P78318 (IGBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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
Renal carcinoma antigen NY-REN-16

Gene names

Name:	IGBP1
Synonyms:	IBP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Associated to surface IgM-receptor; may be involved in signal transduction. May be involved in regulation of the catalytic activity of type 2A-related serine/threonine phosphatases.
Subunit structure	Associates with PP2A-alpha and PP2A-beta catalytic subunits, and with PP4 and PP6. Interacts with MID1 and MID2. Ref.5 Ref.7
Subcellular location	Cytoplasm Potential.
Tissue specificity	Ubiquitously expressed with highest levels in heart, skeletal muscle and pancreas.
Post-translational modification	Phosphorylated By similarity.
Involvement in disease	Defects in IGBP1 are the cause of agenesis of the corpus callosum with mental retardation-ocular coloboma-micrognathia (ACCMRCM) [MIM:300472]. Ref.8
Sequence similarities	Belongs to the IGBP1/TAP42 family.

Ontologies

Keywords
Biological process	B-cell activation
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Disease	Mental retardation
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	B cell activation Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from mutant phenotype. Source: UniProtKB negative regulation of stress-activated MAPK cascade Inferred from mutant phenotype. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: UniProtKB regulation of microtubule-based movement Inferred from mutant phenotype. Source: UniProtKB response to interleukin-1 Inferred from mutant phenotype. Source: UniProtKB response to tumor necrosis factor Inferred from mutant phenotype. Source: UniProtKB signal transduction Non-traceable author statement Ref.5. Source: UniProtKB
Cellular component	cytoplasm Non-traceable author statement Ref.5. Source: UniProtKB
Molecular function	protein phosphatase type 2A regulator activity Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PPP2CA	P67775	9	EBI-1055954,EBI-712311
PPP2CB	P62714	3	EBI-1055954,EBI-1044367
PPP4C	P60510	7	EBI-1055954,EBI-1046072
PPP6C	O00743	8	EBI-1055954,EBI-359751

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 339	338	Immunoglobulin-binding protein 1		PRO_0000218618
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.9
	Modified residue	241	1	N6-acetyllysine Ref.10
Natural variations
	Natural variant	20	1	R → K. Corresponds to variant rs6625580 [ dbSNP | Ensembl ].		VAR_049570

Sequences

	Sequence		Length	Mass (Da)
	P78318 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: BB00A116EB45273A	FASTA	339	39,222
	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

References

	« Hide 'large scale' referencesShow '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: 9441740] [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: 15772651] [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: 15489334] [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: 9647778] [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: 10508479] [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: 11806752] [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: 14556245] [Abstract] Cited for: INVOLVEMENT IN ACCMRCM.
[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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241, MASS SPECTROMETRY.
[11]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	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.
IPI	IPI00019148.
RefSeq	NP_001542.1. NM_001551.2.
UniGene	Hs.496267.
3D structure databases
ProteinModelPortal	P78318.
SMR	P78318. Positions 9-221.
ModBase	Search...
Protein-protein interaction databases
IntAct	P78318. 18 interactions.
STRING	P78318.
PTM databases
PhosphoSite	P78318.
Polymorphism databases
DMDM	14285501.
Proteomic databases
PeptideAtlas	P78318.
PRIDE	P78318.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000342206; ENSP00000363661; ENSG00000089289. ENST00000356413; ENSP00000348784; ENSG00000089289.
GeneID	3476.
KEGG	hsa:3476.
UCSC	uc004dxv.1. human.
Organism-specific databases
CTD	3476.
GeneCards	GC0XP069353.
H-InvDB	HIX0016848.
HGNC	HGNC:5461. IGBP1.
HPA	HPA000634. HPA001004.
MIM	300139. gene. 300472. phenotype.
neXtProt	NX_P78318.
Orphanet	52055. Agenesis of the corpus callosum - intellectual deficit - coloboma - micrognathia.
PharmGKB	PA29694.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06297.
GeneTree	ENSGT00390000002414.
HOGENOM	HBG505864.
HOVERGEN	HBG052090.
InParanoid	P78318.
OMA	NDWYDQH.
OrthoDB	EOG451DRP.
PhylomeDB	P78318.
Gene expression databases
ArrayExpress	P78318.
Bgee	P78318.
CleanEx	HS_IGBP1.
Genevestigator	P78318.
GermOnline	ENSG00000089289. Homo sapiens.
Family and domain databases
InterPro	IPR007304. TAP42-like. [Graphical view]
PANTHER	PTHR10933. TAP42. 1 hit.
Pfam	PF04177. TAP42. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	13672.
SOURCE	Search...

Entry information

Entry name

IGBP1_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.