Q15750 (TAB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
TGF-beta-activated kinase 1 and MAP3K7-binding protein 1

Alternative name(s):
Mitogen-activated protein kinase kinase kinase 7-interacting protein 1
TGF-beta-activated kinase 1-binding protein 1
Short name=TAK1-binding protein 1

Gene names

Name:	TAB1
Synonyms:	MAP3K7IP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	504 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May be an important signaling intermediate between TGFB receptors and MAP3K7/TAK1. May play an important role in mammalian embryogenesis. Ref.15
Subunit structure	Interacts with XIAP and BIRC7. Interacts with TRAF6 and MAP3K7; during IL-1 signaling. Identified in the TRIKA2 complex composed of MAP3K7, TAB1 and TAB2. Ref.1 Ref.7 Ref.8
Tissue specificity	Ubiquitous.
Post-translational modification	Monoubiquitinated. Deubiquitinated by Y.enterocolitica YopP.
Sequence similarities	Contains 1 PP2C-like domain.
Caution	Lacks several key residues involved in metal-binding and catalytic activity, therefore has lost phosphatase activity.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	I-kappaB kinase/NF-kappaB cascade Traceable author statement. Source: Reactome JNK cascade Traceable author statement. Source: Reactome MyD88-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome TRIF-dependent toll-like receptor signaling pathway Traceable author statement. Source: Reactome activation of MAPK activity Traceable author statement. Source: Reactome activation of MAPKKK activity Traceable author statement Ref.1. Source: ProtInc heart morphogenesis Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome lung development Inferred from electronic annotation. Source: Compara nucleotide-binding oligomerization domain containing signaling pathway Traceable author statement. Source: Reactome positive regulation of NF-kappaB transcription factor activity Traceable author statement. Source: Reactome toll-like receptor 10 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 3 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 4 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 5 signaling pathway Traceable author statement. Source: Reactome toll-like receptor 9 signaling pathway Traceable author statement. Source: Reactome toll-like receptor TLR1:TLR2 signaling pathway Traceable author statement. Source: Reactome toll-like receptor TLR6:TLR2 signaling pathway Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome endosome membrane Traceable author statement. Source: Reactome
Molecular_function	catalytic activity Inferred from electronic annotation. Source: InterPro enzyme activator activity Traceable author statement Ref.1. Source: ProtInc kinase activator activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15750-1)

Also known as: TAB1alpha;

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.

Isoform 2 (identifier: Q15750-2)

Also known as: TAB1beta;

The sequence of this isoform differs from the canonical sequence as follows:
     436-504: NQSPTLTLQS...HGEQSVVTAP → KDPSRPASDLTAIPQCQLNLLGSLTPG

Note: Does not bind nor activate MAP3K7/TAK1.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 504

504

TGF-beta-activated kinase 1 and MAP3K7-binding protein 1

PRO_0000057797

Regions

Domain

64 – 368

305

PP2C-like

Compositional bias

452 – 457

6

Poly-Ser

Amino acid modifications

Modified residue

7

1

Phosphoserine Ref.10 Ref.11

Modified residue

378

1

Phosphoserine Ref.12

Modified residue

438

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

436 – 504

69

NQSPT…VVTAP → KDPSRPASDLTAIPQCQLNL LGSLTPG in isoform 2.

VSP_042024

Natural variant

224

1

D → E.
Corresponds to variant rs17001096 [ dbSNP | Ensembl ].

VAR_039271

Experimental info

Mutagenesis

213

1

D → A: Loss of interaction with XIAP. Ref.16

Mutagenesis

216

1

F → A: Loss of interaction with XIAP. Ref.16

Mutagenesis

438

1

S → A: Loss of phosphorylation site. Ref.9

Secondary structure

1

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504

Helix Strand Turn

Details...

Turn

18 – 20

3

Beta strand

27 – 32

6

Beta strand

35 – 37

3

Beta strand

39 – 42

4

Beta strand

51 – 58

8

Turn

59 – 61

3

Beta strand

62 – 74

13

Helix

75 – 86

12

Beta strand

89 – 92

4

Beta strand

94 – 96

3

Helix

99 – 133

35

Helix

141 – 143

3

Helix

146 – 148

3

Helix

149 – 162

14

Beta strand

165 – 174

10

Beta strand

177 – 185

9

Beta strand

187 – 193

7

Beta strand

195 – 202

8

Helix

212 – 219

8

Turn

220 – 222

3

Helix

225 – 231

7

Beta strand

234 – 236

3

Beta strand

239 – 241

3

Helix

246 – 250

5

Helix

252 – 254

3

Turn

256 – 260

5

Beta strand

265 – 267

3

Beta strand

271 – 277

7

Beta strand

283 – 288

6

Helix

290 – 300

11

Beta strand

302 – 304

3

Helix

305 – 319

15

Helix

323 – 343

21

Helix

348 – 351

4

Beta strand

353 – 355

3

Beta strand

358 – 366

9

Beta strand

475 – 478

4

Helix

485 – 495

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TAB1alpha) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A45743288718983A	FASTA	504	54,644
	10 20 30 40 50 60 MAAQRRSLLQ SEQQPSWTDD LPLCHLSGVG SASNRSYSAD GKGTESHPPE DSWLKFRSEN 70 80 90 100 110 120 NCFLYGVFNG YDGNRVTNFV AQRLSAELLL GQLNAEHAEA DVRRVLLQAF DVVERSFLES 130 140 150 160 170 180 IDDALAEKAS LQSQLPEGVP QHQLPPQYQK ILERLKTLER EISGGAMAVV AVLLNNKLYV 190 200 210 220 230 240 ANVGTNRALL CKSTVDGLQV TQLNVDHTTE NEDELFRLSQ LGLDAGKIKQ VGIICGQEST 250 260 270 280 290 300 RRIGDYKVKY GYTDIDLLSA AKSKPIIAEP EIHGAQPLDG VTGFLVLMSE GLYKALEAAH 310 320 330 340 350 360 GPGQANQEIA AMIDTEFAKQ TSLDAVAQAV VDRVKRIHSD TFASGGERAR FCPRHEDMTL 370 380 390 400 410 420 LVRNFGYPLG EMSQPTPSPA PAAGGRVYPV SVPYSSAQST SKTSVTLSLV MPSQGQMVNG 430 440 450 460 470 480 AHSASTLDEA TPTLTNQSPT LTLQSTNTHT QSSSSSSDGG LFRSRPAHSL PPGEDGRVEP 490 500 YVDFAEFYRL WSVDHGEQSV VTAP
	Isoform 2 (TAB1beta) [UniParc]. Checksum: E26443BBE3BD3404	FASTA	462	49,917
	10 20 30 40 50 60 MAAQRRSLLQ SEQQPSWTDD LPLCHLSGVG SASNRSYSAD GKGTESHPPE DSWLKFRSEN 70 80 90 100 110 120 NCFLYGVFNG YDGNRVTNFV AQRLSAELLL GQLNAEHAEA DVRRVLLQAF DVVERSFLES 130 140 150 160 170 180 IDDALAEKAS LQSQLPEGVP QHQLPPQYQK ILERLKTLER EISGGAMAVV AVLLNNKLYV 190 200 210 220 230 240 ANVGTNRALL CKSTVDGLQV TQLNVDHTTE NEDELFRLSQ LGLDAGKIKQ VGIICGQEST 250 260 270 280 290 300 RRIGDYKVKY GYTDIDLLSA AKSKPIIAEP EIHGAQPLDG VTGFLVLMSE GLYKALEAAH 310 320 330 340 350 360 GPGQANQEIA AMIDTEFAKQ TSLDAVAQAV VDRVKRIHSD TFASGGERAR FCPRHEDMTL 370 380 390 400 410 420 LVRNFGYPLG EMSQPTPSPA PAAGGRVYPV SVPYSSAQST SKTSVTLSLV MPSQGQMVNG 430 440 450 460 AHSASTLDEA TPTLTKDPSR PASDLTAIPQ CQLNLLGSLT PG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TAB1: an activator of the TAK1 MAPKKK in TGF-beta signal transduction." Shibuya H., Yamaguchi K., Shirakabe K., Tonegawa A., Gotoh Y., Ueno N., Irie K., Nishida E., Matsumoto K. Science 272:1179-1182(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH MAP3K7. Tissue: Brain.
[2]	"TAB1beta (transforming growth factor-beta-activated protein kinase 1-binding protein 1beta), a novel splicing variant of TAB1 that interacts with p38alpha but not TAK1." Ge B., Xiong X., Jing Q., Mosley J.L., Filose A., Bian D., Huang S., Han J. J. Biol. Chem. 278:2286-2293(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[3]	NHLBI resequencing and genotyping service (RS&G) Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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). Tissue: PNS.
[7]	"The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway." Ninomiya-Tsuji J., Kishimoto K., Hiyama A., Inoue J., Cao Z., Matsumoto K. Nature 398:252-256(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TRAF6 AND MAP3K7.
[8]	"TAK1 is a ubiquitin-dependent kinase of MKK and IKK." Wang C., Deng L., Hong M., Akkaraju G.R., Inoue J., Chen Z.J. Nature 412:346-351(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, IDENTIFICATION IN THE TRIKA2 COMPLEX.
[9]	"The Yersinia enterocolitica effector YopP inhibits host cell signalling by inactivating the protein kinase TAK1 in the IL-1 signalling pathway." Thiefes A., Wolf A., Doerrie A., Grassl G.A., Matsumoto K., Autenrieth I., Bohn E., Sakurai H., Niedenthal R., Resch K., Kracht M. EMBO Rep. 7:838-844(2006) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, PHOSPHORYLATION AT SER-438, MUTAGENESIS OF SER-438, DEUBIQUITINATION BY YOPP.
[10]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"TAK1-binding protein 1 is a pseudophosphatase." Conner S.H., Kular G., Peggie M., Shepherd S., Schuettelkopf A.W., Cohen P., Van Aalten D.M.F. Biochem. J. 399:427-434(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-401, ABSENCE OF FUNCTION AS A PHOSPHATASE.
[16]	"XIAP induces NF-kappaB activation via the BIR1/TAB1 interaction and BIR1 dimerization." Lu M., Lin S.-C., Huang Y., Kang Y.J., Rich R., Lo Y.-C., Myszka D., Han J., Wu H. Mol. Cell 26:689-702(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1-370 IN COMPLEX WITH XIAP, MUTAGENESIS OF ASP-213 AND PHE-216.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U49928 mRNA. Translation: AAC12660.1.
AF425640 mRNA. Translation: AAN32760.1.
DQ314876 Genomic DNA. Translation: ABC40735.1.
AL022312 Genomic DNA. No translation available.
Z83845 Genomic DNA. Translation: CAB55304.1.
Z83845 Genomic DNA. Translation: CAQ07045.1.
CH471095 Genomic DNA. Translation: EAW60326.1.
BC050554 mRNA. Translation: AAH50554.1.

IPI

IPI00019459.

RefSeq

NP_006107.1. NM_006116.2.
NP_705717.1. NM_153497.2.

UniGene

Hs.507681.
Hs.729080.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J4O	X-ray	2.25	A	1-401	[»]
2POM	X-ray	2.27	A	1-370	[»]
2POP	X-ray	3.10	A/C	1-370	[»]
2YIY	X-ray	2.49	A	468-497	[»]
4AY5	X-ray	3.15	I/J/K/L	389-399	[»]
4AY6	X-ray	3.30	E/F/G/H	389-401	[»]
4GS6	X-ray	2.20	A	468-504	[»]

ProteinModelPortal

Q15750.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-27524N.

IntAct

Q15750. 19 interactions.

MINT

MINT-88613.

PTM databases

PhosphoSite

Q15750.

Polymorphism databases

DMDM

10720303.

Proteomic databases

PaxDb

Q15750.

PRIDE

Q15750.

Protocols and materials databases

DNASU

10454.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216160; ENSP00000216160; ENSG00000100324.
ENST00000331454; ENSP00000333049; ENSG00000100324.

GeneID

10454.

KEGG

hsa:10454.

UCSC

uc003axt.3. human.
uc003axu.1. human.

Organism-specific databases

CTD

10454.

GeneCards

GC22P039796.

HGNC

HGNC:18157. TAB1.

HPA

CAB032328.

MIM

602615. gene.

neXtProt

NX_Q15750.

PharmGKB

PA30604.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG320352.

HOGENOM

HOG000044226.

HOVERGEN

HBG007302.

InParanoid

Q15750.

KO

K04403.

OMA

AEHTEAD.

OrthoDB

EOG4R7V9G.

PhylomeDB

Q15750.

Enzyme and pathway databases

Pathway_Interaction_DB

bmppathway. BMP receptor signaling.
il1pathway. IL1-mediated signaling events.
wnt_calcium_pathway. Noncanonical Wnt signaling pathway.
p38_mkk3_6pathway. p38 MAPK signaling pathway.
ps1pathway. Presenilin action in Notch and Wnt signaling.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
tgfbrpathway. TGF-beta receptor signaling.
tnfpathway. TNF receptor signaling pathway.

Reactome

REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6900. Immune System.

SignaLink

Q15750.

Gene expression databases

ArrayExpress

Q15750.

Bgee

Q15750.

CleanEx

HS_MAP3K7IP1.

Genevestigator

Q15750.

GermOnline

ENSG00000100324. Homo sapiens.

Family and domain databases

Gene3D

3.60.40.10. 1 hit.

InterPro

IPR001932. PP2C-like.
IPR015655. Protein_Pase_2C.
[Graphical view]

PANTHER

PTHR13832. PTHR13832. 1 hit.

Pfam

PF00481. PP2C. 1 hit.
[Graphical view]

SMART

SM00332. PP2Cc. 1 hit.
[Graphical view]

SUPFAM

SSF81606. PP2C-related. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q15750.

ChEMBL

CHEMBL5605.

ChiTaRS

TAB1. human.

EvolutionaryTrace

Q15750.

GenomeRNAi

10454.

NextBio

39627.

SOURCE

Search...

Entry information

Entry name

TAB1_HUMAN

Accession

Primary (citable) accession number: Q15750
Secondary accession number(s): Q2PP09, Q8IZW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1996
Last modified:	May 29, 2013
This is version 128 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.