Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BXC9 (BBS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bardet-Biedl syndrome 2 protein
Gene names
Name:BBS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. Ref.5 Ref.8

Subunit structure

Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5, BBS7, BBS8/TTC8, BBS9 and BBIP10. Interacts (via C-terminus) with BBS7. Interacts (via coiled coil domain) with MKKS. Interacts with CCDC28B and ALDOB. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cell projectioncilium membrane. Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite Ref.5 Ref.8.

Tissue specificity

Widely expressed.

Involvement in disease

Bardet-Biedl syndrome 2 (BBS2) [MIM:209900]: A syndrome characterized by usually severe pigmentary retinopathy, early-onset obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease. Bardet-Biedl syndrome inheritance is autosomal recessive, but three mutated alleles (two at one locus, and a third at a second locus) may be required for clinical manifestation of some forms of the disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
Protein transport
Sensory transduction
Transport
Vision
   Cellular componentCell membrane
Cell projection
Cilium
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityPolymorphism
   DiseaseBardet-Biedl syndrome
Ciliopathy
Disease mutation
Mental retardation
Obesity
   DomainCoiled coil
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to plasma membrane protein transport

Inferred from mutant phenotype PubMed 19150989. Source: MGI

adult behavior

Inferred from sequence or structural similarity. Source: BHF-UCL

artery smooth muscle contraction

Inferred from electronic annotation. Source: Ensembl

brain morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cartilage development

Inferred from electronic annotation. Source: Ensembl

cerebral cortex development

Inferred from sequence or structural similarity. Source: BHF-UCL

cilium morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

fat cell differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

hippocampus development

Inferred from sequence or structural similarity. Source: BHF-UCL

melanosome transport

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of appetite by leptin-mediated signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

negative regulation of multicellular organism growth

Inferred from sequence or structural similarity. Source: BHF-UCL

nonmotile primary cilium assembly

Inferred from electronic annotation. Source: InterPro

photoreceptor cell maintenance

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

protein localization

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to organelle

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of cilium beat frequency involved in ciliary motility

Inferred from sequence or structural similarity. Source: BHF-UCL

sperm axoneme assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

striatum development

Inferred from sequence or structural similarity. Source: BHF-UCL

vasodilation

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentBBSome

Inferred from direct assay Ref.5. Source: BHF-UCL

ciliary basal body

Inferred from direct assay PubMed 18299575. Source: BHF-UCL

ciliary membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

motile cilium

Inferred from direct assay PubMed 18299575. Source: BHF-UCL

   Molecular_functionRNA polymerase II repressing transcription factor binding

Inferred from physical interaction PubMed 22302990. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 721721Bardet-Biedl syndrome 2 protein
PRO_0000064843

Regions

Coiled coil325 – 36945 Potential

Natural variations

Natural variant231R → P in BBS2. Ref.13
VAR_038889
Natural variant701N → S in BBS2. Ref.9
Corresponds to variant rs4784677 [ dbSNP | Ensembl ].
VAR_013162
Natural variant751V → G in BBS2; in linkage disequilibrium with V-123 in a Bedouin kindred. Ref.1
VAR_013163
Natural variant811G → C in BBS2. Ref.16
VAR_066280
Natural variant1041D → A in BBS2. Ref.9 Ref.16
VAR_013164
Natural variant1221A → V. Ref.3
Corresponds to variant rs17856449 [ dbSNP | Ensembl ].
VAR_029747
Natural variant1231I → V Polymorphism in linkage disequilibrium with G-75 in a Bedouin kindred. Ref.1 Ref.13 Ref.14
Corresponds to variant rs11373 [ dbSNP | Ensembl ].
VAR_013165
Natural variant1251L → R in BBS2. Ref.16
VAR_066281
Natural variant1361A → P in BBS2. Ref.16
VAR_066282
Natural variant1741D → E in BBS2. Ref.11
VAR_038890
Natural variant3071C → W in BBS2. Ref.16
VAR_066283
Natural variant3151R → Q in BBS2. Ref.9 Ref.10
VAR_013166
Natural variant3151R → W in BBS2. Ref.9
VAR_013167
Natural variant3171Y → C in BBS2. Ref.16
VAR_066284
Natural variant3491L → W in BBS2; has a modifier effect on BBS. Ref.10
VAR_038891
Natural variant5041A → V.
Corresponds to variant rs16957538 [ dbSNP | Ensembl ].
VAR_029748
Natural variant5581T → I in BBS2. Ref.9
VAR_013168
Natural variant6291E → K in a patient with Bardet-Biedl syndrome compound heterozygote for mutations in BBS10; uncertain pathological role. Ref.15
VAR_066285
Natural variant6321R → P in BBS2. Ref.9 Ref.16
VAR_013169
Natural variant6431R → H in BBS2. Ref.12
VAR_038892

Experimental info

Sequence conflict631E → G in BAB55252. Ref.2
Sequence conflict1691C → R in BAB55252. Ref.2
Sequence conflict4571L → S in BAB55252. Ref.2
Sequence conflict6481Y → H in BAB55252. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9BXC9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8FA1CDAED725BEAF

FASTA72179,871
        10         20         30         40         50         60 
MLLPVFTLKL RHKISPRMVA IGRYDGTHPC LAAATQTGKV FIHNPHTRNQ HVSASRVFQS 

        70         80         90        100        110        120 
PLESDVSLLN INQAVSCLTA GVLNPELGYD ALLVGTQTNL LAYDVYNNSD LFYREVADGA 

       130        140        150        160        170        180 
NAIVLGTLGD ISSPLAIIGG NCALQGFNHE GSDLFWTVTG DNVNSLALCD FDGDGKKELL 

       190        200        210        220        230        240 
VGSEDFDIRV FKEDEIVAEM TETEIVTSLC PMYGSRFGYA LSNGTVGVYD KTSRYWRIKS 

       250        260        270        280        290        300 
KNHAMSIHAF DLNSDGVNEL ITGWSNGKVD ARSDRTGEVI FKDNFSSAIA GVVEGDYRMD 

       310        320        330        340        350        360 
GHIQLICCSV DGEIRGYLPG TAEMRGNLMD TSAEQDLIRE LSQKKQNLLL ELRNYEENAK 

       370        380        390        400        410        420 
AELASPLNEA DGHRGIIPAN TRLHTTLSVS LGNETQTAHT ELRISTSNDT IIRAVLIFAE 

       430        440        450        460        470        480 
GIFTGESHVV HPSIHNLSSS ICIPIVPPKD VPVDLHLKAF VGYRSSTQFH VFESTRQLPR 

       490        500        510        520        530        540 
FSMYALTSLD PASEPISYVN FTIAERAQRV VVWLGQNFLL PEDTHIQNAP FQVCFTSLRN 

       550        560        570        580        590        600 
GGHLHIKIKL SGEITINTDD IDLAGDIIQS MASFFAIEDL QVEADFPVYF EELRKVLVKV 

       610        620        630        640        650        660 
DEYHSVHQKL SADMADHSNL IRSLLVGAED ARLMRDMKTM KSRYMELYDL NRDLLNGYKI 

       670        680        690        700        710        720 
RCNNHTELLG NLKAVNQAIQ RAGRLRVGKP KNQVITACRD AIRSNNINTL FKIMRVGTAS 


S 

« Hide

References

« Hide 'large scale' references
[1]"Positional cloning of a novel gene on chromosome 16q causing Bardet-Biedl syndrome (BBS2)."
Nishimura D.Y., Searby C.C., Carmi R., Elbedour K., Van Maldergem L., Fulton A.B., Lam B.L., Powell B.R., Swiderski R.E., Bugge K.E., Haider N.B., Kwitek-Black A.E., Ying L., Duhl D.M., Gorman S.M., Heon E., Iannaccone A., Bonneau D. expand/collapse author list , Biesecker L.G., Jacobson S.G., Stone E.M., Sheffield V.C.
Hum. Mol. Genet. 10:865-874(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT BBS2 GLY-75, VARIANT VAL-123.
[2]"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].
[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], VARIANT VAL-122.
Tissue: Placenta.
[4]"Dissection of epistasis in oligogenic Bardet-Biedl syndrome."
Badano J.L., Leitch C.C., Ansley S.J., May-Simera H., Lawson S., Lewis R.A., Beales P.L., Dietz H.C., Fisher S., Katsanis N.
Nature 439:326-330(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CCDC28B.
[5]"A core complex of BBS proteins cooperates with the GTPase Rab8 to promote ciliary membrane biogenesis."
Nachury M.V., Loktev A.V., Zhang Q., Westlake C.J., Peraenen J., Merdes A., Slusarski D.C., Scheller R.H., Bazan J.F., Sheffield V.C., Jackson P.K.
Cell 129:1201-1213(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, FUNCTION, SUBCELLULAR LOCATION.
[6]"Novel interaction partners of Bardet-Biedl syndrome proteins."
Oeffner F., Moch C., Neundorf A., Hofmann J., Koch M., Grzeschik K.H.
Cell Motil. Cytoskeleton 65:143-155(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ALDOB.
[7]"BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly."
Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., Sheffield V.C.
Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BBS7 AND MKKS.
[8]"A novel protein LZTFL1 regulates ciliary trafficking of the BBSome and Smoothened."
Seo S., Zhang Q., Bugge K., Breslow D.K., Searby C.C., Nachury M.V., Sheffield V.C.
PLoS Genet. 7:E1002358-E1002358(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, FUNCTION OF THE BBSOME COMPLEX, IDENTIFICATION IN THE BBSOME COMPLEX, SUBCELLULAR LOCATION.
[9]"Triallelic inheritance in Bardet-Biedl syndrome, a Mendelian recessive disorder."
Katsanis N., Ansley S.J., Badano J.L., Eichers E.R., Lewis R.A., Hoskins B.E., Scambler P.J., Davidson W.S., Beales P.L., Lupski J.R.
Science 293:2256-2259(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BBS2 SER-70; ALA-104; GLN-315; TRP-315; ILE-558 AND PRO-632.
[10]"Genetic interaction of BBS1 mutations with alleles at other BBS loci can result in non-Mendelian Bardet-Biedl syndrome."
Beales P.L., Badano J.L., Ross A.J., Ansley S.J., Hoskins B.E., Kirsten B., Mein C.A., Froguel P., Scambler P.J., Lewis R.A., Lupski J.R., Katsanis N.
Am. J. Hum. Genet. 72:1187-1199(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BBS2 GLN-315 AND TRP-349.
[11]"Evaluation of multiplex capillary heteroduplex analysis: a rapid and sensitive mutation screening technique."
Hoskins B.E., Thorn A., Scambler P.J., Beales P.L.
Hum. Mutat. 22:151-157(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BBS2 GLU-174.
[12]"Further support for digenic inheritance in Bardet-Biedl syndrome."
Fauser S., Munz M., Besch D.
J. Med. Genet. 40:E104-E104(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BBS2 HIS-643.
[13]"Antenatal presentation of Bardet-Biedl syndrome may mimic Meckel syndrome."
Karmous-Benailly H., Martinovic J., Gubler M.-C., Sirot Y., Clech L., Ozilou C., Auge J., Brahimi N., Etchevers H., Detrait E., Esculpavit C., Audollent S., Goudefroye G., Gonzales M., Tantau J., Loget P., Joubert M., Gaillard D. expand/collapse author list , Jeanne-Pasquier C., Delezoide A.-L., Peter M.-O., Plessis G., Simon-Bouy B., Dollfus H., Le Merrer M., Munnich A., Encha-Razavi F., Vekemans M., Attie-Bitach T.
Am. J. Hum. Genet. 76:493-504(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BBS2 PRO-23, VARIANT VAL-123.
[14]"Testing for triallelism: analysis of six BBS genes in a Bardet-Biedl syndrome family cohort."
Hichri H., Stoetzel C., Laurier V., Caron S., Sigaudy S., Sarda P., Hamel C., Martin-Coignard D., Gilles M., Leheup B., Holder M., Kaplan J., Bitoun P., Lacombe D., Verloes A., Bonneau D., Perrin-Schmitt F., Brandt C. expand/collapse author list , Besancon A.-F., Mandel J.-L., Cossee M., Dollfus H.
Eur. J. Hum. Genet. 13:607-616(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-123.
[15]"Bardet-Biedl syndrome in Denmark -- report of 13 novel sequence variations in six genes."
Hjortshoj T.D., Gronskov K., Philp A.R., Nishimura D.Y., Riise R., Sheffield V.C., Rosenberg T., Brondum-Nielsen K.
Hum. Mutat. 31:429-436(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LYS-629.
[16]"BBS genotype-phenotype assessment of a multiethnic patient cohort calls for a revision of the disease definition."
Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R., Vincent A., Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I., Fishman G.A., Chitayat D., Knueppel T., Millan J.M., Munier F.L., Kennedy D., Jacobson S.G., Innes A.M. expand/collapse author list , Mitchell G.A., Boycott K., Heon E.
Hum. Mutat. 32:610-619(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BBS2 CYS-81; ALA-104; ARG-125; PRO-136; TRP-307; CYS-317 AND PRO-632.
+Additional computationally mapped references.

Web resources

Mutations of the BBS2 gene

Retina International's Scientific Newsletter

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF342736 mRNA. Translation: AAK28552.1.
AK027635 mRNA. Translation: BAB55252.1.
BC014140 mRNA. Translation: AAH14140.1.
RefSeqNP_114091.3. NM_031885.3.
UniGeneHs.333738.

3D structure databases

ProteinModelPortalQ9BXC9.
SMRQ9BXC9. Positions 74-110, 160-230, 246-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107059. 13 interactions.
DIPDIP-46563N.
IntActQ9BXC9. 29 interactions.
MINTMINT-1454659.
STRING9606.ENSP00000245157.

PTM databases

PhosphoSiteQ9BXC9.

Polymorphism databases

DMDM20454827.

Proteomic databases

PaxDbQ9BXC9.
PRIDEQ9BXC9.

Protocols and materials databases

DNASU583.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245157; ENSP00000245157; ENSG00000125124.
GeneID583.
KEGGhsa:583.
UCSCuc002ejd.2. human.

Organism-specific databases

CTD583.
GeneCardsGC16M056569.
HGNCHGNC:967. BBS2.
HPAHPA041315.
MIM209900. phenotype.
606151. gene.
neXtProtNX_Q9BXC9.
Orphanet110. Bardet-Biedl syndrome.
PharmGKBPA25276.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87621.
HOGENOMHOG000007549.
HOVERGENHBG031114.
InParanoidQ9BXC9.
KOK16747.
PhylomeDBQ9BXC9.
TreeFamTF313236.

Gene expression databases

ArrayExpressQ9BXC9.
BgeeQ9BXC9.
CleanExHS_BBS2.
GenevestigatorQ9BXC9.

Family and domain databases

Gene3D2.130.10.10. 2 hits.
InterProIPR016616. Bardet-Biedl_syndrome_2_prot.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERPTHR32465:SF0. PTHR32465:SF0. 1 hit.
PIRSFPIRSF013684. BBS2. 1 hit.
SUPFAMSSF50978. SSF50978. 2 hits.
ProtoNetSearch...

Other

GeneWikiBBS2.
GenomeRNAi583.
NextBio2387.
PROQ9BXC9.
SOURCESearch...

Entry information

Entry nameBBS2_HUMAN
AccessionPrimary (citable) accession number: Q9BXC9
Secondary accession number(s): Q96CM0, Q96SN9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 112 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM