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Q9BVA1

- TBB2B_HUMAN

UniProt

Q9BVA1 - TBB2B_HUMAN

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Protein

Tubulin beta-2B chain

Gene

TUBB2B

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

Functioni

Tubulin is the major constituent of microtubules. 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). TUBB2B is implicated in neuronal migration.By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi140 – 1467GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: InterPro
  2. GTP binding Source: UniProtKB-KW
  3. structural constituent of cytoskeleton Source: InterPro

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. microtubule-based process Source: InterPro
  4. neuron migration Source: UniProtKB
  5. protein folding Source: Reactome
  6. protein polymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin beta-2B chain
Gene namesi
Name:TUBB2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:30829. TUBB2B.

Subcellular locationi

Cytoplasmcytoskeleton By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. microtubule Source: UniProtKB
  3. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Polymicrogyria, symmetric or asymmetric (PMGYSA) [MIM:610031]: A 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti172 – 1721S → P in PMGYSA; affects microtubules assembly. 1 Publication
VAR_063389
Natural varianti210 – 2101I → T in PMGYSA. 1 Publication
VAR_063391
Natural varianti228 – 2281L → P in PMGYSA. 1 Publication
VAR_063392
Natural varianti265 – 2651F → L in PMGYSA; affects microtubules assembly. 1 Publication
VAR_063393
Natural varianti312 – 3121T → M in PMGYSA. 1 Publication
VAR_063394

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi610031. phenotype.
Orphaneti45358. Congenital fibrosis of extraocular muscles.
300573. Polymicrogyria due to TUBB2B mutation.
PharmGKBiPA142670671.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Tubulin beta-2B chainPRO_0000262651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei172 – 1721Phosphoserine; by CDK1By similarity

Post-translational modificationi

Some glutamate residues at the C-terminus are polyglutamylated. This modification occurs exclusively on glutamate residues and results in polyglutamate chains on the gamma-carboxyl group. Also 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) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they regulate the assembly and dynamics of axonemal microtubules (Probable).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BVA1.
PaxDbiQ9BVA1.
PRIDEiQ9BVA1.

PTM databases

PhosphoSiteiQ9BVA1.

Expressioni

Tissue specificityi

High expression in brain.1 Publication

Gene expression databases

BgeeiQ9BVA1.
CleanExiHS_TUBB2B.
ExpressionAtlasiQ9BVA1. baseline and differential.
GenevestigatoriQ9BVA1.

Organism-specific databases

HPAiHPA043640.
HPA046280.

Interactioni

Subunit structurei

Dimer of alpha and beta chains. 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.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi131483. 50 interactions.
IntActiQ9BVA1. 17 interactions.
MINTiMINT-1152234.
STRINGi9606.ENSP00000259818.

Structurei

3D structure databases

ProteinModelPortaliQ9BVA1.
SMRiQ9BVA1. Positions 1-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119061.
HOGENOMiHOG000165710.
HOVERGENiHBG000089.
InParanoidiQ9BVA1.
KOiK07375.
OMAiYQQEEEY.
OrthoDBiEOG71ZP1H.
PhylomeDBiQ9BVA1.
TreeFamiTF300298.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERiPTHR11588. PTHR11588. 1 hit.
PfamiPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSiPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTiSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMiSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEiPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti172 – 1721S → P in PMGYSA; affects microtubules assembly. 1 Publication
VAR_063389
Natural varianti201 – 2011C → S.1 Publication
Corresponds to variant rs1054331 [ dbSNP | Ensembl ].
VAR_063390
Natural varianti210 – 2101I → T in PMGYSA. 1 Publication
VAR_063391
Natural varianti228 – 2281L → P in PMGYSA. 1 Publication
VAR_063392
Natural varianti265 – 2651F → L in PMGYSA; affects microtubules assembly. 1 Publication
VAR_063393
Natural varianti312 – 3121T → M in PMGYSA. 1 Publication
VAR_063394

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BT019930 mRNA. Translation: AAV38733.1.
CR456788 mRNA. Translation: CAG33069.1.
AK289433 mRNA. Translation: BAF82122.1.
AL445309 Genomic DNA. Translation: CAI40952.1.
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.3. human.

Polymorphism databases

DMDMi74761283.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BT019930 mRNA. Translation: AAV38733.1 .
CR456788 mRNA. Translation: CAG33069.1 .
AK289433 mRNA. Translation: BAF82122.1 .
AL445309 Genomic DNA. Translation: CAI40952.1 .
CH471087 Genomic DNA. Translation: EAW55125.1 .
BC001352 mRNA. Translation: AAH01352.1 .
BC063610 mRNA. Translation: AAH63610.1 .
CCDSi CCDS4485.1.
RefSeqi NP_821080.1. NM_178012.4.
UniGenei Hs.300701.

3D structure databases

ProteinModelPortali Q9BVA1.
SMRi Q9BVA1. Positions 1-431.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 131483. 50 interactions.
IntActi Q9BVA1. 17 interactions.
MINTi MINT-1152234.
STRINGi 9606.ENSP00000259818.

Chemistry

BindingDBi Q9BVA1.
ChEMBLi CHEMBL2095182.

PTM databases

PhosphoSitei Q9BVA1.

Polymorphism databases

DMDMi 74761283.

Proteomic databases

MaxQBi Q9BVA1.
PaxDbi Q9BVA1.
PRIDEi Q9BVA1.

Protocols and materials databases

DNASUi 347733.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259818 ; ENSP00000259818 ; ENSG00000137285 .
GeneIDi 347733.
KEGGi hsa:347733.
UCSCi uc003mvg.3. human.

Organism-specific databases

CTDi 347733.
GeneCardsi GC06M003224.
HGNCi HGNC:30829. TUBB2B.
HPAi HPA043640.
HPA046280.
MIMi 610031. phenotype.
612850. gene.
neXtProti NX_Q9BVA1.
Orphaneti 45358. Congenital fibrosis of extraocular muscles.
300573. Polymicrogyria due to TUBB2B mutation.
PharmGKBi PA142670671.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5023.
GeneTreei ENSGT00760000119061.
HOGENOMi HOG000165710.
HOVERGENi HBG000089.
InParanoidi Q9BVA1.
KOi K07375.
OMAi YQQEEEY.
OrthoDBi EOG71ZP1H.
PhylomeDBi Q9BVA1.
TreeFami TF300298.

Enzyme and pathway databases

Reactomei REACT_11039. Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
REACT_121399. MHC class II antigen presentation.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_15510. Recruitment of NuMA to mitotic centrosomes.
REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
REACT_16956. Formation of tubulin folding intermediates by CCT/TriC.
REACT_16967. Post-chaperonin tubulin folding pathway.
REACT_22365. Recycling pathway of L1.
REACT_25201. Kinesins.
REACT_682. Mitotic Prometaphase.
REACT_9509. Gap junction assembly.

Miscellaneous databases

ChiTaRSi TUBB2B. human.
GenomeRNAii 347733.
NextBioi 99262.
PROi Q9BVA1.
SOURCEi Search...

Gene expression databases

Bgeei Q9BVA1.
CleanExi HS_TUBB2B.
ExpressionAtlasi Q9BVA1. baseline and differential.
Genevestigatori Q9BVA1.

Family and domain databases

Gene3Di 1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProi IPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view ]
PANTHERi PTHR11588. PTHR11588. 1 hit.
Pfami PF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view ]
PRINTSi PR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTi SM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEi PS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "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].
  3. "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].
  4. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Brain and Muscle.
  7. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 47-58; 63-121; 163-174; 217-276; 283-297; 310-318; 325-359; 363-379 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  8. "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
    Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
    Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCYLATION.
  9. Cited for: FUNCTION, VARIANTS PMGYSA PRO-172; THR-210; PRO-228; LEU-265 AND MET-312, VARIANT SER-201, CHARACTERIZATION OF VARIANTS PMGYSA PRO-172 AND LEU-265.
  10. Cited for: TISSUE SPECIFICITY.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTBB2B_HUMAN
AccessioniPrimary (citable) accession number: Q9BVA1
Secondary accession number(s): A8K068
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 129 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3