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Q3UTJ2 (SRBS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sorbin and SH3 domain-containing protein 2
Alternative name(s):
Arg/Abl-interacting protein 2
Short name=ArgBP2
Gene names
Name:Sorbs2
Synonyms:Argbp2, Kiaa0777
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length1180 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein that plays a role in the assembling of signaling complexes, being a link between ABL kinases and actin cytoskeleton. Can form complex with ABL1 and CBL, thus promoting ubiquitination and degradation of ABL1 or with AKT1 and PAK1, thus mediating AKT1-mediated activation of PAK1 By similarity.

Subunit structure

Interacts with ABL, CBL, DNM1, DNM2, FLOT1, MLLT4/afadin, PTK2B/PYK2, SAPAP, SPTAN1, SYNJ1, SYNJ2, VCL/vinculin, WASF, ABL1/c-Abl, ABL2/v-Abl/Arg, ACTN, AKT1, CBL, PALLD and PAK1 By similarity.

Subcellular location

Cytoplasm › perinuclear region By similarity. Cytoplasm › myofibril › sarcomere › Z line By similarity. Cell junction › focal adhesion By similarity. Cytoplasm › cytoskeleton By similarity. Note: Found at the Z line sarcomeres, stress fibers, dense bodies and focal adhesion By similarity.

Post-translational modification

Ubiquitinated by CBL By similarity.

Sequence similarities

Contains 3 SH3 domains.

Contains 1 SoHo domain.

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH3 domain
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentZ disc

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay PubMed 21689717. Source: MGI

   Molecular_functionzinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3UTJ2-1)

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.
Note: No experimental confirmation available.
Isoform 2 (identifier: Q3UTJ2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     211-211: P → PDEDTDMYNTPYTYNA
     308-308: P → PPPLPPTPTP...QDHSSGVSNE
Note: No experimental confirmation available. Contains a phosphoserine at position 353. Contains a phosphoserine at position 355.
Isoform 3 (identifier: Q3UTJ2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     4-34: Missing.
     211-211: P → PDEDTDMYNTPYTYNA
     388-914: Missing.
     1126-1180: FQALYNYTPRNEDELELRESDVVDVMEKCDDGWFVGTSRRTKFFGTFPGNYVKRL → LQ
Note: No experimental confirmation available.
Isoform 4 (identifier: Q3UTJ2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     4-34: Missing.
     388-914: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q3UTJ2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     45-67: Missing.
     211-211: P → PDEDTDMYNTPYTYNA
     308-308: P → PPPLPPTPTPVPREPSRKPLSVSPSTDGLRSPSPPPRSCVPAPCPSAPDLSPTRPPKKALDYVQDHSSGVSNE
     388-914: Missing.
     1126-1135: Missing.
Note: No experimental confirmation available. Contains a phosphoserine at position 322. Contains a phosphoserine at position 330. Contains a phosphoserine at position 332. Contains a phosphoserine at position 350.
Isoform 6 (identifier: Q3UTJ2-6)

The sequence of this isoform differs from the canonical sequence as follows:
     45-67: Missing.
     211-211: P → PDEDTDMYNTPYTYNA
     309-316: VSIYQSSI → RSVSSRPL
     317-1180: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q3UTJ2-7)

The sequence of this isoform differs from the canonical sequence as follows:
     311-313: IYQ → PCH
     314-1180: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11801180Sorbin and SH3 domain-containing protein 2
PRO_0000344478

Regions

Domain166 – 23065SoHo
Domain943 – 100260SH3 1
Domain1018 – 107962SH3 2
Domain1121 – 118060SH3 3
Compositional bias720 – 73112His-rich
Compositional bias1011 – 10144Poly-Pro

Amino acid modifications

Modified residue271Phosphoserine Ref.5 Ref.7
Modified residue401Phosphoserine Ref.6
Modified residue1301Phosphoserine Ref.6
Modified residue2391Phosphoserine Ref.8
Modified residue3391Phosphoserine Ref.8
Modified residue3571Phosphothreonine By similarity
Modified residue3581Phosphoserine Ref.6
Modified residue3781Phosphoserine Ref.6
Modified residue3791Phosphoserine Ref.6
Modified residue3811Phosphoserine By similarity
Modified residue3821Phosphoserine Ref.6
Modified residue4511Phosphothreonine Ref.5
Modified residue4561Phosphoserine Ref.5
Modified residue8291Phosphoserine Ref.4
Modified residue10971Phosphoserine Ref.6
Modified residue10981Phosphoserine Ref.6

Natural variations

Alternative sequence4 – 3431Missing in isoform 3 and isoform 4.
VSP_034800
Alternative sequence45 – 6723Missing in isoform 5 and isoform 6.
VSP_034801
Alternative sequence2111P → PDEDTDMYNTPYTYNA in isoform 2, isoform 3, isoform 5 and isoform 6.
VSP_034802
Alternative sequence3081P → PPPLPPTPTPVPREPSRKPL SVSPSTDGLRSPSPPPRSCV PAPRPSAPDLSPTRTGRINP ADIDLENEPWYKFFSELEFG HPPPKKALDYVQDHSSGVSN E in isoform 2.
VSP_034803
Alternative sequence3081P → PPPLPPTPTPVPREPSRKPL SVSPSTDGLRSPSPPPRSCV PAPCPSAPDLSPTRPPKKAL DYVQDHSSGVSNE in isoform 5.
VSP_034804
Alternative sequence309 – 3168VSIYQSSI → RSVSSRPL in isoform 6.
VSP_034805
Alternative sequence311 – 3133IYQ → PCH in isoform 7.
VSP_034806
Alternative sequence314 – 1180867Missing in isoform 7.
VSP_034807
Alternative sequence317 – 1180864Missing in isoform 6.
VSP_034808
Alternative sequence388 – 914527Missing in isoform 3, isoform 4 and isoform 5.
VSP_034809
Alternative sequence1126 – 118055FQALY…YVKRL → LQ in isoform 3.
VSP_034810
Alternative sequence1126 – 113510Missing in isoform 5.
VSP_034811

Experimental info

Sequence conflict2491V → A in AAH39163. Ref.2
Sequence conflict9441E → EV in BAE24407. Ref.1

Sequences

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

Last modified July 22, 2008. Version 2.
Checksum: 99ECA798E95A092E

FASTA1,180132,349
        10         20         30         40         50         60 
MNTDSGGCAR KRAAMSVTLT SVKRVQSSPN LLAAGRESQS PDSAWRSYND RNPETLNGDA 

        70         80         90        100        110        120 
TYSSLAAKGF RSVRPNLQDK RSPTQSQITI NGNSGGAVSP VSYYQRPFSP SAYSLPASLN 

       130        140        150        160        170        180 
SSIIMQHGRS LDSAETYSQH AQSLDGTMGS SIPLYRSSEE EKRVTVIKAP HYPGIGPVDE 

       190        200        210        220        230        240 
SGIPTAIRTT VDRPKDWYKT MFKQIHMVHK PGLYNSPYSA QSHPAAKTQT YRPLSKSHSD 

       250        260        270        280        290        300 
NGTDAFKEVP SPVPPPHVPP RPRDQSSTLK HDWDPPDRKV DTRKFRSEPR SIFEYEPGKS 

       310        320        330        340        350        360 
SILQHERPVS IYQSSIDRSL ERPSSSASMA GDFRKRRKSE PAVGPLRGLG DQSSSRTSPG 

       370        380        390        400        410        420 
RADLPGSSST FTKSFISSSP SSPSRAQGGD DSKMCPPLCS YSGLNGTPSG ELECCNAYRQ 

       430        440        450        460        470        480 
HLDVPGDSQR AITFKNGWQM ARQNAEIWSS TEETVSPKIK SRSCDDLLND DCDSFPDPKT 

       490        500        510        520        530        540 
KSESMGSLLC EEDSKESCPM TWASPYIQEV CGNSRSRLKH RSAHNAPGFL KMYKKMHRIN 

       550        560        570        580        590        600 
RKDLMNSEVI CSVKSRILQY EKEQQHRGLL HGWSQSSTEE VPRDVVPTRI SEFEKLIQKS 

       610        620        630        640        650        660 
KSMPNLGDEM LSPITLEPPQ NGLCPKRRFS IESLLEEETQ VRHPSQGQRS CKSNTLVPIH 

       670        680        690        700        710        720 
IEVTSDEQPR THMEFSDSDQ DGVVSDHSDY VHVEGSSFCS ESDFDHFSFT SSESFYGSSH 

       730        740        750        760        770        780 
HHHHHHHHHR HLISSCKGRC PASYTRFTTM LKHERAKHEN MDRPRRQEMD PGLSKLAFLV 

       790        800        810        820        830        840 
SPVPFRRKKI LTPQKQTEKA KCKASVVEAL DSALKDICDQ IKAEKRRGSL PDNSILHRLI 

       850        860        870        880        890        900 
SELLPQIPER NSSLHALKRS PMHQPFHPLP PDGASHCPLY QNDCGRMPHS ASFPDVDTTS 

       910        920        930        940        950        960 
NYHAQDYGSA LSLQDHESPR SYSSTLTDLG RSASRERRGT PEKEKLPAKA VYDFKAQTSK 

       970        980        990       1000       1010       1020 
ELSFKKGDTV YILRKIDQNW YEGEHHGRVG IFPISYVEKL TPPEKAQPAR PPPPVQPGEI 

      1030       1040       1050       1060       1070       1080 
GEAIAKYNFN ADTNVELSLR KGDRIILLKR VDQNWYEGKI PGTNRQGIFP VSYVEVVKRN 

      1090       1100       1110       1120       1130       1140 
AKGAEDYPDP PLPHSYSSDR IYTLSSNKPQ RPGFSHENIQ GGGEPFQALY NYTPRNEDEL 

      1150       1160       1170       1180 
ELRESDVVDV MEKCDDGWFV GTSRRTKFFG TFPGNYVKRL

« Hide

Isoform 2 [UniParc].

Checksum: 05E03BF51F0D0FE4
Show »

FASTA1,295145,012
Isoform 3 [UniParc].

Checksum: 2E93E14021A5F1AE
Show »

FASTA58464,990
Isoform 4 [UniParc].

Checksum: 63298ED47475B3F1
Show »

FASTA62269,477
Isoform 5 [UniParc].

Checksum: 726FB101E2D1A269
Show »

FASTA70778,102
Isoform 6 [UniParc].

Checksum: EFC3C49B080C2BDB
Show »

FASTA30834,144
Isoform 7 [UniParc].

Checksum: 403BEF28C731B333
Show »

FASTA31334,573

References

[1]"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 3; 4 AND 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-532 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 229-313 (ISOFORM 7), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1097-1180 (ISOFORM 5).
Strain: C57BL/6J.
Tissue: Aorta, Brain cortex, Cerebellum, Embryoid bodies and Vein.
[2]"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 5).
Strain: Czech II.
Tissue: Mammary tumor.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-1180 (ISOFORM 2).
Tissue: Brain.
[4]"Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, MASS SPECTROMETRY.
Tissue: Brain.
[5]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-451 AND SER-456.
Tissue: Brain cortex.
[6]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-130; SER-358; SER-378; SER-379; SER-382; SER-1097 AND SER-1098, MASS SPECTROMETRY.
Tissue: Liver.
[7]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, MASS SPECTROMETRY.
Tissue: Liver.
[8]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-339, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK041051 mRNA. Translation: BAC30799.1.
AK049030 mRNA. Translation: BAC33518.1.
AK079130 mRNA. Translation: BAC37554.1.
AK083429 mRNA. Translation: BAC38913.1.
AK139388 mRNA. Translation: BAE23988.1.
AK140498 mRNA. Translation: BAE24407.1.
BC039163 mRNA. Translation: AAH39163.1.
AK122369 mRNA. Translation: BAC65651.1.
IPIIPI00405462.
IPI00673886.
IPI00900398.
IPI00900438.
IPI00900461.
IPI00900464.
IPI00923680.
UniGeneMm.211096.
Mm.441720.
Mm.447653.

3D structure databases

ProteinModelPortalQ3UTJ2.
SMRQ3UTJ2. Positions 927-1180.
ModBaseSearch...

Proteomic databases

PaxDbQ3UTJ2.
PRIDEQ3UTJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000125295; ENSMUSP00000116768; ENSMUSG00000031626.
ENSMUST00000134675; ENSMUSP00000118160; ENSMUSG00000031626.
ENSMUST00000138049; ENSMUSP00000123503; ENSMUSG00000031626.
ENSMUST00000139869; ENSMUSP00000121235; ENSMUSG00000031626.
ENSMUST00000141039; ENSMUSP00000117544; ENSMUSG00000031626.
ENSMUST00000153798; ENSMUSP00000118353; ENSMUSG00000031626.
UCSCuc009lpb.1. mouse.
uc009lpc.1. mouse.
uc009lpd.1. mouse.
uc009lpf.1. mouse.
uc009lpi.1. mouse.

Organism-specific databases

MGIMGI:1924574. Sorbs2.
RougeSearch...

Phylogenomic databases

eggNOGNOG256936.
GeneTreeENSGT00690000102104.
HOVERGENHBG108509.

Gene expression databases

ArrayExpressQ3UTJ2.
BgeeQ3UTJ2.
GenevestigatorQ3UTJ2.

Family and domain databases

InterProIPR000108. p67phox.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR003127. Sorb.
IPR007087. Znf_C2H2.
[Graphical view]
PfamPF00018. SH3_1. 2 hits.
PF07653. SH3_2. 1 hit.
PF02208. Sorb. 1 hit.
[Graphical view]
PRINTSPR00499. P67PHOX.
PR00452. SH3DOMAIN.
SMARTSM00326. SH3. 3 hits.
SM00459. Sorb. 1 hit.
[Graphical view]
SUPFAMSSF50044. SH3. 3 hits.
PROSITEPS50002. SH3. 3 hits.
PS50831. SOHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio13857343.
SOURCESearch...

Entry information

Entry nameSRBS2_MOUSE
AccessionPrimary (citable) accession number: Q3UTJ2
Secondary accession number(s): Q3USC6 expand/collapse secondary AC list , Q80TS1, Q8BJL6, Q8BJU3, Q8BLW9, Q8BX47, Q8CHU0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: May 1, 2013
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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