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Q9UKB1 (FBW1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
F-box/WD repeat-containing protein 11
Alternative name(s):
F-box and WD repeats protein beta-TrCP2
F-box/WD repeat-containing protein 1B
Homologous to Slimb protein
Short name=HOS
Gene names
Name:FBXW11
Synonyms:BTRCP2, FBW1B, FBXW1B, KIAA0696
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins. SCF(FBXW11) mediates the ubiquitination of CTNNB1 and participates in Wnt signaling. SCF(FBXW11) mediates the ubiquitination of phosphorylated NFKBIA, which degradation frees the associated NFKB1 to translocate into the nucleus and to activate transcription. SCF(FBXW11) mediates the ubiquitination of IFNAR1. Targets phosphorylation-dependent degradation of beta-catenin. Involved in the oxidative stress-induced a ubiquitin-mediated decrease in RCAN1. Mediates the degradation of CDC25A induced by ionizing radiation in cells progressing through S phase and thus may function in the intra-S-phase checkpoint. Has an essential role in the control of the clock-dependent transcription via degradation of PER1 and phosphorylated PER2. Is target of human immunodeficiency virus type 1 (HIV-1) protein VPU to polyubiquitinate and deplete BST2 from cells and antagonize its antiviral action. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Subunit structure

Self-associates. Component of the SCF(FBXW11) complex formed of CUL1, SKP1, RBX1 and a FBXW11 dimer. Interacts with BTRC, BST2, PER1, RCAN1 and USP47. Interacts with phosphorylated ubiquitination substrate PER2 By similarity. Interacts with phosphorylated ubiquitination substrates CTNNB1, NFKBIA, IFNAR1; the interaction requires the phosphorylation of the two serine residues in the substrates' destruction motif D-S-G-X(2,3,4)-S. Interacts with TRIM21. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Induction

Expression is negatively regulated by Wnt/beta-catenin pathway. Ref.13

Domain

The N-terminal D domain mediates homodimerization By similarity.

Sequence similarities

Contains 1 F-box domain.

Contains 7 WD repeats.

Sequence caution

The sequence BAA31671.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processBiological rhythms
Cell cycle
Ubl conjugation pathway
Wnt signaling pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

SCF-dependent proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.18. Source: UniProtKB

Wnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of NF-kappaB import into nucleus

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.19. Source: UniProtKB

positive regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of proteolysis

Inferred from mutant phenotype PubMed 16885022. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.18. Source: UniProtKB

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

protein destabilization

Inferred from mutant phenotype PubMed 16885022. Source: UniProtKB

protein polyubiquitination

Inferred from direct assay Ref.18. Source: UniProtKB

protein ubiquitination

Inferred from direct assay PubMed 16885022. Source: UniProtKB

rhythmic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSCF ubiquitin ligase complex

Inferred from direct assay Ref.11Ref.18. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

ubiquitin ligase complex

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionubiquitin-protein ligase activity

Inferred from direct assay Ref.18. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform C (identifier: Q9UKB1-1)

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 A (identifier: Q9UKB1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     16-49: Missing.
Isoform B (identifier: Q9UKB1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     16-48: CSVPRSLWLGCANLVESMCALSCLQSMPSVRCL → NTSVMEDQNEDESPKKNTLW

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542F-box/WD repeat-containing protein 11
PRO_0000050981

Regions

Domain129 – 16739F-box
Repeat238 – 27538WD 1
Repeat278 – 31538WD 2
Repeat318 – 35538WD 3
Repeat361 – 39838WD 4
Repeat401 – 44040WD 5
Repeat442 – 47837WD 6
Repeat490 – 52738WD 7
Region67 – 11650Homodimerization domain D By similarity

Natural variations

Alternative sequence16 – 4934Missing in isoform A.
VSP_006765
Alternative sequence16 – 4833CSVPR…SVRCL → NTSVMEDQNEDESPKKNTLW in isoform B.
VSP_006766

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 7CD40087EFAA5C8A

FASTA54262,091
        10         20         30         40         50         60 
MEPDSVIEDK TIELMCSVPR SLWLGCANLV ESMCALSCLQ SMPSVRCLQI SNGTSSVIVS 

        70         80         90        100        110        120 
RKRPSEGNYQ KEKDLCIKYF DQWSESDQVE FVEHLISRMC HYQHGHINSY LKPMLQRDFI 

       130        140        150        160        170        180 
TALPEQGLDH IAENILSYLD ARSLCAAELV CKEWQRVISE GMLWKKLIER MVRTDPLWKG 

       190        200        210        220        230        240 
LSERRGWDQY LFKNRPTDGP PNSFYRSLYP KIIQDIETIE SNWRCGRHNL QRIQCRSENS 

       250        260        270        280        290        300 
KGVYCLQYDD EKIISGLRDN SIKIWDKTSL ECLKVLTGHT GSVLCLQYDE RVIVTGSSDS 

       310        320        330        340        350        360 
TVRVWDVNTG EVLNTLIHHN EAVLHLRFSN GLMVTCSKDR SIAVWDMASA TDITLRRVLV 

       370        380        390        400        410        420 
GHRAAVNVVD FDDKYIVSAS GDRTIKVWST STCEFVRTLN GHKRGIACLQ YRDRLVVSGS 

       430        440        450        460        470        480 
SDNTIRLWDI ECGACLRVLE GHEELVRCIR FDNKRIVSGA YDGKIKVWDL QAALDPRAPA 

       490        500        510        520        530        540 
STLCLRTLVE HSGRVFRLQF DEFQIISSSH DDTILIWDFL NVPPSAQNET RSPSRTYTYI 


SR 

« Hide

Isoform A [UniParc].

Checksum: 05C691DB32A91B50
Show »

FASTA50858,422
Isoform B [UniParc].

Checksum: 53D181B789313D0E
Show »

FASTA52960,898

References

« Hide 'large scale' references
[1]"Identification of a family of human F-box proteins."
Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M., Pagano M.
Curr. Biol. 9:1177-1179(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning and genomic structure of the betaTRCP2 gene on chromosome 5q35.1."
Koike J., Sagara N., Kirikoshi H., Takagi A., Miwa T., Hirai M., Katoh M.
Biochem. Biophys. Res. Commun. 269:103-109(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
Tissue: Fetal lung.
[3]"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[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 A).
Tissue: Hippocampus.
[5]"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 B).
Tissue: Lymph.
[6]"IkappaBalpha ubiquitination is catalyzed by an SCF-like complex containing Skp1, cullin-1, and two F-box/WD40-repeat proteins, betaTrCP1 and betaTrCP2."
Suzuki H., Chiba T., Kobayashi M., Takeuchi M., Suzuki T., Ichiyama A., Ikenoue T., Omata M., Furuichi K., Tanaka K.
Biochem. Biophys. Res. Commun. 256:127-132(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SCF(FBXW11) COMPLEX.
[7]"HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1 and targets the phosphorylation-dependent degradation of IkappaB and beta-catenin."
Fuchs S.Y., Chen A., Xiong Y., Pan Z.Q., Ronai Z.
Oncogene 18:2039-2046(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFKBIA AND CTNNB1, FUNCTION IN UBIQUITINATION OF NFKBIA AND CTNNB1.
[8]"Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination."
Suzuki H., Chiba T., Suzuki T., Fujita T., Ikenoue T., Omata M., Furuichi K., Shikama H., Tanaka K.
J. Biol. Chem. 275:2877-2884(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SELF-ASSOCIATION, INTERACTION WITH BTRC AND NFKBIA, FUNCTION IN UBIQUITINATION OF NFKBIA.
[9]"SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of the interferon-alpha receptor."
Kumar K.G., Tang W., Ravindranath A.K., Clark W.A., Croze E., Fuchs S.Y.
EMBO J. 22:5480-5490(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PHOSPHORYLATED IFNAR1, FUNCTION IN IFNAR1 UBIQUITINATION.
[10]"A complex containing betaTrCP recruits Cdc34 to catalyse ubiquitination of IkappaBalpha."
Vuillard L., Nicholson J., Hay R.T.
FEBS Lett. 455:311-314(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SCF(FBXW11) COMPLEX, INTERACTION WITH NFKBIA, FUNCTION IN UBIQUITINATION OF NFKBIA.
[11]"Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein."
Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M., Krek W.
Mol. Cell. Biol. 26:5994-6004(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM21.
[12]"The SCF(HOS/beta-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct domains within CUL1 for substrate targeting and ubiquitin ligation."
Wu K., Fuchs S.Y., Chen A., Tan P., Gomez C., Ronai Z., Pan Z.Q.
Mol. Cell. Biol. 20:1382-1393(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE SCF(FBXW11) COMPLEX.
[13]"Inhibition of HOS expression and activities by Wnt pathway."
Spiegelman V.S., Tang W., Katoh M., Slaga T.J., Fuchs S.Y.
Oncogene 21:856-860(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[14]"Degradation of Cdc25A by beta-TrCP during S phase and in response to DNA damage."
Busino L., Donzelli M., Chiesa M., Guardavaccaro D., Ganoth D., Dorrello N.V., Hershko A., Pagano M., Draetta G.F.
Nature 426:87-91(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDC25A.
[15]"SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein."
Shirogane T., Jin J., Ang X.L., Harper J.W.
J. Biol. Chem. 280:26863-26872(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PER1.
[16]"Oxidative stress-induced ubiquitination of RCAN1 mediated by SCFbeta-TrCP ubiquitin ligase."
Asada S., Ikeda A., Nagao R., Hama H., Sudo T., Fukamizu A., Kasuya Y., Kishi T.
Int. J. Mol. Med. 22:95-104(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RCAN1.
[17]"HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation."
Mangeat B., Gers-Huber G., Lehmann M., Zufferey M., Luban J., Piguet V.
PLoS Pathog. 5:E1000574-E1000574(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH BST2.
[18]"Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for polyubiquitination on a SCF substrate."
Wu K., Kovacev J., Pan Z.Q.
Mol. Cell 37:784-796(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE SCF(FBXW11) COMPLEX, INTERACTION WITH NFKBIA.
[19]"The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor regulating cell survival."
Peschiaroli A., Skaar J.R., Pagano M., Melino G.
Oncogene 29:1384-1393(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH USP47.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF176022 mRNA. Translation: AAF04528.1.
AB033279 mRNA. Translation: BAA92329.1.
AB033280 mRNA. Translation: BAA92330.1.
AB033281 mRNA. Translation: BAA92331.1.
AB014596 mRNA. Translation: BAA31671.1. Different initiation.
AK314999 mRNA. Translation: BAG37495.1.
BC026213 mRNA. Translation: AAH26213.1.
RefSeqNP_036432.2. NM_012300.2.
NP_387448.2. NM_033644.2.
NP_387449.2. NM_033645.2.
UniGeneHs.484138.

3D structure databases

ProteinModelPortalQ9UKB1.
SMRQ9UKB1. Positions 67-518.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116887. 66 interactions.
DIPDIP-27593N.
IntActQ9UKB1. 38 interactions.
MINTMINT-120522.
STRING9606.ENSP00000265094.

PTM databases

PhosphoSiteQ9UKB1.

Polymorphism databases

DMDM13124267.

Proteomic databases

PaxDbQ9UKB1.
PRIDEQ9UKB1.

Protocols and materials databases

DNASU23291.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265094; ENSP00000265094; ENSG00000072803. [Q9UKB1-1]
ENST00000296933; ENSP00000296933; ENSG00000072803. [Q9UKB1-3]
ENST00000393802; ENSP00000377391; ENSG00000072803. [Q9UKB1-2]
GeneID23291.
KEGGhsa:23291.
UCSCuc003mbl.1. human. [Q9UKB1-3]
uc003mbm.1. human. [Q9UKB1-1]
uc003mbn.1. human. [Q9UKB1-2]

Organism-specific databases

CTD23291.
GeneCardsGC05M171288.
HGNCHGNC:13607. FBXW11.
MIM605651. gene.
neXtProtNX_Q9UKB1.
PharmGKBPA28050.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOGENOMHOG000006638.
HOVERGENHBG002521.
InParanoidQ9UKB1.
KOK03362.
OMAFDQWSEA.
OrthoDBEOG76DTS5.
PhylomeDBQ9UKB1.
TreeFamTF105679.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_6900. Immune System.
SignaLinkQ9UKB1.

Gene expression databases

ArrayExpressQ9UKB1.
BgeeQ9UKB1.
CleanExHS_FBXW11.
GenevestigatorQ9UKB1.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR021977. Beta-TrCP_D.
IPR001810. F-box_dom.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF12125. Beta-TrCP_D. 1 hit.
PF00400. WD40. 7 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM01028. Beta-TrCP_D. 1 hit.
SM00256. FBOX. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
SSF81383. SSF81383. 1 hit.
PROSITEPS50181. FBOX. 1 hit.
PS00678. WD_REPEATS_1. 5 hits.
PS50082. WD_REPEATS_2. 7 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiFBXW11.
GenomeRNAi23291.
NextBio45108.
PROQ9UKB1.
SOURCESearch...

Entry information

Entry nameFBW1B_HUMAN
AccessionPrimary (citable) accession number: Q9UKB1
Secondary accession number(s): B2RC98 expand/collapse secondary AC list , Q9P2S8, Q9P2S9, Q9Y4C6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 142 of the entry and version 1 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 5

Human chromosome 5: entries, gene names and cross-references to MIM