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Q8R550 (SH3K1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. 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:
SH3 domain-containing kinase-binding protein 1
Alternative name(s):
Regulator of ubiquitous kinase
Short name=Ruk
SH3-containing, expressed in tumorigenic astrocytes
Gene names
Name:Sh3kbp1
Synonyms:Ruk, Seta
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length709 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein involved in regulating diverse signal transduction pathways. Involved in the regulation of endocytosis and lysosomal degradation of ligand-induced receptor tyrosine kinases, including EGFR and MET/hepatocyte growth factor receptor, through a association with CBL and endophilins. The association with CBL, and thus the receptor internalization, may inhibited by an interaction with PDCD6IP and/or SPRY2. Involved in regulation of ligand-dependent endocytosis of the IgE receptor. Attenuates phosphatidylinositol 3-kinase activity by interaction with its regulatory subunit. May be involved in regulation of cell adhesion; promotes the interaction between TTK2B and PDCD6IP. May be involved in the regulation of cellular stress response via the MAPK pathways through its interaction with MAP3K4. Is involved in modulation of tumor necrosis factor mediated apoptosis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration By similarity.

Subunit structure

Can self-associate and form homotetramers. Interacts with CD2, F-actin capping protein, PIK3R3, GRB2, EGFR, MET, BLNK, MAP3K4, PDCD6IP, SPRY2, ARHGAP17, ARHGAP27, CRK, BCAR1, SOS1, ASAP1, ARAP3, HIP1R, SYNJ2, INPP5D and STAP1. Interacts with CBL and CBLB, but does not interact with CBLC. Two molecules of SH3KBP1 seem to bind through their respective SH3 1 domain to one molecule of CBLB. The interaction with CBL or CBLB and EGFR is increased upon EGF stimulation. The interaction with CBL is attenuated by PDCD6IP. Interacts through its proline-rich region with the SH3 domain of endophilins SH3GL1, SH3GL2 and SH3GL3. The SH3KBP1-endophilin complex seems to associate with a complex containing the phosphorylated receptor (EGFR or MET) and phosphorylated CBL. Probably associates with ASAP1 and phosphorylated EGFR. Probably part of a complex consisting of at least SH3KBP1, ASAP1 and ARAP3. Interacts with focal adhesion kinases PTK2/FAK1 AND PTK2B/PYK2, probably as a dimer. Interacts with DAB2 and probably associates with chathrin through its interaction with DAB2. Part of a complex consisting of SH3KBP1, DAB2, and clathrin heavy chain. DAB2 and clathrin dissociate from SH3KBP1 following growth factor treatment, enabling interaction with CBL. Interacts with DDN and probably associates with MAGI2 through its interaction with DDN. Interacts with the SH3 domains of SRC tyrosine-protein kinases SRC, LCK, LYN, FGR, FYN and HCK. Interacts with TRADD, BIRC2, TRAF1, TRAF2 and TNFR1, and the association with a TNFR1-associated complex upon stimulation with TNF-alpha seems to be mediated by SRC. Probably part of a complex consisting of at least SH3KBP1, ASAP1 and ARAP3 By similarity. Interacts with SHKBP1. Interacts with ATX2. Ref.6 Ref.8

Subcellular location

Cytoplasmcytoskeleton By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein By similarity. Cell junctionsynapsesynaptosome By similarity. Cell junctionfocal adhesion By similarity. Note: Localized in endocytic vesicles containing clustered receptors. Colocalizes with ASAP1 in vesicular structures. Colocalized with actin microfilaments and focal adhesions By similarity. Colocalized with MAGI2 in synaptosomes By similarity.

Domain

The SH3 domains mediate interaction with SHKBP1.

Post-translational modification

Monoubiquitinated by CBL and CBLB after EGF stimulation; probably on its C-terminus By similarity.

Sequence similarities

Contains 3 SH3 domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dlg4Q621083EBI-642709,EBI-300895

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8R550-1)

Also known as: Ruk-xl;

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: Q8R550-2)

Also known as: Ruk-l;

The sequence of this isoform differs from the canonical sequence as follows:
     174-217: Missing.
Isoform 3 (identifier: Q8R550-3)

Also known as: Ruk-deltaA;

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: MVEAIVEFDYQAQHDDELTISVGEVITNIRKEDGGWWEGQINGRRGLFPDNFVR → MELSAAKAPSPTDLPES
     174-217: Missing.
Isoform 4 (identifier: Q8R550-4)

Also known as: Ruk-m1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-286: MVEAIVEFDY...VENDFLPVEK → MGEEVSLGEK...FGVFLVNEET
Isoform 5 (identifier: Q8R550-5)

Also known as: Ruk-m3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-286: MVEAIVEFDY...VENDFLPVEK → MGEE
Isoform 6 (identifier: Q8R550-6)

Also known as: Ruk-t;

The sequence of this isoform differs from the canonical sequence as follows:
     1-477: MVEAIVEFDY...RPVGPLTHTR → MFPFRKGARPPSMNLFRQTCW
Isoform 7 (identifier: Q8R550-7)

Also known as: Ruk-h;

The sequence of this isoform differs from the canonical sequence as follows:
     1-599: Missing.
Isoform 8 (identifier: Q8R550-8)

Also known as: Ruk-deltaCP;

The sequence of this isoform differs from the canonical sequence as follows:
     174-217: Missing.
     320-630: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 709709SH3 domain-containing kinase-binding protein 1
PRO_0000097729

Regions

Domain1 – 5858SH3 1
Domain98 – 15760SH3 2
Domain311 – 37262SH3 3
Coiled coil646 – 70863 Potential

Amino acid modifications

Modified residue2741Phosphoserine Ref.7 Ref.9
Modified residue2981Phosphothreonine By similarity
Modified residue4801Phosphoserine By similarity
Modified residue5531Phosphoserine By similarity
Modified residue5551Phosphoserine By similarity
Modified residue5651Phosphoserine By similarity
Modified residue6311Phosphoserine By similarity

Natural variations

Alternative sequence1 – 599599Missing in isoform 7.
VSP_007509
Alternative sequence1 – 477477MVEAI…LTHTR → MFPFRKGARPPSMNLFRQTC W in isoform 6.
VSP_007508
Alternative sequence1 – 286286MVEAI…LPVEK → MGEEVSLGEKNISPEQASCG ALHPRGWGSQTFGVFLVNEE T in isoform 4.
VSP_007507
Alternative sequence1 – 286286MVEAI…LPVEK → MGEE in isoform 5.
VSP_007506
Alternative sequence1 – 5454MVEAI…DNFVR → MELSAAKAPSPTDLPES in isoform 3.
VSP_007505
Alternative sequence174 – 21744Missing in isoform 2, isoform 3 and isoform 8.
VSP_007510
Alternative sequence320 – 630311Missing in isoform 8.
VSP_007511

Experimental info

Sequence conflict251 – 2599PKKVKGVGF → NDDELTIKE Ref.5
Sequence conflict478 – 52851GDSPK…TTSRP → YCHVLTKAGGHGMIMKIGEG MRTKLCLKIPATFFSSEKVV ARCWGATWCRL in BAC30033. Ref.2
Sequence conflict529 – 709181Missing in BAC30033. Ref.2

Secondary structure

..................... 709
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2002. Version 1.
Checksum: AC2DDFB3248A458B

FASTA70978,170
        10         20         30         40         50         60 
MVEAIVEFDY QAQHDDELTI SVGEVITNIR KEDGGWWEGQ INGRRGLFPD NFVREIKKDM 

        70         80         90        100        110        120 
KKDLLSNKAP EKPMHDVSSG NALLSSETIL RTNKRGERRR RRCQVAFSYL PQNDDELELK 

       130        140        150        160        170        180 
VGDIIEVVGE VEEGWWEGVL NGKTGMFPSN FIKELSGESD ELGISQDEQL SKSRPEGFLP 

       190        200        210        220        230        240 
ASLLPFPAHG AKGKTTFEGT ILYRAAPGKT EGHRRYYSLR ETTGSESDGG DSSSTKSEGA 

       250        260        270        280        290        300 
NGTMATAAIQ PKKVKGVGFG DIFKDKPIKL RPRSIEVEND FLPVEKTIGK KLPPATSTPD 

       310        320        330        340        350        360 
PSKTEMDSRT KTKDYCKVIF PYEAQNDDEL TIKEGDIVTL INKDCIDVGW WEGELNGRRG 

       370        380        390        400        410        420 
VFPDNFVKLL PSDFDKEGNR PKKPPPPSAP VVKQGAGTTE RKHEIKKIPP ERPETLPNRT 

       430        440        450        460        470        480 
EEKERPEREP KLDLQKPSVP AIPPKKPRPP KTNSLNRPGA LPPRRPERPV GPLTHTRGDS 

       490        500        510        520        530        540 
PKIDLAGSAL SGILDKDLSD RSNDIDLEGF DSVISSTEKL SHPTTSRPKA TGRRPPSQSL 

       550        560        570        580        590        600 
TSSSLSSPDI FDSPSPEEDK EEHISLAHRG IDVSKKTSKT VTISQVSDNK TSLPPKPGTM 

       610        620        630        640        650        660 
AAASSGPASL SSVASSPMSS SLGTAGQRAS SPSLFSTEGK PKMEPAVSSQ AAIEELKMQV 

       670        680        690        700 
RELRTIIETM KDQQKREIKQ LLSELDEEKK IRLRLQMEVN DIKKALQSK 

« Hide

Isoform 2 (Ruk-l) [UniParc].

Checksum: 724607807A66B043
Show »

FASTA66573,328
Isoform 3 (Ruk-deltaA) [UniParc].

Checksum: 1C4AEC6BE48D5D17
Show »

FASTA62868,820
Isoform 4 (Ruk-m1) [UniParc].

Checksum: 54F018C499D51044
Show »

FASTA46450,755
Isoform 5 (Ruk-m3) [UniParc].

Checksum: 460A56431A4FDDCD
Show »

FASTA42746,827
Isoform 6 (Ruk-t) [UniParc].

Checksum: D1B221FDDE4C72C7
Show »

FASTA25327,442
Isoform 7 (Ruk-h) [UniParc].

Checksum: 6536493B3B3761DE
Show »

FASTA11011,992
Isoform 8 (Ruk-deltaCP) [UniParc].

Checksum: B580135B37F9B571
Show »

FASTA35439,765

References

« Hide 'large scale' references
[1]"Organization of the mouse Ruk locus and expression of isoforms in mouse tissues."
Buchman V.L., Luke C., Borthwick E.B., Gout I., Ninkina N.
Gene 295:13-17(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7).
Strain: 129/Ola.
[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; 2 AND 3).
Strain: C57BL/6J.
Tissue: Embryonic stem cell, Hypothalamus, Lung and Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Assignment of SETA to distal mouse X chromosome by radiation hybrid mapping."
Hyatt M.A., Sykes V.W., Boyer A.D., Arden K.C., Boegler O.
Cytogenet. Cell Genet. 89:278-278(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 247-286.
Strain: 129/SvJ.
[5]"The WashU-NCI mouse EST project 1999."
Marra M., Hillier L., Kucaba T., Martin J., Beck C., Wylie T., Underwood K., Steptoe M., Theising B., Allen M., Bowers Y., Person B., Swaller T., Gibbons M., Pape D., Harvey N., Schurk R., Ritter E. expand/collapse author list , Kohn S., Shin T., Jackson Y., Cardenas M., McCann R., Waterston R., Wilson R.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 250-709 (ISOFORM 8).
Strain: C57BL/6J.
Tissue: Thymus.
[6]"SETA is a multifunctional adapter protein with three SH3 domains that binds Grb2, Cbl, and the novel SB1 proteins."
Borinstein S.C., Hyatt M.A., Sykes V.W., Straub R.E., Lipkowitz S., Boulter J., Boegler O.
Cell. Signal. 12:769-779(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHKBP1.
[7]"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-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"Ataxin-2 associates with the endocytosis complex and affects EGF receptor trafficking."
Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J., Auburger G.
Cell. Signal. 20:1725-1739(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATX2.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Solution structure of the SH3 domains of SH3-domain kinase binding protein 1."
RIKEN structural genomics initiative (RSGI)
Submitted (JUN-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 101-159 AND 314-370.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF472327 expand/collapse EMBL AC list , AF472306, AF472307, AF472308, AF472309, AF472312, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82456.1.
AF472327, AF472325, AF472326 Genomic DNA. Translation: AAL82457.1.
AF472327 expand/collapse EMBL AC list , AF472304, AF472305, AF472307, AF472308, AF472309, AF472312, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82458.1.
AF472327 expand/collapse EMBL AC list , AF472313, AF472314, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82459.1.
AF472327 expand/collapse EMBL AC list , AF472313, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82460.1.
AF472327 expand/collapse EMBL AC list , AF472321, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82461.1.
AF472327 expand/collapse EMBL AC list , AF472304, AF472305, AF472307, AF472308, AF472309, AF472310, AF472311, AF472312, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82462.1.
AK004636 mRNA. Translation: BAB23427.2.
AK020782 mRNA. Translation: BAB32209.2.
AK038540 mRNA. Translation: BAC30033.1.
AK049182 mRNA. Translation: BAC33592.1.
AL929452 Genomic DNA. Translation: CAM21669.1.
AL929452 Genomic DNA. Translation: CAM21670.1.
AF243508 Genomic DNA. Translation: AAF68439.1.
AI428677 mRNA. No translation available.
CCDSCCDS41194.1. [Q8R550-3]
CCDS53234.1. [Q8R550-2]
CCDS53235.1. [Q8R550-5]
RefSeqNP_001129199.1. NM_001135727.2. [Q8R550-2]
NP_001129200.1. NM_001135728.2. [Q8R550-5]
NP_001277590.1. NM_001290661.1. [Q8R550-7]
NP_001277593.1. NM_001290664.1. [Q8R550-7]
NP_067364.2. NM_021389.6. [Q8R550-3]
XP_006528987.1. XM_006528924.1. [Q8R550-1]
UniGeneMm.286495.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WI7NMR-A101-155[»]
2DA9NMR-A314-370[»]
ProteinModelPortalQ8R550.
SMRQ8R550. Positions 2-166, 314-389.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid208383. 6 interactions.
IntActQ8R550. 9 interactions.
MINTMINT-1591643.

PTM databases

PhosphoSiteQ8R550.

Proteomic databases

MaxQBQ8R550.
PaxDbQ8R550.
PRIDEQ8R550.

Protocols and materials databases

DNASU58194.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000073094; ENSMUSP00000072840; ENSMUSG00000040990. [Q8R550-1]
ENSMUST00000080394; ENSMUSP00000079257; ENSMUSG00000040990. [Q8R550-3]
ENSMUST00000112451; ENSMUSP00000108070; ENSMUSG00000040990. [Q8R550-5]
ENSMUST00000112453; ENSMUSP00000108072; ENSMUSG00000040990. [Q8R550-4]
ENSMUST00000112456; ENSMUSP00000108075; ENSMUSG00000040990. [Q8R550-2]
GeneID58194.
KEGGmmu:58194.
UCSCuc009uss.2. mouse. [Q8R550-1]
uc009usx.2. mouse. [Q8R550-5]

Organism-specific databases

CTD30011.
MGIMGI:1889583. Sh3kbp1.

Phylogenomic databases

eggNOGNOG319250.
GeneTreeENSGT00530000063594.
HOVERGENHBG057824.
InParanoidQ8R550.
KOK12470.
OMAMDSRTKT.
OrthoDBEOG7W41BC.
PhylomeDBQ8R550.
TreeFamTF350191.

Gene expression databases

ArrayExpressQ8R550.
BgeeQ8R550.
CleanExMM_SH3KBP1.
GenevestigatorQ8R550.

Family and domain databases

InterProIPR001452. SH3_domain.
[Graphical view]
PfamPF14604. SH3_9. 3 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
SMARTSM00326. SH3. 3 hits.
[Graphical view]
SUPFAMSSF50044. SSF50044. 3 hits.
PROSITEPS50002. SH3. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSH3KBP1. mouse.
EvolutionaryTraceQ8R550.
NextBio314169.
PROQ8R550.
SOURCESearch...

Entry information

Entry nameSH3K1_MOUSE
AccessionPrimary (citable) accession number: Q8R550
Secondary accession number(s): B1AZ86 expand/collapse secondary AC list , B1AZ87, Q8CAL8, Q8CEF6, Q8R545, Q8R546, Q8R547, Q8R548, Q8R549, Q8R551, Q9CTQ9, Q9DC14, Q9JKC3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 118 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