. Biol. Chem. 272:10739-10745(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Foreskin.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[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. expand/collapse author list , 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 4).
Tissue: Amygdala.
[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] (ISOFORMS 5 AND 6).
Tissue: Colon epithelium.
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , 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 (JUL-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: Cervix.
[9]"Chromosomal localization of the four genes (NFIA, B, C, and X) for the human transcription factor nuclear factor I by FISH."
Qian F., Kruse U., Lichter P., Sippel A.E.
Genomics 28:66-73(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-283.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-312; SER-328 AND SER-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85193 mRNA. Translation: AAB41899.1.
U70862 mRNA. Translation: AAB51197.1.
BT007266 mRNA. Translation: AAP35930.1.
AK131233 mRNA. Translation: BAD18416.1.
BX648416 mRNA. Translation: CAH56156.1.
BX648845 mRNA. No translation available.
AL441963, AL136366 Genomic DNA. Translation: CAH71971.1.
AL136366, AL441963 Genomic DNA. Translation: CAH73585.1.
AL137017 Genomic DNA. No translation available.
AL449443 Genomic DNA. No translation available.
CH471071 Genomic DNA. Translation: EAW58697.1.
CH471071 Genomic DNA. Translation: EAW58699.1.
BC001283 mRNA. Translation: AAH01283.1.
U07810 mRNA. Translation: AAA93125.1.
CCDSCCDS55291.1. [O00712-5]
CCDS6474.1. [O00712-1]
RefSeqNP_001177666.1. NM_001190737.1. [O00712-5]
NP_001177667.1. NM_001190738.1.
NP_001269716.1. NM_001282787.1. [O00712-6]
NP_005587.2. NM_005596.3. [O00712-1]
UniGeneHs.644095.

3D structure databases

ProteinModelPortalO00712.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110853. 9 interactions.
STRING9606.ENSP00000370346.

PTM databases

PhosphoSiteO00712.

Proteomic databases

MaxQBO00712.
PaxDbO00712.
PRIDEO00712.

Protocols and materials databases

DNASU4781.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380953; ENSP00000370340; ENSG00000147862. [O00712-5]
ENST00000380959; ENSP00000370346; ENSG00000147862. [O00712-1]
ENST00000543693; ENSP00000442888; ENSG00000147862.
GeneID4781.
KEGGhsa:4781.
UCSCuc003zle.3. human. [O00712-1]
uc003zlf.3. human.
uc022bdp.1. human. [O00712-4]

Organism-specific databases

CTD4781.
GeneCardsGC09M014077.
HGNCHGNC:7785. NFIB.
HPAHPA003956.
MIM600728. gene.
neXtProtNX_O00712.
PharmGKBPA31591.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG252172.
HOVERGENHBG006561.
KOK09169.
PhylomeDBO00712.
TreeFamTF313889.

Enzyme and pathway databases

SignaLinkO00712.

Gene expression databases

ArrayExpressO00712.
BgeeO00712.
CleanExHS_NFIB.
GenevestigatorO00712.

Family and domain databases

InterProIPR000647. CTF/NFI.
IPR020604. CTF/NFI_DNA-bd-dom.
IPR019739. CTF/NFI_DNA-bd_CS.
IPR019548. CTF/NFI_DNA-bd_N.
IPR003619. MAD_homology1_Dwarfin-type.
[Graphical view]
PANTHERPTHR11492. PTHR11492. 1 hit.
PfamPF00859. CTF_NFI. 1 hit.
PF03165. MH1. 1 hit.
PF10524. NfI_DNAbd_pre-N. 1 hit.
[Graphical view]
SMARTSM00523. DWA. 1 hit.
[Graphical view]
PROSITEPS00349. CTF_NFI_1. 1 hit.
PS51080. CTF_NFI_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNFIB. human.
GeneWikiNFIB_(gene).
GenomeRNAi4781.
NextBio18436.
PROO00712.
SOURCESearch...

Entry information

Entry nameNFIB_HUMAN
AccessionPrimary (citable) accession number: O00712
Secondary accession number(s): G3V1P1 expand/collapse secondary AC list , H7BYE8, O00166, Q12858, Q5VW29, Q63HM5, Q6ZNF9, Q96J45
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: March 15, 2004
Last modified: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM