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Protein

Tubulin alpha-8 chain

Gene

TUBA8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi142 – 1487GTPSequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tubulin alpha-8 chain
Alternative name(s):
Alpha-tubulin 8
Tubulin alpha chain-like 2
Gene namesi
Name:TUBA8
Synonyms:TUBAL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:12410. TUBA8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Polymicrogyria, with optic nerve hypoplasia (PMGONH)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disease characterized by extensive polymicrogyria, optic nerve hypoplasia, severe developmental delay, hypotonia, seizures, a dysplastic or absent corpus callosum and colpocephaly. Polymicrogyria is 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.

See also OMIM:613180

Organism-specific databases

MIMi613180. phenotype.
Orphaneti250972. Polymicrogyria with optic nerve hypoplasia.
PharmGKBiPA37074.

Polymorphism and mutation databases

BioMutaiTUBA8.
DMDMi12585376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Tubulin alpha-8 chainPRO_0000048113Add
BLAST

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

Proteomic databases

MaxQBiQ9NY65.
PaxDbiQ9NY65.
PRIDEiQ9NY65.

PTM databases

PhosphoSiteiQ9NY65.

Miscellaneous databases

PMAP-CutDBQ9NY65.

Expressioni

Tissue specificityi

Preferentially expressed in heart, skeletal muscle and testis. Expressed at low levels in the developing brain.1 Publication

Gene expression databases

BgeeiQ9NY65.
CleanExiHS_TUBA8.
ExpressionAtlasiQ9NY65. baseline.
GenevisibleiQ9NY65. HS.

Organism-specific databases

HPAiCAB046031.
HPA043684.
HPA063394.

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.

Protein-protein interaction databases

BioGridi108282. 27 interactions.
119733. 23 interactions.
DIPiDIP-40751N.
IntActiQ9NY65. 3 interactions.
MINTiMINT-134532.
STRINGi9606.ENSP00000333326.

Structurei

3D structure databases

ProteinModelPortaliQ9NY65.
SMRiQ9NY65. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the tubulin family.Curated

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiQ9NY65.
KOiK07374.
K07514.
PhylomeDBiQ9NY65.
TreeFamiTF300314.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_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]
PRINTSiPR01162. ALPHATUBULIN.
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.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NY65-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MRECISVHVG QAGVQIGNAC WELFCLEHGI QADGTFDAQA SKINDDDSFT
60 70 80 90 100
TFFSETGNGK HVPRAVMIDL EPTVVDEVRA GTYRQLFHPE QLITGKEDAA
110 120 130 140 150
NNYARGHYTV GKESIDLVLD RIRKLTDACS GLQGFLIFHS FGGGTGSGFT
160 170 180 190 200
SLLMERLSLD YGKKSKLEFA IYPAPQVSTA VVEPYNSILT THTTLEHSDC
210 220 230 240 250
AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA SLRFDGALNV
260 270 280 290 300
DLTEFQTNLV PYPRIHFPLV TYAPIISAEK AYHEQLSVAE ITSSCFEPNS
310 320 330 340 350
QMVKCDPRHG KYMACCMLYR GDVVPKDVNV AIAAIKTKRT IQFVDWCPTG
360 370 380 390 400
FKVGINYQPP TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA
410 420 430 440
KRAFVHWYVG EGMEEGEFSE AREDLAALEK DYEEVGTDSF EEENEGEEF
Length:449
Mass (Da):50,094
Last modified:October 1, 2000 - v1
Checksum:i8D1AFB9D131529BD
GO
Isoform 2 (identifier: Q9NY65-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Show »
Length:383
Mass (Da):42,954
Checksum:iFA174EB2B97AF2D5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti128 – 1281A → V.
Corresponds to variant rs2234331 [ dbSNP | Ensembl ].
VAR_052670
Natural varianti301 – 3011Q → R.
Corresponds to variant rs2234333 [ dbSNP | Ensembl ].
VAR_024680

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6666Missing in isoform 2. 1 PublicationVSP_042810Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ245922 mRNA. Translation: CAB88036.1.
CR456600 mRNA. Translation: CAG30486.1.
AK056947 mRNA. Translation: BAG51831.1.
AK301521 mRNA. Translation: BAG63025.1.
AK315316 mRNA. Translation: BAG37719.1.
AC007934 Genomic DNA. No translation available.
AC128680 Genomic DNA. No translation available.
CH471193 Genomic DNA. Translation: EAW57788.1.
CH471193 Genomic DNA. Translation: EAW57789.1.
BC074827 mRNA. Translation: AAH74827.1.
BC104845 mRNA. Translation: AAI04846.1.
CCDSiCCDS13751.1. [Q9NY65-1]
CCDS54495.1. [Q9NY65-2]
RefSeqiNP_001159887.1. NM_001166415.1.
NP_001180343.1. NM_001193414.1. [Q9NY65-2]
NP_061816.1. NM_018943.2. [Q9NY65-1]
XP_011510819.1. XM_011512517.1.
UniGeneiHs.137400.
Hs.429879.

Genome annotation databases

EnsembliENST00000316027; ENSP00000318575; ENSG00000183785. [Q9NY65-2]
ENST00000330423; ENSP00000333326; ENSG00000183785.
GeneIDi1962.
51807.
KEGGihsa:1962.
hsa:51807.
UCSCiuc002znv.2. human. [Q9NY65-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ245922 mRNA. Translation: CAB88036.1.
CR456600 mRNA. Translation: CAG30486.1.
AK056947 mRNA. Translation: BAG51831.1.
AK301521 mRNA. Translation: BAG63025.1.
AK315316 mRNA. Translation: BAG37719.1.
AC007934 Genomic DNA. No translation available.
AC128680 Genomic DNA. No translation available.
CH471193 Genomic DNA. Translation: EAW57788.1.
CH471193 Genomic DNA. Translation: EAW57789.1.
BC074827 mRNA. Translation: AAH74827.1.
BC104845 mRNA. Translation: AAI04846.1.
CCDSiCCDS13751.1. [Q9NY65-1]
CCDS54495.1. [Q9NY65-2]
RefSeqiNP_001159887.1. NM_001166415.1.
NP_001180343.1. NM_001193414.1. [Q9NY65-2]
NP_061816.1. NM_018943.2. [Q9NY65-1]
XP_011510819.1. XM_011512517.1.
UniGeneiHs.137400.
Hs.429879.

3D structure databases

ProteinModelPortaliQ9NY65.
SMRiQ9NY65. Positions 1-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108282. 27 interactions.
119733. 23 interactions.
DIPiDIP-40751N.
IntActiQ9NY65. 3 interactions.
MINTiMINT-134532.
STRINGi9606.ENSP00000333326.

PTM databases

PhosphoSiteiQ9NY65.

Polymorphism and mutation databases

BioMutaiTUBA8.
DMDMi12585376.

Proteomic databases

MaxQBiQ9NY65.
PaxDbiQ9NY65.
PRIDEiQ9NY65.

Protocols and materials databases

DNASUi51807.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000316027; ENSP00000318575; ENSG00000183785. [Q9NY65-2]
ENST00000330423; ENSP00000333326; ENSG00000183785.
GeneIDi1962.
51807.
KEGGihsa:1962.
hsa:51807.
UCSCiuc002znv.2. human. [Q9NY65-1]

Organism-specific databases

CTDi1962.
51807.
GeneCardsiGC22P018593.
H-InvDBHIX0041378.
HGNCiHGNC:12410. TUBA8.
HPAiCAB046031.
HPA043684.
HPA063394.
MIMi605742. gene.
613180. phenotype.
neXtProtiNX_Q9NY65.
Orphaneti250972. Polymicrogyria with optic nerve hypoplasia.
PharmGKBiPA37074.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5023.
GeneTreeiENSGT00760000119060.
HOGENOMiHOG000165711.
HOVERGENiHBG000089.
InParanoidiQ9NY65.
KOiK07374.
K07514.
PhylomeDBiQ9NY65.
TreeFamiTF300314.

Miscellaneous databases

GeneWikiiTUBA8.
NextBioi55932.
PMAP-CutDBQ9NY65.
PROiQ9NY65.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NY65.
CleanExiHS_TUBA8.
ExpressionAtlasiQ9NY65. baseline.
GenevisibleiQ9NY65. HS.

Family and domain databases

Gene3Di1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProiIPR002452. Alpha_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]
PRINTSiPR01162. ALPHATUBULIN.
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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "TUBA8: a new tissue-specific isoform of alpha-tubulin that is highly conserved in human and mouse."
    Stanchi F., Corso V., Scannapieco P., Ievolella C., Negrisolo E., Tiso N., Lanfranchi G., Valle G.
    Biochem. Biophys. Res. Commun. 270:1111-1118(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Skeletal muscle.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Caudate nucleus and Skeletal muscle.
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
  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] (ISOFORM 1).
    Tissue: Brain.
  7. Cited for: INVOLVEMENT IN PMGONH.
  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. "Tuba8 is expressed at low levels in the developing mouse and human brain."
    Braun A., Breuss M., Salzer M.C., Flint J., Cowan N.J., Keays D.A.
    Am. J. Hum. Genet. 86:819-822(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiTBA8_HUMAN
AccessioniPrimary (citable) accession number: Q9NY65
Secondary accession number(s): B2RCX2
, B3KPW9, B4DWG3, Q2M3N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 136 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

Miscellaneous

This tubulin does not have a C-terminal tyrosine.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.