Q69ZI1 (SH3R1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase SH3RF1
EC=6.3.2.-

Alternative name(s):
Plenty of SH3s
Short name=Protein POSH
SH3 domain-containing RING finger protein 1
SH3 multiple domains protein 2

Gene names

Name:	Sh3rf1
Synonyms:	Kiaa1494, Posh, Sh3md2

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 › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	892 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9) By similarity. In fibroblasts, induces apoptosis. Ref.1 Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes such as UBE2D1 or UBE2N and then transfers it to substrates. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis By similarity. Ref.1
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with HERP1 By similarity. Interacts with Rac; in a GTP-dependent manner. Interacts with MAP3K10 and MAP3K11. Interacts with MAPK8IP; this interaction leads to the PJAC complex (POSH-JIP or SH3RF1/MAPK8IP apoptotic complex) with a 1:1 ratio. Interacts with SIAH1. Probably part of a signaling complex that may contain SH3RF1, MAPK8IP, DLK1, MAP2K4, MAP2K7, MAPK8, MAPK9, AKT1 and AKT2. Ref.1 Ref.5 Ref.6 Ref.7 Ref.8
Subcellular location	Cytoplasm › perinuclear region By similarity. Cell projection › lamellipodium. Golgi apparatus › trans-Golgi network. Note: Co-localizes, with AKT2, in lamellipodia By similarity. Co-localizes, with HERP1, in trans-Golgi network By similarity. Ref.6
Tissue specificity	Ubiquitously expressed. Ref.1
Domain	The RING finger domain is responsible of ubiquitination and proteasomal degradation.
Post-translational modification	Phosphorylated at Ser-304 by AKT1 and AKT2. When phosphorylated, it has reduced ability to bind Rac By similarity. Subject to ubiquitination and proteasomal degradation By similarity.
Sequence similarities	Belongs to the SH3RF family. Contains 1 RING-type zinc finger. Contains 4 SH3 domains.
Sequence caution	The sequence BAD32463.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cell projection Cytoplasm Golgi apparatus
Coding sequence diversity	Alternative splicing
Domain	Repeat SH3 domain Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of JNK cascade Inferred from direct assay PubMed 12944902. Source: MGI
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell lamellipodium Inferred from direct assay PubMed 12944902. Source: MGI perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	MAP-kinase scaffold activity Inferred from direct assay PubMed 12944902. Source: MGI ligase activity Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Bnip3l	Q9Z2F7	4	EBI-957380,EBI-1774669
SIAH1	Q8IUQ4	5	EBI-957380,EBI-747107	From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q69ZI1-1)

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.

Isoform 2 (identifier: Q69ZI1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     160-189: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q69ZI1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     788-828: AAGTAALAQD...ACSSLGPVMN → DRWNSSPSPG...GLLLPGPSHE
     829-892: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: Q69ZI1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     345-381: ELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPAFT → APSQVQGRGQLPKRGLLTSGKILAASFIFALVTSSLL
     382-892: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 892	892	E3 ubiquitin-protein ligase SH3RF1		PRO_0000334152
Regions
	Domain	134 – 193	60	SH3 1
	Domain	196 – 259	64	SH3 2
	Domain	452 – 513	62	SH3 3
	Domain	833 – 892	60	SH3 4
	Zinc finger	12 – 53	42	RING-type
	Region	447 – 550	104	Interaction with AKT2
	Compositional bias	84 – 90	7	Poly-Gly
	Compositional bias	397 – 403	7	Poly-Pro
	Compositional bias	406 – 431	26	Ala-rich
Amino acid modifications
	Modified residue	304	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	160 – 189	30	Missing in isoform 2.		VSP_033624
	Alternative sequence	345 – 381	37	ELSGL…GPAFT → APSQVQGRGQLPKRGLLTSG KILAASFIFALVTSSLL in isoform 4.		VSP_033625
	Alternative sequence	382 – 892	511	Missing in isoform 4.		VSP_033626
	Alternative sequence	788 – 828	41	AAGTA…GPVMN → DRWNSSPSPGCLPPQDKLPG LRSAHCSTTSPGLLLPGPSH E in isoform 3.		VSP_033627
	Alternative sequence	829 – 892	64	Missing in isoform 3.		VSP_033628
Experimental info
	Mutagenesis	470	1	E → Q: Loss of binding to AKT2. Ref.6
	Mutagenesis	489	1	W → A: Loss of binding to AKT2 and enhanced binding to MAP3K11. Ref.6
	Sequence conflict	160	1	I → T in AAC40070. Ref.1
	Sequence conflict	321	1	R → S in BAE28367. Ref.3
	Sequence conflict	342	1	R → G in BAE28367. Ref.3
	Sequence conflict	431	1	Missing in BAC32385. Ref.3
	Sequence conflict	431	1	Missing in AAH60113. Ref.4
	Sequence conflict	431	1	Missing in AAH60696. Ref.4
	Sequence conflict	630	1	L → M in BAE28367. Ref.3
	Sequence conflict	679	1	M → V in BAC32385. Ref.3
	Sequence conflict	679	1	M → V in AAH60113. Ref.4
	Sequence conflict	679	1	M → V in AAH60696. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 20, 2008. Version 2. Checksum: D92071116F4D6EBE	FASTA	892	93,447
	10 20 30 40 50 60 MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP ECRTLVGSGV 70 80 90 100 110 120 DELPSNILLV RLLDGIKQRP WKPGPGGGGG TTCTNTLRAQ GSTVVNCGSK DLQSSQCGQQ 130 140 150 160 170 180 PRVQAWSPPV RGIPQLPCAK ALYNYEGKEP GDLKFSKGDI IILRRQVDEN WYHGEVSGVH 190 200 210 220 230 240 GFFPTNFVQI IKPLPQPPPQ CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG 250 260 270 280 290 300 MLADKIGIFP ISYVEFNSAA KQLIEWDKPP VPGVDTAECP SATAQSTSAS KHPDTKKNTR 310 320 330 340 350 360 KRHSFTSLTM ANKSSQGSQN RHSMEISPPV LISSSNPTAA ARISELSGLS CSAPSQVHIS 370 380 390 400 410 420 TTGLIVTPPP SSPVTTGPAF TFPSDVPYQA ALGSMNPPLP PPPLLAATVL ASTPSGATAA 430 440 450 460 470 480 VAAAAAAAAA AGMGPRPVMG SSEQIAHLRP QTRPSVYVAI YPYTPRKEDE LELRKGEMFL 490 500 510 520 530 540 VFERCQDGWY KGTSMHTSKI GVFPGNYVAP VTRAVTNASQ AKVSMSTAGQ ASRGVTMVSP 550 560 570 580 590 600 STAGGPTQKP QGNGVAGNPS VVPTAVVSAA HIQTSPQAKV LLHMSGQMTV NQARNAVRTV 610 620 630 640 650 660 AAHSQERPTA AVTPIQVQNA ACLGPASVGL PHHSLASQPL PPMAGPAAHG AAVSISRTNA 670 680 690 700 710 720 PMACAAGASL ASPNMTSAML ETEPSGRTVT ILPGLPTSPE SAASACGNSS AGKPDKDSKK 730 740 750 760 770 780 EKKGLLKLLS GASTKRKPRV SPPASPTLDV ELGAGEAPLQ GAVGPELPLG GSHGRVGSCP 790 800 810 820 830 840 TDGDGPVAAG TAALAQDAFH RKTSSLDSAV PIAPPPRQAC SSLGPVMNEA RPVVCERHRV 850 860 870 880 890 VVSYPPQSEA ELELKEGDIV FVHKKREDGW FKGTLQRNGK TGLFPGSFVE NI
	Isoform 2 [UniParc]. Checksum: D2B2F85D18812B47	FASTA	862	89,906
	10 20 30 40 50 60 MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP ECRTLVGSGV 70 80 90 100 110 120 DELPSNILLV RLLDGIKQRP WKPGPGGGGG TTCTNTLRAQ GSTVVNCGSK DLQSSQCGQQ 130 140 150 160 170 180 PRVQAWSPPV RGIPQLPCAK ALYNYEGKEP GDLKFSKGDI IKPLPQPPPQ CKALYDFEVK 190 200 210 220 230 240 DKEADKDCLP FAKDDVLTVI RRVDENWAEG MLADKIGIFP ISYVEFNSAA KQLIEWDKPP 250 260 270 280 290 300 VPGVDTAECP SATAQSTSAS KHPDTKKNTR KRHSFTSLTM ANKSSQGSQN RHSMEISPPV 310 320 330 340 350 360 LISSSNPTAA ARISELSGLS CSAPSQVHIS TTGLIVTPPP SSPVTTGPAF TFPSDVPYQA 370 380 390 400 410 420 ALGSMNPPLP PPPLLAATVL ASTPSGATAA VAAAAAAAAA AGMGPRPVMG SSEQIAHLRP 430 440 450 460 470 480 QTRPSVYVAI YPYTPRKEDE LELRKGEMFL VFERCQDGWY KGTSMHTSKI GVFPGNYVAP 490 500 510 520 530 540 VTRAVTNASQ AKVSMSTAGQ ASRGVTMVSP STAGGPTQKP QGNGVAGNPS VVPTAVVSAA 550 560 570 580 590 600 HIQTSPQAKV LLHMSGQMTV NQARNAVRTV AAHSQERPTA AVTPIQVQNA ACLGPASVGL 610 620 630 640 650 660 PHHSLASQPL PPMAGPAAHG AAVSISRTNA PMACAAGASL ASPNMTSAML ETEPSGRTVT 670 680 690 700 710 720 ILPGLPTSPE SAASACGNSS AGKPDKDSKK EKKGLLKLLS GASTKRKPRV SPPASPTLDV 730 740 750 760 770 780 ELGAGEAPLQ GAVGPELPLG GSHGRVGSCP TDGDGPVAAG TAALAQDAFH RKTSSLDSAV 790 800 810 820 830 840 PIAPPPRQAC SSLGPVMNEA RPVVCERHRV VVSYPPQSEA ELELKEGDIV FVHKKREDGW 850 860 FKGTLQRNGK TGLFPGSFVE NI
	Isoform 3 [UniParc]. Checksum: C670E8A5CF0EB1D4	FASTA	828	86,342
	10 20 30 40 50 60 MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP ECRTLVGSGV 70 80 90 100 110 120 DELPSNILLV RLLDGIKQRP WKPGPGGGGG TTCTNTLRAQ GSTVVNCGSK DLQSSQCGQQ 130 140 150 160 170 180 PRVQAWSPPV RGIPQLPCAK ALYNYEGKEP GDLKFSKGDI IILRRQVDEN WYHGEVSGVH 190 200 210 220 230 240 GFFPTNFVQI IKPLPQPPPQ CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG 250 260 270 280 290 300 MLADKIGIFP ISYVEFNSAA KQLIEWDKPP VPGVDTAECP SATAQSTSAS KHPDTKKNTR 310 320 330 340 350 360 KRHSFTSLTM ANKSSQGSQN RHSMEISPPV LISSSNPTAA ARISELSGLS CSAPSQVHIS 370 380 390 400 410 420 TTGLIVTPPP SSPVTTGPAF TFPSDVPYQA ALGSMNPPLP PPPLLAATVL ASTPSGATAA 430 440 450 460 470 480 VAAAAAAAAA AGMGPRPVMG SSEQIAHLRP QTRPSVYVAI YPYTPRKEDE LELRKGEMFL 490 500 510 520 530 540 VFERCQDGWY KGTSMHTSKI GVFPGNYVAP VTRAVTNASQ AKVSMSTAGQ ASRGVTMVSP 550 560 570 580 590 600 STAGGPTQKP QGNGVAGNPS VVPTAVVSAA HIQTSPQAKV LLHMSGQMTV NQARNAVRTV 610 620 630 640 650 660 AAHSQERPTA AVTPIQVQNA ACLGPASVGL PHHSLASQPL PPMAGPAAHG AAVSISRTNA 670 680 690 700 710 720 PMACAAGASL ASPNMTSAML ETEPSGRTVT ILPGLPTSPE SAASACGNSS AGKPDKDSKK 730 740 750 760 770 780 EKKGLLKLLS GASTKRKPRV SPPASPTLDV ELGAGEAPLQ GAVGPELPLG GSHGRVGSCP 790 800 810 820 TDGDGPVDRW NSSPSPGCLP PQDKLPGLRS AHCSTTSPGL LLPGPSHE
	Isoform 4 [UniParc]. Checksum: 991E47F760D876CB	FASTA	381	41,433
	10 20 30 40 50 60 MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP ECRTLVGSGV 70 80 90 100 110 120 DELPSNILLV RLLDGIKQRP WKPGPGGGGG TTCTNTLRAQ GSTVVNCGSK DLQSSQCGQQ 130 140 150 160 170 180 PRVQAWSPPV RGIPQLPCAK ALYNYEGKEP GDLKFSKGDI IILRRQVDEN WYHGEVSGVH 190 200 210 220 230 240 GFFPTNFVQI IKPLPQPPPQ CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG 250 260 270 280 290 300 MLADKIGIFP ISYVEFNSAA KQLIEWDKPP VPGVDTAECP SATAQSTSAS KHPDTKKNTR 310 320 330 340 350 360 KRHSFTSLTM ANKSSQGSQN RHSMEISPPV LISSSNPTAA ARISAPSQVQ GRGQLPKRGL 370 380 LTSGKILAAS FIFALVTSSL L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A new rac target POSH is an SH3-containing scaffold protein involved in the JNK and NF-kappaB signalling pathways." Tapon N., Nagata K., Lamarche N., Hall A. EMBO J. 17:1395-1404(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH RAC.
[2]	"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 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., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H. DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Embryonic tail.
[3]	"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 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-892 (ISOFORM 1). Strain: C57BL/6J and NOD. Tissue: Corpora quadrigemina and Thymus.
[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] (ISOFORM 2). Strain: C57BL/6. Tissue: Brain.
[5]	"POSH acts as a scaffold for a multiprotein complex that mediates JNK activation in apoptosis." Xu Z., Kukekov N.V., Greene L.A. EMBO J. 22:252-261(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAP3K10; MAP3K11; DLK1; MAP2K4; MAP2K7; MAPK8 AND MAPK9.
[6]	"Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling complex." Figueroa C., Tarras S., Taylor J., Vojtek A.B. J. Biol. Chem. 278:47922-47927(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AKT2, MUTAGENESIS OF GLU-470 AND TRP-489, SUBCELLULAR LOCATION.
[7]	"Siah1 interacts with the scaffold protein POSH to promote JNK activation and apoptosis." Xu Z., Sproul A., Wang W., Kukekov N., Greene L.A. J. Biol. Chem. 281:303-312(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SIAH1.
[8]	"Direct interaction of the molecular scaffolds POSH and JIP is required for apoptotic activation of JNKs." Kukekov N.V., Xu Z., Greene L.A. J. Biol. Chem. 281:15517-15524(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAPK8IP.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF030131 mRNA. Translation: AAC40070.1. AK173185 mRNA. Translation: BAD32463.1. Different initiation. BC060113 mRNA. Translation: AAH60113.1. BC060696 mRNA. Translation: AAH60696.1. AK088003 mRNA. Translation: BAC40088.1. AK045470 mRNA. Translation: BAC32385.1. AK148137 mRNA. Translation: BAE28367.1.
IPI	IPI00399469. IPI00458726. IPI00894976. IPI00895133.
PIR	T09071.
RefSeq	NP_067481.2. NM_021506.2.
UniGene	Mm.27949.
3D structure databases
HSSP	HSSP built from PDB template 1WI7 based on UniProtKB Q8R551.
ProteinModelPortal	Q69ZI1.
SMR	Q69ZI1. Positions 5-78, 137-255, 457-512, 839-892.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q69ZI1. 5 interactions.
PTM databases
PhosphoSite	Q69ZI1.
Proteomic databases
PaxDb	Q69ZI1.
PRIDE	Q69ZI1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	59009.
KEGG	mmu:59009.
UCSC	uc009ltw.1. mouse.
Organism-specific databases
CTD	57630.
MGI	MGI:1913066. Sh3rf1.
Rouge	Search...
Phylogenomic databases
eggNOG	NOG314495.
HOGENOM	HOG000045564.
HOVERGEN	HBG069552.
InParanoid	Q69ZI1.
KO	K12171.
OrthoDB	EOG4PG61S.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
Genevestigator	Q69ZI1.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR000108. p67phox. IPR001452. SH3_domain. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00018. SH3_1. 4 hits. [Graphical view]
PRINTS	PR00499. P67PHOX. PR00452. SH3DOMAIN.
SMART	SM00184. RING. 1 hit. SM00326. SH3. 4 hits. [Graphical view]
SUPFAM	SSF50044. SH3. 4 hits.
PROSITE	PS50002. SH3. 4 hits. PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	314548.
SOURCE	Search...

Entry information

Entry name

SH3R1_MOUSE

Accession

Primary (citable) accession number: Q69ZI1
Secondary accession number(s): O70254 , Q3UG42, Q6P9M8, Q8BR66, Q8C2T5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program