Q8R550 (SH3K1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Sh3kbp1
Synonyms:	Ruk, Seta

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	709 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein By similarity. Cell junction › synapse › synaptosome By similarity. Cell junction › focal 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.

Ontologies

Keywords
Biological process	Apoptosis Endocytosis
Cellular component	Cell junction Cytoplasm Cytoplasmic vesicle Cytoskeleton Membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat SH3 domain SH3-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cell migration Inferred from sequence or structural similarity. Source: UniProtKB cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB endocytosis Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cell-cell junction Inferred from direct assay PubMed 23793062. Source: MGI cytoplasmic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from electronic annotation. Source: UniProtKB-SubCell neuron projection Inferred from electronic annotation. Source: UniProtKB-SubCell synapse Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	protein binding Inferred from physical interaction PubMed 20551902. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dlg4	Q62108	3	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 709

709

SH3 domain-containing kinase-binding protein 1

PRO_0000097729

Regions

Domain

1 – 58

58

SH3 1

Domain

98 – 157

60

SH3 2

Domain

311 – 372

62

SH3 3

Coiled coil

646 – 708

63

Potential

Amino acid modifications

Modified residue

274

1

Phosphoserine Ref.7 Ref.9

Modified residue

298

1

Phosphothreonine By similarity

Modified residue

480

1

Phosphoserine By similarity

Modified residue

553

1

Phosphoserine By similarity

Modified residue

555

1

Phosphoserine By similarity

Modified residue

565

1

Phosphoserine By similarity

Modified residue

631

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 599

599

Missing in isoform 7.

VSP_007509

Alternative sequence

1 – 477

477

MVEAI…LTHTR → MFPFRKGARPPSMNLFRQTC W in isoform 6.

VSP_007508

Alternative sequence

1 – 286

286

MVEAI…LPVEK → MGEEVSLGEKNISPEQASCG ALHPRGWGSQTFGVFLVNEE T in isoform 4.

VSP_007507

Alternative sequence

1 – 286

286

MVEAI…LPVEK → MGEE in isoform 5.

VSP_007506

Alternative sequence

1 – 54

54

MVEAI…DNFVR → MELSAAKAPSPTDLPES in isoform 3.

VSP_007505

Alternative sequence

174 – 217

44

Missing in isoform 2, isoform 3 and isoform 8.

VSP_007510

Alternative sequence

320 – 630

311

Missing in isoform 8.

VSP_007511

Experimental info

Sequence conflict

251 – 259

9

PKKVKGVGF → NDDELTIKE Ref.5

Sequence conflict

478 – 528

51

GDSPK…TTSRP → YCHVLTKAGGHGMIMKIGEG MRTKLCLKIPATFFSSEKVV ARCWGATWCRL in BAC30033. Ref.2

Sequence conflict

529 – 709

181

Missing in BAC30033. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

709

Helix Strand Turn

Details...

Beta strand

103 – 107

5

Beta strand

129 – 132

4

Beta strand

135 – 138

4

Beta strand

145 – 148

4

Beta strand

151 – 154

4

Beta strand

314 – 318

5

Beta strand

336 – 342

7

Beta strand

350 – 354

5

Beta strand

359 – 363

5

Helix

364 – 366

3

Beta strand

367 – 369

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Ruk-xl) [UniParc]. Last modified June 1, 2002. Version 1. Checksum: AC2DDFB3248A458B	FASTA	709	78,170
	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
	Isoform 2 (Ruk-l) [UniParc]. Checksum: 724607807A66B043	FASTA	665	73,328
	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 SKSSLRETTG 190 200 210 220 230 240 SESDGGDSSS TKSEGANGTM ATAAIQPKKV KGVGFGDIFK DKPIKLRPRS IEVENDFLPV 250 260 270 280 290 300 EKTIGKKLPP ATSTPDPSKT EMDSRTKTKD YCKVIFPYEA QNDDELTIKE GDIVTLINKD 310 320 330 340 350 360 CIDVGWWEGE LNGRRGVFPD NFVKLLPSDF DKEGNRPKKP PPPSAPVVKQ GAGTTERKHE 370 380 390 400 410 420 IKKIPPERPE TLPNRTEEKE RPEREPKLDL QKPSVPAIPP KKPRPPKTNS LNRPGALPPR 430 440 450 460 470 480 RPERPVGPLT HTRGDSPKID LAGSALSGIL DKDLSDRSND IDLEGFDSVI SSTEKLSHPT 490 500 510 520 530 540 TSRPKATGRR PPSQSLTSSS LSSPDIFDSP SPEEDKEEHI SLAHRGIDVS KKTSKTVTIS 550 560 570 580 590 600 QVSDNKTSLP PKPGTMAAAS SGPASLSSVA SSPMSSSLGT AGQRASSPSL FSTEGKPKME 610 620 630 640 650 660 PAVSSQAAIE ELKMQVRELR TIIETMKDQQ KREIKQLLSE LDEEKKIRLR LQMEVNDIKK ALQSK
	Isoform 3 (Ruk-deltaA) [UniParc]. Checksum: 1C4AEC6BE48D5D17	FASTA	628	68,820
	10 20 30 40 50 60 MELSAAKAPS PTDLPESEIK KDMKKDLLSN KAPEKPMHDV SSGNALLSSE TILRTNKRGE 70 80 90 100 110 120 RRRRRCQVAF SYLPQNDDEL ELKVGDIIEV VGEVEEGWWE GVLNGKTGMF PSNFIKELSG 130 140 150 160 170 180 ESDELGISQD EQLSKSSLRE TTGSESDGGD SSSTKSEGAN GTMATAAIQP KKVKGVGFGD 190 200 210 220 230 240 IFKDKPIKLR PRSIEVENDF LPVEKTIGKK LPPATSTPDP SKTEMDSRTK TKDYCKVIFP 250 260 270 280 290 300 YEAQNDDELT IKEGDIVTLI NKDCIDVGWW EGELNGRRGV FPDNFVKLLP SDFDKEGNRP 310 320 330 340 350 360 KKPPPPSAPV VKQGAGTTER KHEIKKIPPE RPETLPNRTE EKERPEREPK LDLQKPSVPA 370 380 390 400 410 420 IPPKKPRPPK TNSLNRPGAL PPRRPERPVG PLTHTRGDSP KIDLAGSALS GILDKDLSDR 430 440 450 460 470 480 SNDIDLEGFD SVISSTEKLS HPTTSRPKAT GRRPPSQSLT SSSLSSPDIF DSPSPEEDKE 490 500 510 520 530 540 EHISLAHRGI DVSKKTSKTV TISQVSDNKT SLPPKPGTMA AASSGPASLS SVASSPMSSS 550 560 570 580 590 600 LGTAGQRASS PSLFSTEGKP KMEPAVSSQA AIEELKMQVR ELRTIIETMK DQQKREIKQL 610 620 LSELDEEKKI RLRLQMEVND IKKALQSK
	Isoform 4 (Ruk-m1) [UniParc]. Checksum: 54F018C499D51044	FASTA	464	50,755
	10 20 30 40 50 60 MGEEVSLGEK NISPEQASCG ALHPRGWGSQ TFGVFLVNEE TTIGKKLPPA TSTPDPSKTE 70 80 90 100 110 120 MDSRTKTKDY CKVIFPYEAQ NDDELTIKEG DIVTLINKDC IDVGWWEGEL NGRRGVFPDN 130 140 150 160 170 180 FVKLLPSDFD KEGNRPKKPP PPSAPVVKQG AGTTERKHEI KKIPPERPET LPNRTEEKER 190 200 210 220 230 240 PEREPKLDLQ KPSVPAIPPK KPRPPKTNSL NRPGALPPRR PERPVGPLTH TRGDSPKIDL 250 260 270 280 290 300 AGSALSGILD KDLSDRSNDI DLEGFDSVIS STEKLSHPTT SRPKATGRRP PSQSLTSSSL 310 320 330 340 350 360 SSPDIFDSPS PEEDKEEHIS LAHRGIDVSK KTSKTVTISQ VSDNKTSLPP KPGTMAAASS 370 380 390 400 410 420 GPASLSSVAS SPMSSSLGTA GQRASSPSLF STEGKPKMEP AVSSQAAIEE LKMQVRELRT 430 440 450 460 IIETMKDQQK REIKQLLSEL DEEKKIRLRL QMEVNDIKKA LQSK
	Isoform 5 (Ruk-m3) [UniParc]. Checksum: 460A56431A4FDDCD	FASTA	427	46,827
	10 20 30 40 50 60 MGEETIGKKL PPATSTPDPS KTEMDSRTKT KDYCKVIFPY EAQNDDELTI KEGDIVTLIN 70 80 90 100 110 120 KDCIDVGWWE GELNGRRGVF PDNFVKLLPS DFDKEGNRPK KPPPPSAPVV KQGAGTTERK 130 140 150 160 170 180 HEIKKIPPER PETLPNRTEE KERPEREPKL DLQKPSVPAI PPKKPRPPKT NSLNRPGALP 190 200 210 220 230 240 PRRPERPVGP LTHTRGDSPK IDLAGSALSG ILDKDLSDRS NDIDLEGFDS VISSTEKLSH 250 260 270 280 290 300 PTTSRPKATG RRPPSQSLTS SSLSSPDIFD SPSPEEDKEE HISLAHRGID VSKKTSKTVT 310 320 330 340 350 360 ISQVSDNKTS LPPKPGTMAA ASSGPASLSS VASSPMSSSL GTAGQRASSP SLFSTEGKPK 370 380 390 400 410 420 MEPAVSSQAA IEELKMQVRE LRTIIETMKD QQKREIKQLL SELDEEKKIR LRLQMEVNDI KKALQSK
	Isoform 6 (Ruk-t) [UniParc]. Checksum: D1B221FDDE4C72C7	FASTA	253	27,442
	10 20 30 40 50 60 MFPFRKGARP PSMNLFRQTC WGDSPKIDLA GSALSGILDK DLSDRSNDID LEGFDSVISS 70 80 90 100 110 120 TEKLSHPTTS RPKATGRRPP SQSLTSSSLS SPDIFDSPSP EEDKEEHISL AHRGIDVSKK 130 140 150 160 170 180 TSKTVTISQV SDNKTSLPPK PGTMAAASSG PASLSSVASS PMSSSLGTAG QRASSPSLFS 190 200 210 220 230 240 TEGKPKMEPA VSSQAAIEEL KMQVRELRTI IETMKDQQKR EIKQLLSELD EEKKIRLRLQ 250 MEVNDIKKAL QSK
	Isoform 7 (Ruk-h) [UniParc]. Checksum: 6536493B3B3761DE	FASTA	110	11,992
	10 20 30 40 50 60 MAAASSGPAS LSSVASSPMS SSLGTAGQRA SSPSLFSTEG KPKMEPAVSS QAAIEELKMQ 70 80 90 100 110 VRELRTIIET MKDQQKREIK QLLSELDEEK KIRLRLQMEV NDIKKALQSK
	Isoform 8 (Ruk-deltaCP) [UniParc]. Checksum: B580135B37F9B571	FASTA	354	39,765
	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 SKSSLRETTG 190 200 210 220 230 240 SESDGGDSSS TKSEGANGTM ATAAIQPKKV KGVGFGDIFK DKPIKLRPRS IEVENDFLPV 250 260 270 280 290 300 EKTIGKKLPP ATSTPDPSKT EMDSRTKTKD YCKVISPSLF STEGKPKMEP AVSSQAAIEE 310 320 330 340 350 LKMQVRELRT IIETMKDQQK REIKQLLSEL DEEKKIRLRL QMEVNDIKKA LQSK

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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 , 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.

CCDS

CCDS41194.1. [Q8R550-3]
CCDS53234.1. [Q8R550-2]
CCDS53235.1. [Q8R550-5]

RefSeq

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]

UniGene

Mm.286495.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WI7	NMR	-	A	101-155	[»]
2DA9	NMR	-	A	314-370	[»]

ProteinModelPortal

Q8R550.

SMR

Q8R550. Positions 2-166, 314-389.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

208383. 6 interactions.

IntAct

Q8R550. 9 interactions.

MINT

MINT-1591643.

PTM databases

PhosphoSite

Q8R550.

Proteomic databases

MaxQB

Q8R550.

PaxDb

Q8R550.

PRIDE

Q8R550.

Protocols and materials databases

DNASU

58194.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

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]

GeneID

58194.

KEGG

mmu:58194.

UCSC

uc009uss.2. mouse. [Q8R550-1]
uc009usx.2. mouse. [Q8R550-5]

Organism-specific databases

CTD

30011.

MGI

MGI:1889583. Sh3kbp1.

Phylogenomic databases

eggNOG

NOG319250.

GeneTree

ENSGT00530000063594.

HOVERGEN

HBG057824.

InParanoid

Q8R550.

KO

K12470.

OMA

MDSRTKT.

OrthoDB

EOG7W41BC.

PhylomeDB

Q8R550.

TreeFam

TF350191.

Gene expression databases

ArrayExpress

Q8R550.

Bgee

Q8R550.

CleanEx

MM_SH3KBP1.

Genevestigator

Q8R550.

Family and domain databases

InterPro

IPR001452. SH3_domain.
[Graphical view]

Pfam

PF14604. SH3_9. 3 hits.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.

SMART

SM00326. SH3. 3 hits.
[Graphical view]

SUPFAM

SSF50044. SSF50044. 3 hits.

PROSITE

PS50002. SH3. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SH3KBP1. mouse.

EvolutionaryTrace

Q8R550.

NextBio

314169.

PRO

Q8R550.

SOURCE

Search...

Entry information

Entry name

SH3K1_MOUSE

Accession

Primary (citable) accession number: Q8R550
Secondary accession number(s): B1AZ86 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program