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Q8TF42 (UBS3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 94. 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:
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:KIAA1959, STS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length649 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.7 Ref.8

Catalytic activity

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

Subunit structure

Homodimer By similarity. Interacts with CBL. Part of a complex containing CBL and activated EGFR. Interacts with ubiquitin and with mono-ubiquitinated proteins. Ref.7

Subcellular location

Cytoplasm By similarity. Nucleus Potential.

Sequence similarities

Contains 1 SH3 domain.

Contains 1 UBA domain.

Sequence caution

The sequence AAL16953.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB85545.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SYKP434052EBI-1380492,EBI-78302

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 649649Ubiquitin-associated and SH3 domain-containing protein B
PRO_0000245508

Regions

Domain27 – 7650UBA
Domain254 – 31966SH3
Region380 – 649270Protein tyrosine phosphatase By similarity

Sites

Active site3901 By similarity
Active site3911Tele-phosphohistidine intermediate By similarity
Active site5761 By similarity

Amino acid modifications

Modified residue201Phosphoserine Ref.9
Modified residue231Phosphothreonine Ref.9

Natural variations

Natural variant681A → T. Ref.3
Corresponds to variant rs12790613 [ dbSNP | Ensembl ].
VAR_052676
Natural variant5691N → S.
Corresponds to variant rs35343548 [ dbSNP | Ensembl ].
VAR_061923

Experimental info

Sequence conflict4651H → R in BAD96563. Ref.3
Sequence conflict4651H → R in BAD96566. Ref.3

Secondary structure

........................... 649
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8TF42 [UniParc].

Last modified July 11, 2006. Version 2.
Checksum: 70ED9F50EA20BF43

FASTA64972,696
        10         20         30         40         50         60 
MAQYGHPSPL GMAAREELYS KVTPRRNRQQ RPGTIKHGSA LDVLLSMGFP RARAQKALAS 

        70         80         90        100        110        120 
TGGRSVQAAC DWLFSHVGDP FLDDPLPREY VLYLRPTGPL AQKLSDFWQQ SKQICGKNKA 

       130        140        150        160        170        180 
HNIFPHITLC QFFMCEDSKV DALGEALQTT VSRWKCKFSA PLPLELYTSS NFIGLFVKED 

       190        200        210        220        230        240 
SAEVLKKFAA DFAAEAASKT EVHVEPHKKQ LHVTLAYHFQ ASHLPTLEKL AQNIDVKLGC 

       250        260        270        280        290        300 
DWVATIFSRD IRFANHETLQ VIYPYTPQND DELELVPGDF IFMSPMEQTS TSEGWIYGTS 

       310        320        330        340        350        360 
LTTGCSGLLP ENYITKADEC STWIFHGSYS ILNTSSSNSL TFGDGVLERR PYEDQGLGET 

       370        380        390        400        410        420 
TPLTIICQPM QPLRVNSQPG PQKRCLFVCR HGERMDVVFG KYWLSQCFDA KGRYIRTNLN 

       430        440        450        460        470        480 
MPHSLPQRSG GFRDYEKDAP ITVFGCMQAR LVGEALLESN TIIDHVYCSP SLRCVQTAHN 

       490        500        510        520        530        540 
ILKGLQQENH LKIRVEPGLF EWTKWVAGST LPAWIPPSEL AAANLSVDTT YRPHIPISKL 

       550        560        570        580        590        600 
VVSESYDTYI SRSFQVTKEI ISECKSKGNN ILIVAHASSL EACTCQLQGL SPQNSKDFVQ 

       610        620        630        640 
MVRKIPYLGF CSCEELGETG IWQLTDPPIL PLTHGPTGGF NWRETLLQE 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins."
Nagase T., Kikuno R., Ohara O.
DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[3]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-68.
Tissue: Liver.
[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: Kidney.
[5]Bienvenut W.V., Claeys D.
Submitted (NOV-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 89-112; 188-199; 230-237 AND 417-428, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[6]"A novel SH3 containing protein is phosphorylated by the nm23-H1 protein kinase activity in vitro and shows reduced mRNA expression in human tumors."
Engel M., Seifert M., Maschlanka M., Welter C.
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 116-649.
[7]"Suppressors of T-cell receptor signaling Sts-1 and Sts-2 bind to Cbl and inhibit endocytosis of receptor tyrosine kinases."
Kowanetz K., Crosetto N., Haglund K., Schmidt M.H., Heldin C.-H., Dikic I.
J. Biol. Chem. 279:32786-32795(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CBL AND UBIQUITIN, IDENTIFICATION IN A COMPLEX WITH EGFR.
[8]"Suppressor of T-cell receptor signalling 1 and 2 differentially regulate endocytosis and signalling of receptor tyrosine kinases."
Raguz J., Wagner S., Dikic I., Hoeller D.
FEBS Lett. 581:4767-4772(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[9]"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-20 AND THR-23, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Solution structure of RSGI RUH-031, a UBA domain from human cDNA."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 26-76.
[11]"Solution structure of SH3 domain in suppressor of T-cell receptor signaling 1."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 248-328.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB075839 mRNA. Translation: BAB85545.1. Different initiation.
AK075203 mRNA. Translation: BAC11468.1.
AK222843 mRNA. Translation: BAD96563.1.
AK222846 mRNA. Translation: BAD96566.1.
BC007541 mRNA. Translation: AAH07541.2.
AF425252 mRNA. Translation: AAL16953.1. Different initiation.
RefSeqNP_116262.2. NM_032873.4.
UniGeneHs.444075.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPWNMR-A26-76[»]
2E5KNMR-A248-328[»]
ProteinModelPortalQ8TF42.
SMRQ8TF42. Positions 26-78, 249-328, 384-647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124390. 74 interactions.
IntActQ8TF42. 24 interactions.
MINTMINT-4829673.
STRING9606.ENSP00000284273.

PTM databases

PhosphoSiteQ8TF42.

Polymorphism databases

DMDM110287974.

Proteomic databases

PaxDbQ8TF42.
PRIDEQ8TF42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000284273; ENSP00000284273; ENSG00000154127.
GeneID84959.
KEGGhsa:84959.
UCSCuc001pyi.4. human.

Organism-specific databases

CTD84959.
GeneCardsGC11P122526.
HGNCHGNC:29884. UBASH3B.
HPAHPA038605.
HPA038607.
MIM609201. gene.
neXtProtNX_Q8TF42.
PharmGKBPA162407840.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG276661.
HOGENOMHOG000012936.
HOVERGENHBG018025.
InParanoidQ8TF42.
OMALSMGFPK.
OrthoDBEOG7P5T0D.
PhylomeDBQ8TF42.
TreeFamTF313334.

Enzyme and pathway databases

SignaLinkQ8TF42.

Gene expression databases

BgeeQ8TF42.
CleanExHS_UBASH3B.
GenevestigatorQ8TF42.

Family and domain databases

InterProIPR013078. His_Pase_superF_clade-1.
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.
PF00627. UBA. 1 hit.
[Graphical view]
SMARTSM00326. SH3. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8TF42.
GeneWikiSTS-1_(gene).
GenomeRNAi84959.
NextBio75468.
PROQ8TF42.
SOURCESearch...

Entry information

Entry nameUBS3B_HUMAN
AccessionPrimary (citable) accession number: Q8TF42
Secondary accession number(s): Q53GT5 expand/collapse secondary AC list , Q53GT8, Q8NBV7, Q96IG9, Q96NZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 11, 2006
Last modified: April 16, 2014
This is version 94 of the entry and version 2 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 11

Human chromosome 11: entries, gene names and cross-references to MIM