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Protein

Tubulin beta-2B chain

Gene

TUBB2B

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

Functioni

Tubulin is the major constituent of microtubules (PubMed:23001566, PubMed:28013290, PubMed:26732629). It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain (By similarity). Plays a critical role in proper axon guidance in both central and peripheral axon tracts (PubMed:23001566). Implicated in neuronal migration (PubMed:19465910).By similarity4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi140 – 146GTPSequence analysis7

GO - Molecular functioni

  • GTPase activity Source: InterPro
  • GTP binding Source: GO_Central
  • protein heterodimerization activity Source: UniProtKB
  • structural constituent of cytoskeleton Source: GO_Central

GO - Biological processi

Keywordsi

Biological processNeurogenesis
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-HSA-190861 Gap junction assembly
R-HSA-2132295 MHC class II antigen presentation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977 Post-chaperonin tubulin folding pathway
R-HSA-437239 Recycling pathway of L1
R-HSA-5610787 Hedgehog 'off' state
R-HSA-5617833 Cilium Assembly
R-HSA-5620924 Intraflagellar transport
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6807878 COPI-mediated anterograde transport
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877 Mitotic Prometaphase
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8955332 Carboxyterminal post-translational modifications of tubulin
R-HSA-983189 Kinesins

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-2B chain
Gene namesi
Name:TUBB2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000137285.9
HGNCiHGNC:30829 TUBB2B
MIMi612850 gene
neXtProtiNX_Q9BVA1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Cortical dysplasia, complex, with other brain malformations 7 (CDCBM7)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA malformation of the cortex in which the brain surface is irregular and characterized by an excessive number of small gyri with abnormal lamination. Polymicrogyria is a heterogeneous disorder, considered to be the result of postmigratory abnormal cortical organization.
See also OMIM:610031
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078186117L → P in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514569EnsemblClinVar.1
Natural variantiVAR_063389172S → P in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant dbSNP:rs137853194EnsemblClinVar.1
Natural variantiVAR_063391210I → T in CDCBM7. 1 Publication1
Natural variantiVAR_063392228L → P in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs137853195EnsemblClinVar.1
Natural variantiVAR_078188256N → S in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514568EnsemblClinVar.1
Natural variantiVAR_063393265F → L in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant dbSNP:rs137853196EnsemblClinVar.1
Natural variantiVAR_063394312T → M in CDCBM7. 1 Publication1
Natural variantiVAR_078190417D → N in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514567EnsemblClinVar.1
Natural variantiVAR_078191421E → K in CDCBM7; decreased protein expression; decreased tubulin heterodimer formation; no effect on integration into the microtubule lattice; no effect on microtubule cytoskeleton subcellular location; loss of axon guidance. 1 PublicationCorresponds to variant dbSNP:rs398122369EnsemblClinVar.1
Fetal akinesia deformation sequence (FADS)1 Publication
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionA clinically and genetically heterogeneous group of disorders with congenital malformations related to impaired fetal movement. Clinical features include fetal akinesia, intrauterine growth retardation, polyhydramnios, arthrogryposis, pulmonary hypoplasia, craniofacial abnormalities, and cryptorchidism.
See also OMIM:208150
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078187239C → F in FADS; decreased tubulin heterodimer formation; decreased ability to incorporate into the cytoskeleton; no effect on microtubules disintegration; increased ability to repolymerize. 1 PublicationCorresponds to variant dbSNP:rs878853284EnsemblClinVar.1
Defects in TUBB2B may be involved in cerebellar ataxia, mental retardation, and dysequilibrium syndrome (CAMRQ).1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi347733
MalaCardsiTUBB2B
MIMi208150 phenotype
610031 phenotype
OpenTargetsiENSG00000137285
Orphaneti45358 Congenital fibrosis of extraocular muscles
1766 Dysequilibrium syndrome
300573 Polymicrogyria due to TUBB2B mutation
467166 Tubulinopathy-associated dysgyria
PharmGKBiPA142670671

Chemistry databases

ChEMBLiCHEMBL2095182
DrugBankiDB05147 CYT997

Polymorphism and mutation databases

BioMutaiTUBB2B
DMDMi74761283

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002626511 – 445Tubulin beta-2B chainAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineBy similarity1
Modified residuei55PhosphothreonineBy similarity1
Modified residuei58N6-acetyllysine; alternateBy similarity1
Modified residuei58N6-succinyllysine; alternateBy similarity1
Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei172Phosphoserine; by CDK11 Publication1
Modified residuei285PhosphothreonineBy similarity1
Modified residuei290PhosphothreonineBy similarity1
Modified residuei318Omega-N-methylarginineBy similarity1
Cross-linki324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei4385-glutamyl polyglutamateBy similarity1

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866).1 Publication
Some glutamate residues at the C-terminus are monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).1 Publication
Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9BVA1
MaxQBiQ9BVA1
PaxDbiQ9BVA1
PeptideAtlasiQ9BVA1
PRIDEiQ9BVA1
ProteomicsDBi79190
TopDownProteomicsiQ9BVA1

PTM databases

iPTMnetiQ9BVA1
PhosphoSitePlusiQ9BVA1
SwissPalmiQ9BVA1

Expressioni

Tissue specificityi

High expression in brain.1 Publication

Gene expression databases

BgeeiENSG00000137285 Expressed in 206 organ(s), highest expression level in brain
CleanExiHS_TUBB2B
GenevisibleiQ9BVA1 HS

Organism-specific databases

HPAiHPA043640
HPA046280

Interactioni

Subunit structurei

Dimer of alpha and beta chains (PubMed:23001566, PubMed:28013290, PubMed:26732629). A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CACNA1AO005552EBI-355665,EBI-766279

GO - Molecular functioni

Protein-protein interaction databases

BioGridi131483, 71 interactors
CORUMiQ9BVA1
IntActiQ9BVA1, 28 interactors
MINTiQ9BVA1
STRINGi9606.ENSP00000259818

Structurei

3D structure databases

ProteinModelPortaliQ9BVA1
SMRiQ9BVA1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119061
HOGENOMiHOG000165710
HOVERGENiHBG000089
InParanoidiQ9BVA1
KOiK07375
OMAiDMSATFI
OrthoDBiEOG091G06U2
PhylomeDBiQ9BVA1
TreeFamiTF300298

Family and domain databases

Gene3Di1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
InterProiView protein in InterPro
IPR013838 Beta-tubulin_BS
IPR002453 Beta_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase
PANTHERiPTHR11588 PTHR11588, 1 hit
PTHR11588:SF256 PTHR11588:SF256, 1 hit
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01163 BETATUBULIN
PR01161 TUBULIN
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227 TUBULIN, 1 hit
PS00228 TUBULIN_B_AUTOREG, 1 hit

Sequencei

Sequence statusi: Complete.

Q9BVA1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY
60 70 80 90 100
YNEATGNKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKESESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVM PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM
310 320 330 340 350
AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA DEQGEFEEEE GEDEA
Length:445
Mass (Da):49,953
Last modified:June 1, 2001 - v1
Checksum:i4DC3956EFF880746
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078186117L → P in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514569EnsemblClinVar.1
Natural variantiVAR_063389172S → P in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant dbSNP:rs137853194EnsemblClinVar.1
Natural variantiVAR_063390201C → S1 PublicationCorresponds to variant dbSNP:rs1054331Ensembl.1
Natural variantiVAR_063391210I → T in CDCBM7. 1 Publication1
Natural variantiVAR_063392228L → P in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs137853195EnsemblClinVar.1
Natural variantiVAR_078187239C → F in FADS; decreased tubulin heterodimer formation; decreased ability to incorporate into the cytoskeleton; no effect on microtubules disintegration; increased ability to repolymerize. 1 PublicationCorresponds to variant dbSNP:rs878853284EnsemblClinVar.1
Natural variantiVAR_078188256N → S in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514568EnsemblClinVar.1
Natural variantiVAR_063393265F → L in CDCBM7; affects microtubules assembly. 1 PublicationCorresponds to variant dbSNP:rs137853196EnsemblClinVar.1
Natural variantiVAR_063394312T → M in CDCBM7. 1 Publication1
Natural variantiVAR_078189390R → Q Probable disease-associated mutation found in a patient with cerebellar ataxia mental retardation and dysequilibrium syndrome; unknown pathological significance; no effect on protein folding; no effect on tubulin heterodimer formation; no effect on integration into the microtubule lattice; no effect on cytoskeleton subcellular location. 1 Publication1
Natural variantiVAR_078190417D → N in CDCBM7. 1 PublicationCorresponds to variant dbSNP:rs397514567EnsemblClinVar.1
Natural variantiVAR_078191421E → K in CDCBM7; decreased protein expression; decreased tubulin heterodimer formation; no effect on integration into the microtubule lattice; no effect on microtubule cytoskeleton subcellular location; loss of axon guidance. 1 PublicationCorresponds to variant dbSNP:rs398122369EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT019930 mRNA Translation: AAV38733.1
CR456788 mRNA Translation: CAG33069.1
AK289433 mRNA Translation: BAF82122.1
AL445309 Genomic DNA No translation available.
CH471087 Genomic DNA Translation: EAW55125.1
BC001352 mRNA Translation: AAH01352.1
BC063610 mRNA Translation: AAH63610.1
CCDSiCCDS4485.1
RefSeqiNP_821080.1, NM_178012.4
UniGeneiHs.300701

Genome annotation databases

EnsembliENST00000259818; ENSP00000259818; ENSG00000137285
GeneIDi347733
KEGGihsa:347733
UCSCiuc003mvg.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT019930 mRNA Translation: AAV38733.1
CR456788 mRNA Translation: CAG33069.1
AK289433 mRNA Translation: BAF82122.1
AL445309 Genomic DNA No translation available.
CH471087 Genomic DNA Translation: EAW55125.1
BC001352 mRNA Translation: AAH01352.1
BC063610 mRNA Translation: AAH63610.1
CCDSiCCDS4485.1
RefSeqiNP_821080.1, NM_178012.4
UniGeneiHs.300701

3D structure databases

ProteinModelPortaliQ9BVA1
SMRiQ9BVA1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi131483, 71 interactors
CORUMiQ9BVA1
IntActiQ9BVA1, 28 interactors
MINTiQ9BVA1
STRINGi9606.ENSP00000259818

Chemistry databases

ChEMBLiCHEMBL2095182
DrugBankiDB05147 CYT997

PTM databases

iPTMnetiQ9BVA1
PhosphoSitePlusiQ9BVA1
SwissPalmiQ9BVA1

Polymorphism and mutation databases

BioMutaiTUBB2B
DMDMi74761283

Proteomic databases

EPDiQ9BVA1
MaxQBiQ9BVA1
PaxDbiQ9BVA1
PeptideAtlasiQ9BVA1
PRIDEiQ9BVA1
ProteomicsDBi79190
TopDownProteomicsiQ9BVA1

Protocols and materials databases

DNASUi347733
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259818; ENSP00000259818; ENSG00000137285
GeneIDi347733
KEGGihsa:347733
UCSCiuc003mvg.4 human

Organism-specific databases

CTDi347733
DisGeNETi347733
EuPathDBiHostDB:ENSG00000137285.9
GeneCardsiTUBB2B
HGNCiHGNC:30829 TUBB2B
HPAiHPA043640
HPA046280
MalaCardsiTUBB2B
MIMi208150 phenotype
610031 phenotype
612850 gene
neXtProtiNX_Q9BVA1
OpenTargetsiENSG00000137285
Orphaneti45358 Congenital fibrosis of extraocular muscles
1766 Dysequilibrium syndrome
300573 Polymicrogyria due to TUBB2B mutation
467166 Tubulinopathy-associated dysgyria
PharmGKBiPA142670671
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1375 Eukaryota
COG5023 LUCA
GeneTreeiENSGT00760000119061
HOGENOMiHOG000165710
HOVERGENiHBG000089
InParanoidiQ9BVA1
KOiK07375
OMAiDMSATFI
OrthoDBiEOG091G06U2
PhylomeDBiQ9BVA1
TreeFamiTF300298

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-190840 Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane
R-HSA-190861 Gap junction assembly
R-HSA-2132295 MHC class II antigen presentation
R-HSA-2467813 Separation of Sister Chromatids
R-HSA-2500257 Resolution of Sister Chromatid Cohesion
R-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-HSA-380320 Recruitment of NuMA to mitotic centrosomes
R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-389960 Formation of tubulin folding intermediates by CCT/TriC
R-HSA-389977 Post-chaperonin tubulin folding pathway
R-HSA-437239 Recycling pathway of L1
R-HSA-5610787 Hedgehog 'off' state
R-HSA-5617833 Cilium Assembly
R-HSA-5620924 Intraflagellar transport
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-6807878 COPI-mediated anterograde transport
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-HSA-68877 Mitotic Prometaphase
R-HSA-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8955332 Carboxyterminal post-translational modifications of tubulin
R-HSA-983189 Kinesins

Miscellaneous databases

ChiTaRSiTUBB2B human
GenomeRNAii347733
PROiPR:Q9BVA1
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000137285 Expressed in 206 organ(s), highest expression level in brain
CleanExiHS_TUBB2B
GenevisibleiQ9BVA1 HS

Family and domain databases

Gene3Di1.10.287.600, 1 hit
3.30.1330.20, 1 hit
3.40.50.1440, 1 hit
InterProiView protein in InterPro
IPR013838 Beta-tubulin_BS
IPR002453 Beta_tubulin
IPR008280 Tub_FtsZ_C
IPR000217 Tubulin
IPR018316 Tubulin/FtsZ_2-layer-sand-dom
IPR037103 Tubulin/FtsZ_C_sf
IPR036525 Tubulin/FtsZ_GTPase_sf
IPR023123 Tubulin_C
IPR017975 Tubulin_CS
IPR003008 Tubulin_FtsZ_GTPase
PANTHERiPTHR11588 PTHR11588, 1 hit
PTHR11588:SF256 PTHR11588:SF256, 1 hit
PfamiView protein in Pfam
PF00091 Tubulin, 1 hit
PF03953 Tubulin_C, 1 hit
PRINTSiPR01163 BETATUBULIN
PR01161 TUBULIN
SMARTiView protein in SMART
SM00864 Tubulin, 1 hit
SM00865 Tubulin_C, 1 hit
SUPFAMiSSF52490 SSF52490, 1 hit
SSF55307 SSF55307, 1 hit
PROSITEiView protein in PROSITE
PS00227 TUBULIN, 1 hit
PS00228 TUBULIN_B_AUTOREG, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiTBB2B_HUMAN
AccessioniPrimary (citable) accession number: Q9BVA1
Secondary accession number(s): A8K068
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 2001
Last modified: November 7, 2018
This is version 167 of the entry and version 1 of the sequence. See 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
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