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P23258

- TBG1_HUMAN

UniProt

P23258 - TBG1_HUMAN

Protein

Tubulin gamma-1 chain

Gene

TUBG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 2 (02 May 2002)
      Previous versions | rss
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    Functioni

    Tubulin is the major constituent of microtubules. The gamma chain is found at microtubule organizing centers (MTOC) such as the spindle poles or the centrosome. Pericentriolar matrix component that regulates alpha/beta chain minus-end nucleation, centrosome duplication and spindle formation.

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. cytoplasmic microtubule organization Source: InterPro
    2. G2/M transition of mitotic cell cycle Source: Reactome
    3. meiotic spindle organization Source: UniProtKB
    4. microtubule cytoskeleton organization Source: ProtInc
    5. microtubule nucleation Source: InterPro
    6. mitotic cell cycle Source: Reactome
    7. protein polymerization Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tubulin gamma-1 chain
    Alternative name(s):
    Gamma-1-tubulin
    Gamma-tubulin complex component 1
    Short name:
    GCP-1
    Gene namesi
    Name:TUBG1
    Synonyms:TUBG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:12417. TUBG1.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome 1 Publication

    GO - Cellular componenti

    1. apical part of cell Source: Ensembl
    2. cell leading edge Source: Ensembl
    3. centriole Source: Ensembl
    4. centrosome Source: UniProtKB
    5. ciliary basal body Source: Ensembl
    6. condensed nuclear chromosome Source: UniProtKB
    7. cytoplasm Source: UniProtKB
    8. cytoplasmic microtubule Source: Ensembl
    9. cytosol Source: Reactome
    10. gamma-tubulin complex Source: UniProtKB
    11. nonmotile primary cilium Source: Ensembl
    12. pericentriolar material Source: Ensembl
    13. polar microtubule Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule

    Pathology & Biotechi

    Involvement in diseasei

    Cortical dysplasia, complex, with other brain malformations 4 (CDCBM4) [MIM:615412]: A disorder of aberrant neuronal migration and disturbed axonal guidance. Clinical features include early-onset seizures, microcephaly, spastic tetraplegia, and various malformations of cortical development, such as agyria, posterior or frontal pachygyria, thick cortex, and subcortical band heterotopia and thin corpus callosum in some patients.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti92 – 921Y → C in CDCBM4. 1 Publication
    VAR_070577
    Natural varianti331 – 3311T → P in CDCBM4. 1 Publication
    VAR_070578
    Natural varianti387 – 3871L → P in CDCBM4; the chaperonin-dependent folding and hence the yield of monomeric gamma-tubulin is compromised. 1 Publication
    VAR_070579

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615412. phenotype.
    PharmGKBiPA37079.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 451451Tubulin gamma-1 chainPRO_0000048465Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei131 – 1311Phosphoserine; by BRSK1By similarity

    Post-translational modificationi

    Phosphorylation at Ser-131 by BRSK1 regulates centrosome duplication, possibly by mediating relocation of gamma-tubulin and its associated proteins from the cytoplasm to the centrosome.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP23258.
    PaxDbiP23258.
    PRIDEiP23258.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00295081.

    PTM databases

    PhosphoSiteiP23258.

    Miscellaneous databases

    PMAP-CutDBP23258.

    Expressioni

    Gene expression databases

    ArrayExpressiP23258.
    BgeeiP23258.
    CleanExiHS_TUBG1.
    GenevestigatoriP23258.

    Organism-specific databases

    HPAiCAB004608.

    Interactioni

    Subunit structurei

    Interacts with TUBGCP2 and TUBGCP3. Interacts with B9D2 By similarity. Interacts with CDK5RAP2; the interaction is leading to centrosomal localization of TUBG1 and CDK5RAP2. Interacts with PIFO.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AXIN1O151694EBI-302589,EBI-710484
    MARK4Q96L344EBI-302589,EBI-302319
    MZT1Q08AG72EBI-302589,EBI-2637198
    MZT2BQ6NZ672EBI-302589,EBI-1052566

    Protein-protein interaction databases

    BioGridi113134. 59 interactions.
    DIPiDIP-29890N.
    IntActiP23258. 31 interactions.
    MINTiMINT-4051249.
    STRINGi9606.ENSP00000251413.

    Structurei

    Secondary structure

    1
    451
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Helixi11 – 2818
    Beta strandi33 – 353
    Helixi48 – 503
    Beta strandi52 – 543
    Beta strandi60 – 623
    Beta strandi64 – 718
    Helixi72 – 798
    Turni81 – 855
    Helixi88 – 903
    Beta strandi91 – 933
    Helixi104 – 12724
    Beta strandi134 – 14411
    Helixi145 – 16016
    Beta strandi164 – 1729
    Helixi184 – 19714
    Beta strandi200 – 2067
    Helixi207 – 21610
    Helixi225 – 23915
    Turni240 – 2434
    Beta strandi244 – 2474
    Beta strandi248 – 2503
    Helixi253 – 2608
    Beta strandi262 – 2654
    Beta strandi268 – 2747
    Helixi290 – 2967
    Helixi300 – 3023
    Beta strandi303 – 3053
    Beta strandi317 – 32711
    Helixi330 – 34213
    Beta strandi350 – 3523
    Beta strandi356 – 3616
    Beta strandi374 – 3818
    Helixi382 – 3843
    Helixi385 – 40016
    Helixi406 – 4094
    Helixi412 – 4143
    Helixi419 – 43719
    Helixi441 – 4433

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z5VX-ray2.71A1-449[»]
    1Z5WX-ray3.00A1-449[»]
    3CB2X-ray2.30A/B1-451[»]
    ProteinModelPortaliP23258.
    SMRiP23258. Positions 2-446.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23258.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the tubulin family.Curated

    Phylogenomic databases

    eggNOGiCOG5023.
    HOGENOMiHOG000165714.
    HOVERGENiHBG098558.
    InParanoidiP23258.
    KOiK10389.
    OMAiEGFMLMH.
    OrthoDBiEOG70S755.
    PhylomeDBiP23258.
    TreeFamiTF300477.

    Family and domain databases

    Gene3Di1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProiIPR002454. Gamma_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]
    PRINTSiPR01164. GAMMATUBULIN.
    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]

    Sequencei

    Sequence statusi: Complete.

    P23258-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV    50
    FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA 100
    GNNWASGFSQ GEKIHEDIFD IIDREADGSD SLEGFVLCHS IAGGTGSGLG 150
    SYLLERLNDR YPKKLVQTYS VFPNQDEMSD VVVQPYNSLL TLKRLTQNAD 200
    CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST TTLRYPGYMN 250
    NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP 300
    KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP 350
    WGPASIQVAL SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQYDKLRK 400
    REAFLEQFRK EDMFKDNFDE MDTSREIVQQ LIDEYHAATR PDYISWGTQE 450
    Q 451
    Length:451
    Mass (Da):51,170
    Last modified:May 2, 2002 - v2
    Checksum:iE2A4C0179ED0CFE8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351G → A in AAA52620. (PubMed:1904010)Curated
    Sequence conflicti202 – 2021V → L in AAA52620. (PubMed:1904010)Curated

    Mass spectrometryi

    Molecular mass is 51197.98 Da from positions 1 - 451. Determined by MALDI. 1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti92 – 921Y → C in CDCBM4. 1 Publication
    VAR_070577
    Natural varianti331 – 3311T → P in CDCBM4. 1 Publication
    VAR_070578
    Natural varianti387 – 3871L → P in CDCBM4; the chaperonin-dependent folding and hence the yield of monomeric gamma-tubulin is compromised. 1 Publication
    VAR_070579
    Natural varianti413 – 4131M → V.
    Corresponds to variant rs13663 [ dbSNP | Ensembl ].
    VAR_052674

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61764 mRNA. Translation: AAA52620.1.
    BT019931 mRNA. Translation: AAV38734.1.
    CR407642 mRNA. Translation: CAG28570.1.
    AK313339 mRNA. Translation: BAG36143.1.
    BC000619 mRNA. Translation: AAH00619.1.
    CCDSiCCDS11433.1.
    PIRiA39527. UBHUG.
    RefSeqiNP_001061.2. NM_001070.4.
    UniGeneiHs.279669.

    Genome annotation databases

    EnsembliENST00000251413; ENSP00000251413; ENSG00000131462.
    GeneIDi7283.
    KEGGihsa:7283.
    UCSCiuc002ian.3. human.

    Polymorphism databases

    DMDMi20455518.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61764 mRNA. Translation: AAA52620.1 .
    BT019931 mRNA. Translation: AAV38734.1 .
    CR407642 mRNA. Translation: CAG28570.1 .
    AK313339 mRNA. Translation: BAG36143.1 .
    BC000619 mRNA. Translation: AAH00619.1 .
    CCDSi CCDS11433.1.
    PIRi A39527. UBHUG.
    RefSeqi NP_001061.2. NM_001070.4.
    UniGenei Hs.279669.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z5V X-ray 2.71 A 1-449 [» ]
    1Z5W X-ray 3.00 A 1-449 [» ]
    3CB2 X-ray 2.30 A/B 1-451 [» ]
    ProteinModelPortali P23258.
    SMRi P23258. Positions 2-446.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113134. 59 interactions.
    DIPi DIP-29890N.
    IntActi P23258. 31 interactions.
    MINTi MINT-4051249.
    STRINGi 9606.ENSP00000251413.

    PTM databases

    PhosphoSitei P23258.

    Polymorphism databases

    DMDMi 20455518.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00295081.

    Proteomic databases

    MaxQBi P23258.
    PaxDbi P23258.
    PRIDEi P23258.

    Protocols and materials databases

    DNASUi 7283.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251413 ; ENSP00000251413 ; ENSG00000131462 .
    GeneIDi 7283.
    KEGGi hsa:7283.
    UCSCi uc002ian.3. human.

    Organism-specific databases

    CTDi 7283.
    GeneCardsi GC17P040761.
    HGNCi HGNC:12417. TUBG1.
    HPAi CAB004608.
    MIMi 191135. gene.
    615412. phenotype.
    neXtProti NX_P23258.
    PharmGKBi PA37079.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5023.
    HOGENOMi HOG000165714.
    HOVERGENi HBG098558.
    InParanoidi P23258.
    KOi K10389.
    OMAi EGFMLMH.
    OrthoDBi EOG70S755.
    PhylomeDBi P23258.
    TreeFami TF300477.

    Enzyme and pathway databases

    Reactomei REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
    REACT_15364. Loss of Nlp from mitotic centrosomes.
    REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
    REACT_15510. Recruitment of NuMA to mitotic centrosomes.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

    Miscellaneous databases

    EvolutionaryTracei P23258.
    GeneWikii TUBG1.
    GenomeRNAii 7283.
    NextBioi 28475.
    PMAP-CutDB P23258.
    PROi P23258.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23258.
    Bgeei P23258.
    CleanExi HS_TUBG1.
    Genevestigatori P23258.

    Family and domain databases

    Gene3Di 1.10.287.600. 1 hit.
    3.30.1330.20. 1 hit.
    3.40.50.1440. 1 hit.
    InterProi IPR002454. Gamma_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 PR01164. GAMMATUBULIN.
    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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gamma-tubulin is present in Drosophila melanogaster and Homo sapiens and is associated with the centrosome."
      Zheng Y., Jung M.K., Oakley B.R.
      Cell 65:817-823(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
    3. "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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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.
      , 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].
      Tissue: Testis.
    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].
      Tissue: Skin.
    6. "Cluster analysis of an extensive human breast cancer cell line protein expression map database."
      Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.
      Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY.
      Tissue: Mammary cancer.
    7. "Characterization of the human homologue of the yeast spc98p and its association with gamma-tubulin."
      Tassin A.-M., Celati C., Moudjou M., Bornens M.
      J. Cell Biol. 141:689-701(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "CDK5RAP2 is a pericentriolar protein that functions in centrosomal attachment of the gamma-tubulin ring complex."
      Fong K.W., Choi Y.K., Rattner J.B., Qi R.Z.
      Mol. Biol. Cell 19:115-125(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDK5RAP2.
    9. Cited for: INTERACTION WITH PIFO.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: VARIANTS CDCBM4 CYS-92; PRO-331 AND PRO-387, CHARACTERIZATION OF VARIANT CDCBM4 PRO-387.

    Entry informationi

    Entry nameiTBG1_HUMAN
    AccessioniPrimary (citable) accession number: P23258
    Secondary accession number(s): Q53X79, Q9BW59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: May 2, 2002
    Last modified: October 1, 2014
    This is version 156 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3