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P78318 (IGBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:IGBP1
Synonyms:IBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.16

Subunit structure

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. Ref.5 Ref.7 Ref.10 Ref.12 Ref.16

Subcellular location

Cytoplasm Potential.

Tissue specificity

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

Domain

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

Post-translational modification

Phosphorylated By similarity.

Monoubiquitination by MID1 triggers calpain-mediated cleavage and switches IGBP1 activity from protective to destructive.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the IGBP1/TAP42 family.

Contains 1 UIM (ubiquitin-interacting motif) repeat.

Ontologies

Keywords
   Biological processB-cell activation
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DiseaseMental retardation
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 17438131. Source: UniProtKB

negative regulation of protein dephosphorylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of stress-activated MAPK cascade

Inferred from mutant phenotype PubMed 17438131. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17438131. Source: UniProtKB

positive regulation of dephosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of microtubule-based movement

Inferred from mutant phenotype PubMed 18949047. Source: UniProtKB

response to interleukin-1

Inferred from mutant phenotype PubMed 17438131. Source: UniProtKB

response to tumor necrosis factor

Inferred from mutant phenotype PubMed 17438131. Source: UniProtKB

signal transduction

Non-traceable author statement Ref.5. Source: UniProtKB

   Cellular_componentcytoplasm

Non-traceable author statement Ref.5. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 16085932PubMed 16769727PubMed 18186651PubMed 18715871PubMed 18782753PubMed 19156129PubMed 21988832PubMed 23892082PubMed 24255178Ref.5. Source: IntAct

protein phosphatase type 2A regulator activity

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 339338Immunoglobulin-binding protein 1
PRO_0000218618

Regions

Repeat46 – 6015UIM
Region98 – 202105Interaction with PPP2CA
Region225 – 29066Interaction with MID1

Sites

Site255 – 2562Cleavage; by calpain

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.15
Modified residue2411N6-acetyllysine Ref.11

Natural variations

Natural variant201R → K.
Corresponds to variant rs6625580 [ dbSNP | Ensembl ].
VAR_049570

Experimental info

Mutagenesis1551R → E: Abolishes interaction with PPP2CA. Ref.16
Mutagenesis1581K → D: Abolishes interaction with PPP2CA. Ref.16
Mutagenesis1621Y → D: Abolishes interaction with PPP2CA. Ref.16
Mutagenesis2141E → R: Abolishes interaction with PPP2CA. Ref.16

Secondary structure

...................... 339
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P78318 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: BB00A116EB45273A

FASTA33939,222
        10         20         30         40         50         60 
MAAEDELQLP RLPELFETGR QLLDEVEVAT EPAGSRIVQE KVFKGLDLLE KAAEMLSQLD 

        70         80         90        100        110        120 
LFSRNEDLEE IASTDLKYLL VPAFQGALTM KQVNPSKRLD HLQRAREHFI NYLTQCHCYH 

       130        140        150        160        170        180 
VAEFELPKTM NNSAENHTAN SSMAYPSLVA MASQRQAKIQ RYKQKKELEH RLSAMKSAVE 

       190        200        210        220        230        240 
SGQADDERVR EYYLLHLQRW IDISLEEIES IDQEIKILRE RDSSREASTS NSSRQERPPV 

       250        260        270        280        290        300 
KPFILTRNMA QAKVFGAGYP SLPTMTVSDW YEQHRKYGAL PDQGIAKAAP EEFRKAAQQQ 

       310        320        330 
EEQEEKEEED DEQTLHRARE WDDWKDTHPR GYGNRQNMG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Structural basis of protein phosphatase 2A stable latency."
Jiang L., Stanevich V., Satyshur K.A., Kong M., Watkins G.R., Wadzinski B.E., Sengupta R., Xing Y.
Nat. Commun. 4:1699-1699(2013) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08915 mRNA. Translation: CAA70119.1.
BT006736 mRNA. Translation: AAP35382.1.
AL158141, AL139111 Genomic DNA. Translation: CAD13488.2.
BC004137 mRNA. Translation: AAH04137.1.
CCDSCCDS14396.1.
RefSeqNP_001542.1. NM_001551.2.
UniGeneHs.496267.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IYPX-ray2.80A2-234[»]
ProteinModelPortalP78318.
SMRP78318. Positions 1-221.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109698. 112 interactions.
IntActP78318. 20 interactions.
MINTMINT-3022988.
STRING9606.ENSP00000348784.

PTM databases

PhosphoSiteP78318.

Polymorphism databases

DMDM14285501.

Proteomic databases

MaxQBP78318.
PaxDbP78318.
PeptideAtlasP78318.
PRIDEP78318.

Protocols and materials databases

DNASU3476.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342206; ENSP00000363661; ENSG00000089289.
ENST00000356413; ENSP00000348784; ENSG00000089289.
GeneID3476.
KEGGhsa:3476.
UCSCuc004dxv.3. human.

Organism-specific databases

CTD3476.
GeneCardsGC0XP069353.
HGNCHGNC:5461. IGBP1.
HPACAB034139.
HPA000634.
HPA001004.
MIM300139. gene.
300472. phenotype.
neXtProtNX_P78318.
Orphanet52055. Agenesis of the corpus callosum - intellectual disability - coloboma - micrognathia.
PharmGKBPA29694.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG332001.
HOGENOMHOG000038526.
HOVERGENHBG052090.
InParanoidP78318.
KOK17606.
OMAGSRIIQD.
OrthoDBEOG7992R2.
PhylomeDBP78318.
TreeFamTF313433.

Gene expression databases

BgeeP78318.
CleanExHS_IGBP1.
GenevestigatorP78318.

Family and domain databases

InterProIPR007304. TAP42-like.
[Graphical view]
PANTHERPTHR10933. PTHR10933. 1 hit.
PfamPF04177. TAP42. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIGBP1. human.
GeneWikiIGBP1.
GenomeRNAi3476.
NextBio13672.
PROP78318.
SOURCESearch...

Entry information

Entry nameIGBP1_HUMAN
AccessionPrimary (citable) accession number: P78318
Secondary accession number(s): Q8TAB2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM