Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P78318

- IGBP1_HUMAN

UniProt

P78318 - IGBP1_HUMAN

Protein

Immunoglobulin-binding protein 1

Gene

IGBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Associated to surface IgM-receptor; may be involved in signal transduction. Involved in regulation of the catalytic activity of the phosphatases PP2A, PP4 and PP6 by protecting their partially folded catalytic subunits from degradative polyubiquitination until they associate with regulatory subunits.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei255 – 2562Cleavage; by calpain

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein phosphatase type 2A regulator activity Source: UniProtKB

    GO - Biological processi

    1. B cell activation Source: UniProtKB-KW
    2. negative regulation of apoptotic signaling pathway Source: Ensembl
    3. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    4. negative regulation of protein dephosphorylation Source: Ensembl
    5. negative regulation of stress-activated MAPK cascade Source: UniProtKB
    6. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    7. positive regulation of dephosphorylation Source: Ensembl
    8. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    9. regulation of microtubule-based movement Source: UniProtKB
    10. response to interleukin-1 Source: UniProtKB
    11. response to tumor necrosis factor Source: UniProtKB
    12. signal transduction Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    B-cell activation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Immunoglobulin-binding protein 1
    Alternative name(s):
    B-cell signal transduction molecule alpha 4
    Short name:
    Protein alpha-4
    CD79a-binding protein 1
    Protein phosphatase 2/4/6 regulatory subunit
    Renal carcinoma antigen NY-REN-16
    Gene namesi
    Name:IGBP1
    Synonyms:IBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:5461. IGBP1.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Mental retardation, X-linked, syndromic, 28 (MRXS28) [MIM:300472]: A mental retardation syndrome characterized by agenesis of the corpus callosum, coloboma of the iris and optic nerve, severe retrognathia, and intellectual deficit. Mental retardation is defined by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi155 – 1551R → E: Abolishes interaction with PPP2CA. 1 Publication
    Mutagenesisi158 – 1581K → D: Abolishes interaction with PPP2CA. 1 Publication
    Mutagenesisi162 – 1621Y → D: Abolishes interaction with PPP2CA. 1 Publication
    Mutagenesisi214 – 2141E → R: Abolishes interaction with PPP2CA. 1 Publication

    Keywords - Diseasei

    Mental retardation

    Organism-specific databases

    MIMi300472. phenotype.
    Orphaneti52055. Agenesis of the corpus callosum - intellectual disability - coloboma - micrognathia.
    PharmGKBiPA29694.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 339338Immunoglobulin-binding protein 1PRO_0000218618Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei241 – 2411N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated.By similarity
    Monoubiquitination by MID1 triggers calpain-mediated cleavage and switches IGBP1 activity from protective to destructive.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP78318.
    PaxDbiP78318.
    PeptideAtlasiP78318.
    PRIDEiP78318.

    PTM databases

    PhosphoSiteiP78318.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed with highest levels in heart, skeletal muscle and pancreas.

    Gene expression databases

    BgeeiP78318.
    CleanExiHS_IGBP1.
    GenevestigatoriP78318.

    Organism-specific databases

    HPAiCAB034139.
    HPA000634.
    HPA001004.

    Interactioni

    Subunit structurei

    Interacts with partially folded PPP2CA, but not with the fully active protein. Interacts with PPP2CB, and with PP4 and PP6. Interacts with MID1 and MID2. Interacts with ubiquitin.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PPP2CAP6777510EBI-1055954,EBI-712311
    PPP2CBP627143EBI-1055954,EBI-1044367
    PPP4CP605107EBI-1055954,EBI-1046072
    PPP6CO0074310EBI-1055954,EBI-359751
    TIPRLO756632EBI-1055954,EBI-1054735

    Protein-protein interaction databases

    BioGridi109698. 113 interactions.
    IntActiP78318. 20 interactions.
    MINTiMINT-3022988.
    STRINGi9606.ENSP00000348784.

    Structurei

    Secondary structure

    1
    339
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 54
    Helixi12 – 2716
    Helixi36 – 5924
    Helixi68 – 703
    Turni73 – 753
    Helixi76 – 805
    Helixi81 – 9010
    Helixi95 – 973
    Helixi98 – 11821
    Beta strandi143 – 1453
    Helixi156 – 18025
    Helixi186 – 21934

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IYPX-ray2.80A2-234[»]
    ProteinModelPortaliP78318.
    SMRiP78318. Positions 1-221.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati46 – 6015UIMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 202105Interaction with PPP2CAAdd
    BLAST
    Regioni225 – 29066Interaction with MID1Add
    BLAST

    Domaini

    The UIM domain is required for protective effect on PP2A.By similarity

    Sequence similaritiesi

    Belongs to the IGBP1/TAP42 family.Curated

    Phylogenomic databases

    eggNOGiNOG332001.
    HOGENOMiHOG000038526.
    HOVERGENiHBG052090.
    InParanoidiP78318.
    KOiK17606.
    OMAiGSRIIQD.
    OrthoDBiEOG7992R2.
    PhylomeDBiP78318.
    TreeFamiTF313433.

    Family and domain databases

    InterProiIPR007304. TAP42-like.
    [Graphical view]
    PANTHERiPTHR10933. PTHR10933. 1 hit.
    PfamiPF04177. TAP42. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P78318-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAEDELQLP RLPELFETGR QLLDEVEVAT EPAGSRIVQE KVFKGLDLLE    50
    KAAEMLSQLD LFSRNEDLEE IASTDLKYLL VPAFQGALTM KQVNPSKRLD 100
    HLQRAREHFI NYLTQCHCYH VAEFELPKTM NNSAENHTAN SSMAYPSLVA 150
    MASQRQAKIQ RYKQKKELEH RLSAMKSAVE SGQADDERVR EYYLLHLQRW 200
    IDISLEEIES IDQEIKILRE RDSSREASTS NSSRQERPPV KPFILTRNMA 250
    QAKVFGAGYP SLPTMTVSDW YEQHRKYGAL PDQGIAKAAP EEFRKAAQQQ 300
    EEQEEKEEED DEQTLHRARE WDDWKDTHPR GYGNRQNMG 339
    Length:339
    Mass (Da):39,222
    Last modified:May 1, 1997 - v1
    Checksum:iBB00A116EB45273A
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201R → K.
    Corresponds to variant rs6625580 [ dbSNP | Ensembl ].
    VAR_049570

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08915 mRNA. Translation: CAA70119.1.
    BT006736 mRNA. Translation: AAP35382.1.
    AL158141, AL139111 Genomic DNA. Translation: CAD13488.2.
    BC004137 mRNA. Translation: AAH04137.1.
    CCDSiCCDS14396.1.
    RefSeqiNP_001542.1. NM_001551.2.
    UniGeneiHs.496267.

    Genome annotation databases

    EnsembliENST00000342206; ENSP00000363661; ENSG00000089289.
    ENST00000356413; ENSP00000348784; ENSG00000089289.
    GeneIDi3476.
    KEGGihsa:3476.
    UCSCiuc004dxv.3. human.

    Polymorphism databases

    DMDMi14285501.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08915 mRNA. Translation: CAA70119.1 .
    BT006736 mRNA. Translation: AAP35382.1 .
    AL158141 , AL139111 Genomic DNA. Translation: CAD13488.2 .
    BC004137 mRNA. Translation: AAH04137.1 .
    CCDSi CCDS14396.1.
    RefSeqi NP_001542.1. NM_001551.2.
    UniGenei Hs.496267.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IYP X-ray 2.80 A 2-234 [» ]
    ProteinModelPortali P78318.
    SMRi P78318. Positions 1-221.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109698. 113 interactions.
    IntActi P78318. 20 interactions.
    MINTi MINT-3022988.
    STRINGi 9606.ENSP00000348784.

    PTM databases

    PhosphoSitei P78318.

    Polymorphism databases

    DMDMi 14285501.

    Proteomic databases

    MaxQBi P78318.
    PaxDbi P78318.
    PeptideAtlasi P78318.
    PRIDEi P78318.

    Protocols and materials databases

    DNASUi 3476.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342206 ; ENSP00000363661 ; ENSG00000089289 .
    ENST00000356413 ; ENSP00000348784 ; ENSG00000089289 .
    GeneIDi 3476.
    KEGGi hsa:3476.
    UCSCi uc004dxv.3. human.

    Organism-specific databases

    CTDi 3476.
    GeneCardsi GC0XP069353.
    HGNCi HGNC:5461. IGBP1.
    HPAi CAB034139.
    HPA000634.
    HPA001004.
    MIMi 300139. gene.
    300472. phenotype.
    neXtProti NX_P78318.
    Orphaneti 52055. Agenesis of the corpus callosum - intellectual disability - coloboma - micrognathia.
    PharmGKBi PA29694.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG332001.
    HOGENOMi HOG000038526.
    HOVERGENi HBG052090.
    InParanoidi P78318.
    KOi K17606.
    OMAi GSRIIQD.
    OrthoDBi EOG7992R2.
    PhylomeDBi P78318.
    TreeFami TF313433.

    Miscellaneous databases

    ChiTaRSi IGBP1. human.
    GeneWikii IGBP1.
    GenomeRNAii 3476.
    NextBioi 13672.
    PROi P78318.
    SOURCEi Search...

    Gene expression databases

    Bgeei P78318.
    CleanExi HS_IGBP1.
    Genevestigatori P78318.

    Family and domain databases

    InterProi IPR007304. TAP42-like.
    [Graphical view ]
    PANTHERi PTHR10933. PTHR10933. 1 hit.
    Pfami PF04177. TAP42. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression and chromosomal localization of the human alpha 4/IGBP1 gene, the structure of which is closely related to the yeast TAP42 protein of the rapamycin-sensitive signal transduction pathway."
      Onda M., Inui S., Maeda K., Suzuki M., Takahashi E., Sakaguchi N.
      Genomics 46:373-378(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: B-cell.
    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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Placenta.
    5. "Alpha 4 associates with protein phosphatases 2A, 4, and 6."
      Chen J., Peterson R.T., Schreiber S.L.
      Biochem. Biophys. Res. Commun. 247:827-832(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SERINE/THREONINE PROTEIN PHOSPHATASES.
    6. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    7. "MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, Alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disorders."
      Short K.M., Hopwood B., Yi Z., Cox T.C.
      BMC Cell Biol. 3:1-1(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MID1 AND MID2.
    8. "A new X-linked syndrome with agenesis of the corpus callosum, mental retardation, coloboma, micrognathia, and a mutation in the alpha 4 gene at Xq13."
      Graham J.M. Jr., Wheeler P., Tackels-Horne D., Lin A.E., Hall B.D., May M., Short K.M., Schwartz C.E., Cox T.C.
      Am. J. Med. Genet. A 123:37-44(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MRXS28.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "Alpha4 is an essential regulator of PP2A phosphatase activity."
      Kong M., Ditsworth D., Lindsten T., Thompson C.B.
      Mol. Cell 36:51-60(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PPP2CA.
    11. "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-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination."
      McConnell J.L., Watkins G.R., Soss S.E., Franz H.S., McCorvey L.R., Spiller B.W., Chazin W.J., Wadzinski B.E.
      Biochemistry 49:1713-1718(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH PPP2CA AND UBIQUITIN.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit alpha4, altering PP2A stability and microtubule-associated protein phosphorylation."
      Watkins G.R., Wang N., Mazalouskas M.D., Gomez R.J., Guthrie C.R., Kraemer B.C., Schweiger S., Spiller B.W., Wadzinski B.E.
      J. Biol. Chem. 287:24207-24215(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY MID1, PROTEOLYTIC CLEAVAGE.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-234 IN COMPLEX WITH PPP2CA, FUNCTION, MUTAGENESIS OF ARG-155; LYS-158; TYR-162 AND GLU-214, INTERACTION WITH PPP2CA.

    Entry informationi

    Entry nameiIGBP1_HUMAN
    AccessioniPrimary (citable) accession number: P78318
    Secondary accession number(s): Q8TAB2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 130 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 X
      Human chromosome X: 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