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Q14232

- EI2BA_HUMAN

UniProt

Q14232 - EI2BA_HUMAN

Protein

Translation initiation factor eIF-2B subunit alpha

Gene

EIF2B1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.

    GO - Molecular functioni

    1. enzyme regulator activity Source: Ensembl
    2. GDP binding Source: Ensembl
    3. GTP binding Source: Ensembl
    4. protein binding Source: IntAct
    5. translation initiation factor activity Source: UniProtKB-KW

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. cellular response to stimulus Source: UniProtKB
    3. gene expression Source: Reactome
    4. negative regulation of translational initiation in response to stress Source: Ensembl
    5. oligodendrocyte development Source: UniProtKB
    6. positive regulation of GTPase activity Source: GOC
    7. regulation of translational initiation Source: RefGenome
    8. response to glucose Source: UniProtKB
    9. response to heat Source: UniProtKB
    10. response to peptide hormone Source: UniProtKB
    11. translation Source: Reactome
    12. translational initiation Source: UniProtKB

    Keywords - Molecular functioni

    Initiation factor

    Keywords - Biological processi

    Protein biosynthesis

    Enzyme and pathway databases

    ReactomeiREACT_1815. Recycling of eIF2:GDP.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Translation initiation factor eIF-2B subunit alpha
    Alternative name(s):
    eIF-2B GDP-GTP exchange factor subunit alpha
    Gene namesi
    Name:EIF2B1
    Synonyms:EIF2BA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:3257. EIF2B1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. eukaryotic translation initiation factor 2B complex Source: UniProtKB
    4. membrane Source: MGI
    5. plasma membrane Source: MGI

    Pathology & Biotechi

    Involvement in diseasei

    Leukodystrophy with vanishing white matter (VWM) [MIM:603896]: A leukodystrophy that occurs mainly in children. Neurological signs include progressive cerebellar ataxia, spasticity, inconstant optic atrophy and relatively preserved mental abilities. The disease is chronic-progressive with, in most individuals, additional episodes of rapid deterioration following febrile infections or minor head trauma. While childhood onset is the most common form of the disorder, some severe forms are apparent at birth. A severe, early-onset form seen among the Cree and Chippewayan populations of Quebec and Manitoba is called Cree leukoencephalopathy. Milder forms may not become evident until adolescence or adulthood. Some females with milder forms of the disease who survive to adolescence exhibit ovarian dysfunction. This variant of the disorder is called ovarioleukodystrophy.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti183 – 1831V → F in VWM. 1 Publication
    VAR_068450
    Natural varianti208 – 2081N → Y in VWM. 1 Publication
    VAR_015404

    Keywords - Diseasei

    Disease mutation, Leukodystrophy

    Organism-specific databases

    MIMi603896. phenotype.
    Orphaneti99854. Cree leukoencephalopathy.
    157716. Late infantile CACH syndrome.
    99853. Ovarioleukodystrophy.
    PharmGKBiPA27688.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 305305Translation initiation factor eIF-2B subunit alphaPRO_0000156055Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei35 – 351N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ14232.
    PaxDbiQ14232.
    PRIDEiQ14232.

    PTM databases

    PhosphoSiteiQ14232.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14232.
    BgeeiQ14232.
    CleanExiHS_EIF2B1.
    GenevestigatoriQ14232.

    Organism-specific databases

    HPAiCAB034258.
    HPA049509.

    Interactioni

    Subunit structurei

    Complex of five different subunits; alpha, beta, gamma, delta and epsilon.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Adra2aQ013382EBI-491065,EBI-491073From a different organism.
    Adra2bP305452EBI-491065,EBI-491084From a different organism.

    Protein-protein interaction databases

    BioGridi108286. 18 interactions.
    IntActiQ14232. 19 interactions.
    MINTiMINT-1412710.
    STRINGi9606.ENSP00000228958.

    Structurei

    Secondary structure

    1
    305
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614
    Helixi22 – 3413
    Helixi44 – 5411
    Turni55 – 595
    Helixi63 – 7513
    Helixi92 – 10413
    Helixi107 – 1159
    Helixi116 – 1183
    Beta strandi123 – 1275
    Helixi132 – 14211
    Turni143 – 1453
    Beta strandi148 – 1536
    Turni156 – 1594
    Helixi160 – 16910
    Turni170 – 1723
    Beta strandi175 – 1784
    Helixi180 – 1823
    Helixi183 – 1864
    Helixi187 – 1893
    Beta strandi191 – 1966
    Beta strandi198 – 2003
    Beta strandi206 – 2094
    Helixi212 – 22110
    Beta strandi226 – 2294
    Helixi232 – 2343
    Helixi243 – 2453
    Helixi248 – 2503
    Beta strandi272 – 2765
    Helixi278 – 2803
    Beta strandi282 – 2865
    Beta strandi289 – 2913
    Helixi293 – 2953
    Helixi296 – 3049

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ECSX-ray2.65A/B/C/D/E/F/G/H1-305[»]
    ProteinModelPortaliQ14232.
    SMRiQ14232. Positions 1-305.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14232.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1184.
    HOGENOMiHOG000175731.
    HOVERGENiHBG051457.
    InParanoidiQ14232.
    KOiK03239.
    OMAiTESHKFV.
    OrthoDBiEOG7VHSZ3.
    PhylomeDBiQ14232.
    TreeFamiTF101505.

    Family and domain databases

    InterProiIPR000649. IF-2B-related.
    [Graphical view]
    PfamiPF01008. IF-2B. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14232-1) [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

    MDDKELIEYF KSQMKEDPDM ASAVAAIRTL LEFLKRDKGE TIQGLRANLT    50
    SAIETLCGVD SSVAVSSGGE LFLRFISLAS LEYSDYSKCK KIMIERGELF 100
    LRRISLSRNK IADLCHTFIK DGATILTHAY SRVVLRVLEA AVAAKKRFSV 150
    YVTESQPDLS GKKMAKALCH LNVPVTVVLD AAVGYIMEKA DLVIVGAEGV 200
    VENGGIINKI GTNQMAVCAK AQNKPFYVVA ESFKFVRLFP LNQQDVPDKF 250
    KYKADTLKVA QTGQDLKEEH PWVDYTAPSL ITLLFTDLGV LTPSAVSDEL 300
    IKLYL 305
    Length:305
    Mass (Da):33,712
    Last modified:November 1, 1997 - v1
    Checksum:i91A915FF1B80B780
    GO
    Isoform 2 (identifier: Q14232-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         162-222: KKMAKALCHL...NQMAVCAKAQ → QVPFCSVMCP...ITEFAAGRSI
         223-305: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:222
    Mass (Da):24,618
    Checksum:i12DDBDF049B4D351
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti183 – 1831V → F in VWM. 1 Publication
    VAR_068450
    Natural varianti208 – 2081N → Y in VWM. 1 Publication
    VAR_015404

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei162 – 22261KKMAK…CAKAQ → QVPFCSVMCPAIILQSKLRI TVQQDQNQNVPPACQQSALP FIVPFPAFGRKITEFAAGRS I in isoform 2. 1 PublicationVSP_055469Add
    BLAST
    Alternative sequencei223 – 30583Missing in isoform 2. 1 PublicationVSP_055470Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95648 mRNA. Translation: CAA64950.1.
    AK294815 mRNA. Translation: BAG57931.1.
    CR456831 mRNA. Translation: CAG33112.1.
    AC117503 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW98424.1.
    BC103763 mRNA. Translation: AAI03764.1.
    BC104188 mRNA. Translation: AAI04189.1.
    BC104189 mRNA. Translation: AAI04190.1.
    CCDSiCCDS31924.1.
    RefSeqiNP_001405.1. NM_001414.3.
    UniGeneiHs.741273.

    Genome annotation databases

    EnsembliENST00000424014; ENSP00000416250; ENSG00000111361. [Q14232-1]
    ENST00000537073; ENSP00000444183; ENSG00000111361. [Q14232-2]
    GeneIDi1967.
    KEGGihsa:1967.
    UCSCiuc001ufm.3. human.

    Polymorphism databases

    DMDMi2494303.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Mendelian genes eukaryotic translation initiation factor 2B, subunit 1 alpha, 26kDa (EIF2B1)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X95648 mRNA. Translation: CAA64950.1 .
    AK294815 mRNA. Translation: BAG57931.1 .
    CR456831 mRNA. Translation: CAG33112.1 .
    AC117503 Genomic DNA. No translation available.
    CH471054 Genomic DNA. Translation: EAW98424.1 .
    BC103763 mRNA. Translation: AAI03764.1 .
    BC104188 mRNA. Translation: AAI04189.1 .
    BC104189 mRNA. Translation: AAI04190.1 .
    CCDSi CCDS31924.1.
    RefSeqi NP_001405.1. NM_001414.3.
    UniGenei Hs.741273.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ECS X-ray 2.65 A/B/C/D/E/F/G/H 1-305 [» ]
    ProteinModelPortali Q14232.
    SMRi Q14232. Positions 1-305.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108286. 18 interactions.
    IntActi Q14232. 19 interactions.
    MINTi MINT-1412710.
    STRINGi 9606.ENSP00000228958.

    PTM databases

    PhosphoSitei Q14232.

    Polymorphism databases

    DMDMi 2494303.

    Proteomic databases

    MaxQBi Q14232.
    PaxDbi Q14232.
    PRIDEi Q14232.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000424014 ; ENSP00000416250 ; ENSG00000111361 . [Q14232-1 ]
    ENST00000537073 ; ENSP00000444183 ; ENSG00000111361 . [Q14232-2 ]
    GeneIDi 1967.
    KEGGi hsa:1967.
    UCSCi uc001ufm.3. human.

    Organism-specific databases

    CTDi 1967.
    GeneCardsi GC12M124105.
    GeneReviewsi EIF2B1.
    HGNCi HGNC:3257. EIF2B1.
    HPAi CAB034258.
    HPA049509.
    MIMi 603896. phenotype.
    606686. gene.
    neXtProti NX_Q14232.
    Orphaneti 99854. Cree leukoencephalopathy.
    157716. Late infantile CACH syndrome.
    99853. Ovarioleukodystrophy.
    PharmGKBi PA27688.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1184.
    HOGENOMi HOG000175731.
    HOVERGENi HBG051457.
    InParanoidi Q14232.
    KOi K03239.
    OMAi TESHKFV.
    OrthoDBi EOG7VHSZ3.
    PhylomeDBi Q14232.
    TreeFami TF101505.

    Enzyme and pathway databases

    Reactomei REACT_1815. Recycling of eIF2:GDP.

    Miscellaneous databases

    EvolutionaryTracei Q14232.
    GeneWikii EIF2B1.
    GenomeRNAii 1967.
    NextBioi 7975.
    PROi Q14232.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14232.
    Bgeei Q14232.
    CleanExi HS_EIF2B1.
    Genevestigatori Q14232.

    Family and domain databases

    InterProi IPR000649. IF-2B-related.
    [Graphical view ]
    Pfami PF01008. IF-2B. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Torp A.
      Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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.
      , 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] (ISOFORM 2).
      Tissue: Brain.
    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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [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] (ISOFORM 1).
    7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Mutations in each of the five subunits of translation initiation factor eIF2B can cause leukoencephalopathy with vanishing white matter."
      van der Knaap M.S., Leegwater P.A.J., Koenst A.A.M., Visser A., Naidu S., Oudejans C.B.M., Schutgens R.B.H., Pronk J.C.
      Ann. Neurol. 51:264-270(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWM TYR-208.
    11. "Identification of ten novel mutations in patients with eIF2B-related disorders."
      Ohlenbusch A., Henneke M., Brockmann K., Goerg M., Hanefeld F., Kohlschutter A., Gartner J.
      Hum. Mutat. 25:411-411(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT VWM PHE-183.

    Entry informationi

    Entry nameiEI2BA_HUMAN
    AccessioniPrimary (citable) accession number: Q14232
    Secondary accession number(s): A6NLY9, B4DGX0, Q3SXP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 122 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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