SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8R550

- SH3K1_MOUSE

UniProt

Q8R550 - SH3K1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

SH3 domain-containing kinase-binding protein 1

Gene
Sh3kbp1, Ruk, Seta
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cell migration Source: UniProtKB
  3. cytoskeleton organization Source: UniProtKB
  4. endocytosis Source: UniProtKB-KW
  5. regulation of cell shape Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Endocytosis

Enzyme and pathway databases

ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_203917. EGFR downregulation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Sh3kbp1
Synonyms:Ruk, Seta
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1889583. Sh3kbp1.

Subcellular locationi

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.

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  3. cytoskeleton Source: UniProtKB-SubCell
  4. focal adhesion Source: UniProtKB-SubCell
  5. neuron projection Source: UniProtKB-SubCell
  6. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Synapse, Synaptosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 709709SH3 domain-containing kinase-binding protein 1PRO_0000097729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei274 – 2741Phosphoserine2 Publications
Modified residuei298 – 2981Phosphothreonine By similarity
Modified residuei480 – 4801Phosphoserine By similarity
Modified residuei553 – 5531Phosphoserine By similarity
Modified residuei555 – 5551Phosphoserine By similarity
Modified residuei565 – 5651Phosphoserine By similarity
Modified residuei631 – 6311Phosphoserine By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ8R550.
PaxDbiQ8R550.
PRIDEiQ8R550.

PTM databases

PhosphoSiteiQ8R550.

Expressioni

Gene expression databases

ArrayExpressiQ8R550.
BgeeiQ8R550.
CleanExiMM_SH3KBP1.
GenevestigatoriQ8R550.

Interactioni

Subunit structurei

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 ATX2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Dlg4Q621083EBI-642709,EBI-300895

Protein-protein interaction databases

BioGridi208383. 6 interactions.
IntActiQ8R550. 9 interactions.
MINTiMINT-1591643.

Structurei

Secondary structure

1
709
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi103 – 1075
Beta strandi129 – 1324
Beta strandi135 – 1384
Beta strandi145 – 1484
Beta strandi151 – 1544
Beta strandi314 – 3185
Beta strandi336 – 3427
Beta strandi350 – 3545
Beta strandi359 – 3635
Helixi364 – 3663
Beta strandi367 – 3693

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WI7NMR-A101-155[»]
2DA9NMR-A314-370[»]
ProteinModelPortaliQ8R550.
SMRiQ8R550. Positions 2-166, 314-389.

Miscellaneous databases

EvolutionaryTraceiQ8R550.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5858SH3 1Add
BLAST
Domaini98 – 15760SH3 2Add
BLAST
Domaini311 – 37262SH3 3Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili646 – 70863 Reviewed predictionAdd
BLAST

Domaini

The SH3 domains mediate interaction with SHKBP1.

Sequence similaritiesi

Contains 3 SH3 domains.

Keywords - Domaini

Coiled coil, Repeat, SH3 domain, SH3-binding

Phylogenomic databases

eggNOGiNOG319250.
GeneTreeiENSGT00530000063594.
HOVERGENiHBG057824.
InParanoidiQ8R550.
KOiK12470.
OMAiMDSRTKT.
OrthoDBiEOG7W41BC.
PhylomeDBiQ8R550.
TreeFamiTF350191.

Family and domain databases

InterProiIPR001452. SH3_domain.
[Graphical view]
PfamiPF14604. SH3_9. 3 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00326. SH3. 3 hits.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 3 hits.
PROSITEiPS50002. SH3. 3 hits.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8R550-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MVEAIVEFDY QAQHDDELTI SVGEVITNIR KEDGGWWEGQ INGRRGLFPD    50
NFVREIKKDM KKDLLSNKAP EKPMHDVSSG NALLSSETIL RTNKRGERRR 100
RRCQVAFSYL PQNDDELELK VGDIIEVVGE VEEGWWEGVL NGKTGMFPSN 150
FIKELSGESD ELGISQDEQL SKSRPEGFLP ASLLPFPAHG AKGKTTFEGT 200
ILYRAAPGKT EGHRRYYSLR ETTGSESDGG DSSSTKSEGA NGTMATAAIQ 250
PKKVKGVGFG DIFKDKPIKL RPRSIEVEND FLPVEKTIGK KLPPATSTPD 300
PSKTEMDSRT KTKDYCKVIF PYEAQNDDEL TIKEGDIVTL INKDCIDVGW 350
WEGELNGRRG VFPDNFVKLL PSDFDKEGNR PKKPPPPSAP VVKQGAGTTE 400
RKHEIKKIPP ERPETLPNRT EEKERPEREP KLDLQKPSVP AIPPKKPRPP 450
KTNSLNRPGA LPPRRPERPV GPLTHTRGDS PKIDLAGSAL SGILDKDLSD 500
RSNDIDLEGF DSVISSTEKL SHPTTSRPKA TGRRPPSQSL TSSSLSSPDI 550
FDSPSPEEDK EEHISLAHRG IDVSKKTSKT VTISQVSDNK TSLPPKPGTM 600
AAASSGPASL SSVASSPMSS SLGTAGQRAS SPSLFSTEGK PKMEPAVSSQ 650
AAIEELKMQV RELRTIIETM KDQQKREIKQ LLSELDEEKK IRLRLQMEVN 700
DIKKALQSK 709
Length:709
Mass (Da):78,170
Last modified:June 1, 2002 - v1
Checksum:iAC2DDFB3248A458B
GO
Isoform 2 (identifier: Q8R550-2) [UniParc]FASTAAdd to Basket

Also known as: Ruk-l

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

Show »
Length:665
Mass (Da):73,328
Checksum:i724607807A66B043
GO
Isoform 3 (identifier: Q8R550-3) [UniParc]FASTAAdd to Basket

Also known as: Ruk-deltaA

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: MVEAIVEFDYQAQHDDELTISVGEVITNIRKEDGGWWEGQINGRRGLFPDNFVR → MELSAAKAPSPTDLPES
     174-217: Missing.

Show »
Length:628
Mass (Da):68,820
Checksum:i1C4AEC6BE48D5D17
GO
Isoform 4 (identifier: Q8R550-4) [UniParc]FASTAAdd to Basket

Also known as: Ruk-m1

The sequence of this isoform differs from the canonical sequence as follows:
     1-286: MVEAIVEFDY...VENDFLPVEK → MGEEVSLGEK...FGVFLVNEET

Show »
Length:464
Mass (Da):50,755
Checksum:i54F018C499D51044
GO
Isoform 5 (identifier: Q8R550-5) [UniParc]FASTAAdd to Basket

Also known as: Ruk-m3

The sequence of this isoform differs from the canonical sequence as follows:
     1-286: MVEAIVEFDY...VENDFLPVEK → MGEE

Show »
Length:427
Mass (Da):46,827
Checksum:i460A56431A4FDDCD
GO
Isoform 6 (identifier: Q8R550-6) [UniParc]FASTAAdd to Basket

Also known as: Ruk-t

The sequence of this isoform differs from the canonical sequence as follows:
     1-477: MVEAIVEFDY...RPVGPLTHTR → MFPFRKGARPPSMNLFRQTCW

Show »
Length:253
Mass (Da):27,442
Checksum:iD1B221FDDE4C72C7
GO
Isoform 7 (identifier: Q8R550-7) [UniParc]FASTAAdd to Basket

Also known as: Ruk-h

The sequence of this isoform differs from the canonical sequence as follows:
     1-599: Missing.

Show »
Length:110
Mass (Da):11,992
Checksum:i6536493B3B3761DE
GO
Isoform 8 (identifier: Q8R550-8) [UniParc]FASTAAdd to Basket

Also known as: Ruk-deltaCP

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

Show »
Length:354
Mass (Da):39,765
Checksum:iB580135B37F9B571
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 599599Missing in isoform 7. VSP_007509Add
BLAST
Alternative sequencei1 – 477477MVEAI…LTHTR → MFPFRKGARPPSMNLFRQTC W in isoform 6. VSP_007508Add
BLAST
Alternative sequencei1 – 286286MVEAI…LPVEK → MGEEVSLGEKNISPEQASCG ALHPRGWGSQTFGVFLVNEE T in isoform 4. VSP_007507Add
BLAST
Alternative sequencei1 – 286286MVEAI…LPVEK → MGEE in isoform 5. VSP_007506Add
BLAST
Alternative sequencei1 – 5454MVEAI…DNFVR → MELSAAKAPSPTDLPES in isoform 3. VSP_007505Add
BLAST
Alternative sequencei174 – 21744Missing in isoform 2, isoform 3 and isoform 8. VSP_007510Add
BLAST
Alternative sequencei320 – 630311Missing in isoform 8. VSP_007511Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti251 – 2599PKKVKGVGF → NDDELTIKE1 Publication
Sequence conflicti478 – 52851GDSPK…TTSRP → YCHVLTKAGGHGMIMKIGEG MRTKLCLKIPATFFSSEKVV ARCWGATWCRL in BAC30033. 1 PublicationAdd
BLAST
Sequence conflicti529 – 709181Missing in BAC30033. 1 PublicationAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF472327
, 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
, AF472304, AF472305, AF472307, AF472308, AF472309, AF472312, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82458.1.
AF472327
, AF472313, AF472314, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82459.1.
AF472327
, AF472313, AF472315, AF472316, AF472317, AF472318, AF472319, AF472320, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82460.1.
AF472327
, AF472321, AF472322, AF472323, AF472324, AF472325, AF472326 Genomic DNA. Translation: AAL82461.1.
AF472327
, 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.
CCDSiCCDS41194.1. [Q8R550-3]
CCDS53234.1. [Q8R550-2]
CCDS53235.1. [Q8R550-5]
RefSeqiNP_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]
UniGeneiMm.286495.

Genome annotation databases

EnsembliENSMUST00000073094; ENSMUSP00000072840; ENSMUSG00000040990. [Q8R550-1]
ENSMUST00000080394; ENSMUSP00000079257; ENSMUSG00000040990. [Q8R550-3]
ENSMUST00000112451; ENSMUSP00000108070; ENSMUSG00000040990. [Q8R550-5]
ENSMUST00000112453; ENSMUSP00000108072; ENSMUSG00000040990. [Q8R550-4]
ENSMUST00000112456; ENSMUSP00000108075; ENSMUSG00000040990. [Q8R550-2]
GeneIDi58194.
KEGGimmu:58194.
UCSCiuc009uss.2. mouse. [Q8R550-1]
uc009usx.2. mouse. [Q8R550-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF472327
, 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
, AF472304 , AF472305 , AF472307 , AF472308 , AF472309 , AF472312 , AF472315 , AF472316 , AF472317 , AF472318 , AF472319 , AF472320 , AF472322 , AF472323 , AF472324 , AF472325 , AF472326 Genomic DNA. Translation: AAL82458.1 .
AF472327
, AF472313 , AF472314 , AF472315 , AF472316 , AF472317 , AF472318 , AF472319 , AF472320 , AF472322 , AF472323 , AF472324 , AF472325 , AF472326 Genomic DNA. Translation: AAL82459.1 .
AF472327
, AF472313 , AF472315 , AF472316 , AF472317 , AF472318 , AF472319 , AF472320 , AF472322 , AF472323 , AF472324 , AF472325 , AF472326 Genomic DNA. Translation: AAL82460.1 .
AF472327
, AF472321 , AF472322 , AF472323 , AF472324 , AF472325 , AF472326 Genomic DNA. Translation: AAL82461.1 .
AF472327
, 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.
CCDSi CCDS41194.1. [Q8R550-3 ]
CCDS53234.1. [Q8R550-2 ]
CCDS53235.1. [Q8R550-5 ]
RefSeqi NP_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 ]
UniGenei Mm.286495.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WI7 NMR - A 101-155 [» ]
2DA9 NMR - A 314-370 [» ]
ProteinModelPortali Q8R550.
SMRi Q8R550. Positions 2-166, 314-389.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208383. 6 interactions.
IntActi Q8R550. 9 interactions.
MINTi MINT-1591643.

PTM databases

PhosphoSitei Q8R550.

Proteomic databases

MaxQBi Q8R550.
PaxDbi Q8R550.
PRIDEi Q8R550.

Protocols and materials databases

DNASUi 58194.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000073094 ; ENSMUSP00000072840 ; ENSMUSG00000040990 . [Q8R550-1 ]
ENSMUST00000080394 ; ENSMUSP00000079257 ; ENSMUSG00000040990 . [Q8R550-3 ]
ENSMUST00000112451 ; ENSMUSP00000108070 ; ENSMUSG00000040990 . [Q8R550-5 ]
ENSMUST00000112453 ; ENSMUSP00000108072 ; ENSMUSG00000040990 . [Q8R550-4 ]
ENSMUST00000112456 ; ENSMUSP00000108075 ; ENSMUSG00000040990 . [Q8R550-2 ]
GeneIDi 58194.
KEGGi mmu:58194.
UCSCi uc009uss.2. mouse. [Q8R550-1 ]
uc009usx.2. mouse. [Q8R550-5 ]

Organism-specific databases

CTDi 30011.
MGIi MGI:1889583. Sh3kbp1.

Phylogenomic databases

eggNOGi NOG319250.
GeneTreei ENSGT00530000063594.
HOVERGENi HBG057824.
InParanoidi Q8R550.
KOi K12470.
OMAi MDSRTKT.
OrthoDBi EOG7W41BC.
PhylomeDBi Q8R550.
TreeFami TF350191.

Enzyme and pathway databases

Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_203917. EGFR downregulation.

Miscellaneous databases

ChiTaRSi SH3KBP1. mouse.
EvolutionaryTracei Q8R550.
NextBioi 314169.
PROi Q8R550.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8R550.
Bgeei Q8R550.
CleanExi MM_SH3KBP1.
Genevestigatori Q8R550.

Family and domain databases

InterProi IPR001452. SH3_domain.
[Graphical view ]
Pfami PF14604. SH3_9. 3 hits.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi SM00326. SH3. 3 hits.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 3 hits.
PROSITEi PS50002. SH3. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiSH3K1_MOUSE
AccessioniPrimary (citable) accession number: Q8R550
Secondary accession number(s): B1AZ86
, B1AZ87, Q8CAL8, Q8CEF6, Q8R545, Q8R546, Q8R547, Q8R548, Q8R549, Q8R551, Q9CTQ9, Q9DC14, Q9JKC3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: June 1, 2002
Last modified: September 3, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi