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Q8BGG7 (UBS3B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-associated and SH3 domain-containing protein B

EC=3.1.3.48
Alternative name(s):
Cbl-interacting protein p70
Suppressor of T-cell receptor signaling 1
Short name=STS-1
T-cell ubiquitin ligand 2
Short name=TULA-2
Tyrosine-protein phosphatase STS1/TULA2
Gene names
Name:Ubash3b
Synonyms:Sts1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination. Ref.5 Ref.6 Ref.7 Ref.10

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. Ref.8

Subunit structure

Homodimer. Interacts with JAK2 (in vitro). Interacts with CBL. Part of a complex containing CBL and activated EGFR. Interacts with ubiquitin and with mono-ubiquitinated proteins By similarity. Ref.4 Ref.9 Ref.10

Subcellular location

Cytoplasm By similarity. Nucleus Potential.

Tissue specificity

Detected in splenic T-cells and B-cells, total spleen, skeletal muscle, heart, lung, kidney, thymus, brain and liver (at protein level). Highly expressed in brain. Detected in heart, spleen, lung, liver, kidney and testis. Ref.4 Ref.5

Disruption phenotype

Mice display strikingly elevated levels of tyrosine phosphorylated, ubiquitinated proteins following TCR stimulation. They are prothrombotic and have shorter bleeding times, which is attributed to insufficient SYK dephosphorylation in platelets. Ref.6 Ref.7

Sequence similarities

Contains 1 SH3 domain.

Contains 1 UBA domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ZAP70P4340310EBI-8846415,EBI-1211276From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BGG7-1)

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: Q8BGG7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-122: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 638638Ubiquitin-associated and SH3 domain-containing protein B
PRO_0000245509

Regions

Domain23 – 6543UBA
Domain243 – 30866SH3
Region369 – 638270Protein tyrosine phosphatase
Compositional bias325 – 3284Poly-Ser

Sites

Active site3791 Ref.9 Ref.10
Active site3801Tele-phosphohistidine intermediate Ref.9 Ref.10
Active site5651 Ref.9 Ref.10

Amino acid modifications

Modified residue91Phosphoserine By similarity
Modified residue121Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 122122Missing in isoform 2.
VSP_019716

Experimental info

Sequence conflict3001E → G in BAE30779. Ref.2
Sequence conflict3001E → G in BAE30875. Ref.2

Secondary structure

............................................... 638
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 9B665F45AF208EF6

FASTA63871,443
        10         20         30         40         50         60 
MAAREELYSK VTPRRDRLQR PGTVKHGSAL DVLLSMGFPR ARAQKALAST GGRSVQAACD 

        70         80         90        100        110        120 
WLFSHVGDPF LDDPLPREYV LYLRPTGPLA QKLSDFWQQS KQICGKNKAH NIFPHITLCQ 

       130        140        150        160        170        180 
FFMCEDSKVD ALGEALQTTV SRWKCKFSAP LPLELYTSSN FIGLFVKEDS AEVLKKFAAD 

       190        200        210        220        230        240 
FAAEAASKTE VHVEPHKKQL HVTLAYHFQA SHLPTLEKLA QNIDVKLGCD WVATIFSRDI 

       250        260        270        280        290        300 
RFANHETLQV IYPYSPQNDD ELELVPGDFI FMSPMEQTST SEGWIYGTSL TTGCSGLLPE 

       310        320        330        340        350        360 
NYITKADECS TWIFHGSYSI LNTVSSSSLA FGDGALERRQ YEDQGLGETT PLTIICQPMQ 

       370        380        390        400        410        420 
PLRVNSQPGP QKRCLFVCRH GERMDVVFGK YWLSQCFDAK GRYIRTNLNM PHSLPQRSGG 

       430        440        450        460        470        480 
FRDYEKDAPI TVFGCMQARL VGEALLESNT VIDHVYCSPS LRCVQTAHNI LKGLQQDNHL 

       490        500        510        520        530        540 
KIRVEPGLFE WTKWVAGSTL PAWIPPSELA AANLSVDTTY RPHIPVSKLA ISESYDTYIN 

       550        560        570        580        590        600 
RSFQVTKEII SECKSKGNNI LIVAHASSLE ACTCQLQGLS PQNSKDFVQM VRKIPYLGFC 

       610        620        630 
SCEELGETGI WQLTDPPILP LTHGPTGGFN WRETLLQE 

« Hide

Isoform 2 [UniParc].

Checksum: 2F00BDB1F01C31FD
Show »

FASTA51657,693

References

« Hide 'large scale' references
[1]"NF-E2 inducible megakaryocyte specific novel gene."
Nagata Y., Oda M., Haruta H., Todokoro K.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Megakaryocyte.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Cerebellum, Dendritic cell, Diencephalon and Embryo.
[3]"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: Embryonic limb.
[4]"Identification, cDNA cloning, and targeted deletion of p70, a novel, ubiquitously expressed SH3 domain-containing protein."
Carpino N., Kobayashi R., Zang H., Takahashi Y., Jou S.-T., Feng J., Nakajima H., Ihle J.N.
Mol. Cell. Biol. 22:7491-7500(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 93-101; 199-215; 403-410; 482-493 AND 495-515, INTERACTION WITH JAK2, TISSUE SPECIFICITY.
[5]"Regulation of ZAP-70 activation and TCR signaling by two related proteins, Sts-1 and Sts-2."
Carpino N., Turner S., Mekala D., Takahashi Y., Zang H., Geiger T.L., Doherty P., Ihle J.N.
Immunity 20:37-46(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[6]"The Sts proteins target tyrosine phosphorylated, ubiquitinated proteins within TCR signaling pathways."
Carpino N., Chen Y., Nassar N., Oh H.W.
Mol. Immunol. 46:3224-3231(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[7]"A novel histidine tyrosine phosphatase, TULA-2, associates with Syk and negatively regulates GPVI signaling in platelets."
Thomas D.H., Getz T.M., Newman T.N., Dangelmaier C.A., Carpino N., Kunapuli S.P., Tsygankov A.Y., Daniel J.L.
Blood 116:2570-2578(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[8]"Determination of the substrate specificity of protein-tyrosine phosphatase TULA-2 and identification of Syk as a TULA-2 substrate."
Chen X., Ren L., Kim S., Carpino N., Daniel J.L., Kunapuli S.P., Tsygankov A.Y., Pei D.
J. Biol. Chem. 285:31268-31276(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY.
[9]"The 1.35 A resolution structure of the phosphatase domain of the suppressor of T-cell receptor signaling protein in complex with sulfate."
Jakoncic J., Sondgeroth B., Carpino N., Nassar N.
Acta Crystallogr. F 66:643-647(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 373-636 IN COMPLEX WITH SULFATE, SUBUNIT, ACTIVE SITE.
[10]"A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling."
Mikhailik A., Ford B., Keller J., Chen Y., Nassar N., Carpino N.
Mol. Cell 27:486-497(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 373-633, SUBUNIT, FUNCTION, PHOSPHATASE ACTIVITY, ACTIVE SITE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB075602 mRNA. Translation: BAD06450.1.
AK013361 mRNA. Translation: BAC25403.1.
AK034450 mRNA. Translation: BAC28714.1.
AK035764 mRNA. Translation: BAC29178.1.
AK133948 mRNA. Translation: BAE21945.1.
AK151895 mRNA. Translation: BAE30779.1.
AK152013 mRNA. Translation: BAE30875.1.
AK154576 mRNA. Translation: BAE32688.1.
BC053436 mRNA. Translation: AAH53436.1.
CCDSCCDS23085.1. [Q8BGG7-1]
RefSeqNP_789830.1. NM_176860.5. [Q8BGG7-1]
XP_006510700.1. XM_006510637.1. [Q8BGG7-2]
UniGeneMm.133615.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2H0QX-ray1.82A/B/C373-633[»]
2IKQX-ray2.61A/B/M369-638[»]
3MBKX-ray1.35A/B373-636[»]
ProteinModelPortalQ8BGG7.
SMRQ8BGG7. Positions 15-67, 238-317, 373-636.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BGG7. 1 interaction.
STRING10090.ENSMUSP00000043865.

PTM databases

PhosphoSiteQ8BGG7.

Proteomic databases

MaxQBQ8BGG7.
PaxDbQ8BGG7.
PRIDEQ8BGG7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044155; ENSMUSP00000043865; ENSMUSG00000032020. [Q8BGG7-1]
ENSMUST00000151485; ENSMUSP00000116038; ENSMUSG00000032020. [Q8BGG7-2]
GeneID72828.
KEGGmmu:72828.
UCSCuc009pag.1. mouse. [Q8BGG7-1]

Organism-specific databases

CTD84959.
MGIMGI:1920078. Ubash3b.

Phylogenomic databases

eggNOGNOG276661.
GeneTreeENSGT00390000018249.
HOGENOMHOG000012936.
HOVERGENHBG018025.
InParanoidQ8BGG7.
OMAADECGTW.
OrthoDBEOG7P5T0D.
PhylomeDBQ8BGG7.
TreeFamTF313334.

Gene expression databases

ArrayExpressQ8BGG7.
BgeeQ8BGG7.
CleanExMM_UBASH3B.
GenevestigatorQ8BGG7.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
InterProIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001452. SH3_domain.
IPR009060. UBA-like.
IPR015940. UBA/transl_elong_EF1B_N_euk.
IPR000449. UBA/Ts_N.
[Graphical view]
PfamPF00300. His_Phos_1. 1 hit.
PF14604. SH3_9. 1 hit.
PF00627. UBA. 1 hit.
[Graphical view]
SMARTSM00326. SH3. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF53254. SSF53254. 2 hits.
PROSITEPS50002. SH3. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8BGG7.
NextBio337005.
PROQ8BGG7.
SOURCESearch...

Entry information

Entry nameUBS3B_MOUSE
AccessionPrimary (citable) accession number: Q8BGG7
Secondary accession number(s): Q3U8Z2, Q8BMW9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot