Q9Z0R4 (ITSN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Intersectin-1

Alternative name(s):
EH and SH3 domains protein 1

Gene names

Name:	Itsn1
Synonyms:	Ese1, Itsn

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	1714 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adapter protein that may provide indirect link between the endocytic membrane traffic and the actin assembly machinery. May regulate the formation of clathrin-coated vesicles. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR); internalization of ITGB1 as DAB2-dependent cargo but not TFR may involve association with DAB2. Inhibits ARHGAP31 activity toward RAC1.
Subunit structure	Interacts with dynamin, CDC42, SNAP25 and SNAP23. Clusters several dynamin in a manner that is regulated by alternative splicing. Interacts with clathrin-associated proteins and other components of the endocytic machinery, such as SPIN90, EPS15, EPN1, EPN2, STON2, FCHO1, FCHO2 and DAB2. Interacts (via SH3 domains) with REPS1 and SGIP1. Interacts with ARHGAP31. Interacts with ADAM15. Ref.4 Ref.11
Subcellular location	Endomembrane system By similarity. Cell junction › synapse › synaptosome By similarity. Cell projection › lamellipodium By similarity. Membrane › clathrin-coated pit By similarity. Note: Colocalizes with SGIP1 at the plasma membrane in structures corresponding most problably to clathrin-coated pits By similarity.
Tissue specificity	Widely expressed. Expressed at high levels in brain, heart and skeletal muscle.
Domain	SH3-3, SH3-4 and SH3-5, but not SH3-1 and SH3-2 domains, bind to dynamin By similarity. SH3-1 and SH3-4 bind to ARHGAP31. The KLERQ domain binds to SNAP-25 and SNAP-23 By similarity.
Miscellaneous	Overexpression results in the inhibition of the transferrin uptake and the blockage of the clathrin-mediated endocytosis.
Sequence similarities	Contains 1 C2 domain. Contains 1 DH (DBL-homology) domain. Contains 2 EF-hand domains. Contains 2 EH domains. Contains 1 PH domain. Contains 5 SH3 domains.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell junction Cell projection Coated pit Membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat SH3 domain
Ligand	Calcium Metal-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endocytosis Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 17875942. Source: MGI positive regulation of protein kinase B signaling cascade Inferred from direct assay PubMed 17875942. Source: MGI regulation of Rho protein signal transduction Inferred from electronic annotation. Source: InterPro small GTPase mediated signal transduction Inferred from direct assay Ref.4. Source: MGI
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell endocytic vesicle Inferred from direct assay PubMed 17875942. Source: MGI lamellipodium Inferred from direct assay Ref.4. Source: MGI neuron projection Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: Compara synapse Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	Rho guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: InterPro calcium ion binding Inferred from electronic annotation. Source: InterPro kinase activator activity Inferred from direct assay PubMed 17875942. Source: MGI phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Arhgap31	A6X8Z5	3	EBI-645386,EBI-4325995

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9Z0R4-1)

Also known as: Ese1L;

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: Q9Z0R4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1214-1714: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1714

1714

Intersectin-1

PRO_0000080958

Regions

Domain

21 – 109

89

EH 1

Domain

53 – 88

36

EF-hand 1

Domain

221 – 310

90

EH 2

Domain

254 – 289

36

EF-hand 2

Domain

738 – 799

62

SH3 1

Domain

906 – 964

59

SH3 2

Domain

995 – 1053

59

SH3 3

Domain

1067 – 1131

65

SH3 4

Domain

1148 – 1207

60

SH3 5

Domain

1230 – 1416

187

DH

Domain

1455 – 1564

110

PH

Domain

1576 – 1672

97

C2

Calcium binding

66 – 78

13

1 Potential

Calcium binding

267 – 279

13

2 Potential

Region

326 – 702

377

KLERQ

Coiled coil

352 – 662

311

Potential

Compositional bias

321 – 324

4

Poly-Ser

Amino acid modifications

Modified residue

313

1

Phosphoserine Ref.9

Modified residue

315

1

Phosphoserine Ref.5

Modified residue

318

1

Phosphoserine Ref.9

Modified residue

334

1

Phosphoserine Ref.9

Modified residue

335

1

Phosphoserine Ref.5 Ref.7 Ref.9 Ref.10

Modified residue

895

1

Phosphoserine Ref.5 Ref.9

Modified residue

897

1

Phosphoserine Ref.9

Modified residue

970

1

Phosphothreonine Ref.8

Modified residue

977

1

Phosphothreonine Ref.9

Modified residue

1130

1

Phosphoserine Ref.6

Natural variations

Alternative sequence

1214 – 1714

501

Missing in isoform 2.

VSP_004296

Experimental info

Sequence conflict

179

1

L → W in AAD19749. Ref.1

Sequence conflict

179

1

L → W in AAD19746. Ref.1

Sequence conflict

402

1

R → A in AAD19749. Ref.1

Sequence conflict

402

1

R → A in AAD19746. Ref.1

Secondary structure

1

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1714

Helix Strand Turn

Details...

Beta strand

1151 – 1157

7

Beta strand

1174 – 1179

6

Beta strand

1185 – 1190

6

Beta strand

1193 – 1198

6

Helix

1199 – 1201

3

Beta strand

1202 – 1204

3

Helix

1205 – 1207

3

Helix

1210 – 1214

5

Helix

1221 – 1223

3

Helix

1226 – 1255

30

Helix

1258 – 1261

4

Helix

1268 – 1275

8

Helix

1278 – 1299

22

Helix

1309 – 1315

7

Helix

1316 – 1320

5

Helix

1321 – 1342

22

Helix

1344 – 1353

10

Helix

1357 – 1359

3

Helix

1364 – 1367

4

Helix

1370 – 1386

17

Helix

1396 – 1422

27

Helix

1423 – 1425

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Ese1L) [UniParc]. Last modified October 3, 2012. Version 2. Checksum: BCF5038160E8208E	FASTA	1,714	194,297
	10 20 30 40 50 60 MAQFPTPFGG SLDVWAITVE ERAKHDQQFL SLKPIAGFIT GDQARNFFFQ SGLPQPVLAQ 70 80 90 100 110 120 IWALADMNND GRMDQVEFSI AMKLIKLKLQ GYQLPSTLPP VMKQQPVAIS SAPAFGIGGI 130 140 150 160 170 180 ASMPPLTAVA PVPMGSIPVV GMSPPLVSSV PPAAVPPLAN GAPPVIQPLP AFAHPAATLP 190 200 210 220 230 240 KSSSFSRSGP GSQLNTKLQK AQSFDVASAP PAAEWAVPQS SRLKYRQLFN SHDKTMSGHL 250 260 270 280 290 300 TGPQARTILM QSSLPQAQLA SIWNLSDIDQ DGKLTAEEFI LAMHLIDVAM SGQPLPPVLP 310 320 330 340 350 360 PEYIPPSFRR VRSGSGMSVI SSSSVDQRLP EEPSSEDEQQ PEKKLPVTFE DKKRENFERG 370 380 390 400 410 420 SVELEKRRQA LLEQQRKEQE RLAQLERAEQ ERKERERQEQ ERKRQLELEK QLEKQRELER 430 440 450 460 470 480 QREEERRKEI ERREAAKREL ERQRQLEWER NRRQELLNQR NKEQEGTVVL KARRKTLEFE 490 500 510 520 530 540 LEALNDKKHQ LEGKLQDIRC RLATQRQEIE STNKSRELRI AEITHLQQQL QESQQMLGRL 550 560 570 580 590 600 IPEKQILSDQ LKQVQQNSLH RDSLLTLKRA LEAKELARQQ LREQLDEVER ETRSKLQEID 610 620 630 640 650 660 VFNNQLKELR EIHSKQQLQK QRSLEAARLK QKEQERKSLE LEKQKEDAQR RVQERDKQWL 670 680 690 700 710 720 EHVQQEEQPR PRKPHEEDRL KREDSVRKKE AEERAKPEMQ DKQSRLFHPH QEPAKLATQA 730 740 750 760 770 780 PWSTTEKGPL TISAQESVKV VYYRALYPFE SRSHDEITIQ PGDIVMVDES QTGEPGWLGG 790 800 810 820 830 840 ELKGKTGWFP ANYAEKIPEN EVPTPAKPVT DLTSAPAPKL ALRETPAPLP VTSSEPSTTP 850 860 870 880 890 900 NNWADFSSTW PSSSNEKPET DNWDTWAAQP SLTVPSAGQL RQRSAFTPAT ATGSSPSPVL 910 920 930 940 950 960 GQGEKVEGLQ AQALYPWRAK KDNHLNFNKS DVITVLEQQD MWWFGEVQGQ KGWFPKSYVK 970 980 990 1000 1010 1020 LISGPVRKST SIDTGPTESP ASLKRVASPA AKPAIPGEEF IAMYTYESSE QGDLTFQQGD 1030 1040 1050 1060 1070 1080 VIVVTKKDGD WWTGTVGDKS GVFPSNYVRL KDSEGSGTAG KTGSLGKKPE IAQVIASYAA 1090 1100 1110 1120 1130 1140 TGPEQLTLAP GQLILIRKKN PGGWWEGELQ ARGKKRQIGW FPANYVKLLS PGTSKITPTE 1150 1160 1170 1180 1190 1200 LPKTAVQPAV CQVIGMYDYT AQNDDELAFS KGQIINVLNK EDPDWWKGEV SGQVGLFPSN 1210 1220 1230 1240 1250 1260 YVKLTTDMDP SQQWCSDLHL LDMLTPTERK RQGYIHELIV TEENYVNDLQ LVTEIFQKPL 1270 1280 1290 1300 1310 1320 TESELLTEKE VAMIFVNWKE LIMCNIKLLK ALRVRKKMSG EKMPVKMIGD ILSAQLPHMQ 1330 1340 1350 1360 1370 1380 PYIRFCSCQL NGAALIQQKT DEAPDFKEFV KRLAMDPRCK GMPLSSFILK PMQRVTRYPL 1390 1400 1410 1420 1430 1440 IIKNILENTP ENHPDHSHLK HALEKAEELC SQVNEGVREK ENSDRLEWIQ AHVQCEGLSE 1450 1460 1470 1480 1490 1500 QLVFNSVTNC LGPRKFLHSG KLYKAKSNKE LYGFLFNDFL LLTQITKPLG SSGTDKVFSP 1510 1520 1530 1540 1550 1560 KSNLQYKMYK TPIFLNEVLV KLPTDPSGDE PIFHISHIDR VYTLRAESIN ERTAWVQKIK 1570 1580 1590 1600 1610 1620 AASELYIETE KKKREKAYLV RSQRATGIGR LMVNVVEGIE LKPCRSHGKS NPYCEVTMGS 1630 1640 1650 1660 1670 1680 QCHITKTIQD TLNPKWNSNC QFFIRDLEQE VLCITVFERD QFSPDDFLGR TEIRVADIKK 1690 1700 1710 DQGSKGPVTK CLLLHEVPTG EIVVRLDLQL FDEP
	Isoform 2 [UniParc]. Checksum: 1376AD0DFBD503C2	FASTA	1,213	136,607
	10 20 30 40 50 60 MAQFPTPFGG SLDVWAITVE ERAKHDQQFL SLKPIAGFIT GDQARNFFFQ SGLPQPVLAQ 70 80 90 100 110 120 IWALADMNND GRMDQVEFSI AMKLIKLKLQ GYQLPSTLPP VMKQQPVAIS SAPAFGIGGI 130 140 150 160 170 180 ASMPPLTAVA PVPMGSIPVV GMSPPLVSSV PPAAVPPLAN GAPPVIQPLP AFAHPAATLP 190 200 210 220 230 240 KSSSFSRSGP GSQLNTKLQK AQSFDVASAP PAAEWAVPQS SRLKYRQLFN SHDKTMSGHL 250 260 270 280 290 300 TGPQARTILM QSSLPQAQLA SIWNLSDIDQ DGKLTAEEFI LAMHLIDVAM SGQPLPPVLP 310 320 330 340 350 360 PEYIPPSFRR VRSGSGMSVI SSSSVDQRLP EEPSSEDEQQ PEKKLPVTFE DKKRENFERG 370 380 390 400 410 420 SVELEKRRQA LLEQQRKEQE RLAQLERAEQ ERKERERQEQ ERKRQLELEK QLEKQRELER 430 440 450 460 470 480 QREEERRKEI ERREAAKREL ERQRQLEWER NRRQELLNQR NKEQEGTVVL KARRKTLEFE 490 500 510 520 530 540 LEALNDKKHQ LEGKLQDIRC RLATQRQEIE STNKSRELRI AEITHLQQQL QESQQMLGRL 550 560 570 580 590 600 IPEKQILSDQ LKQVQQNSLH RDSLLTLKRA LEAKELARQQ LREQLDEVER ETRSKLQEID 610 620 630 640 650 660 VFNNQLKELR EIHSKQQLQK QRSLEAARLK QKEQERKSLE LEKQKEDAQR RVQERDKQWL 670 680 690 700 710 720 EHVQQEEQPR PRKPHEEDRL KREDSVRKKE AEERAKPEMQ DKQSRLFHPH QEPAKLATQA 730 740 750 760 770 780 PWSTTEKGPL TISAQESVKV VYYRALYPFE SRSHDEITIQ PGDIVMVDES QTGEPGWLGG 790 800 810 820 830 840 ELKGKTGWFP ANYAEKIPEN EVPTPAKPVT DLTSAPAPKL ALRETPAPLP VTSSEPSTTP 850 860 870 880 890 900 NNWADFSSTW PSSSNEKPET DNWDTWAAQP SLTVPSAGQL RQRSAFTPAT ATGSSPSPVL 910 920 930 940 950 960 GQGEKVEGLQ AQALYPWRAK KDNHLNFNKS DVITVLEQQD MWWFGEVQGQ KGWFPKSYVK 970 980 990 1000 1010 1020 LISGPVRKST SIDTGPTESP ASLKRVASPA AKPAIPGEEF IAMYTYESSE QGDLTFQQGD 1030 1040 1050 1060 1070 1080 VIVVTKKDGD WWTGTVGDKS GVFPSNYVRL KDSEGSGTAG KTGSLGKKPE IAQVIASYAA 1090 1100 1110 1120 1130 1140 TGPEQLTLAP GQLILIRKKN PGGWWEGELQ ARGKKRQIGW FPANYVKLLS PGTSKITPTE 1150 1160 1170 1180 1190 1200 LPKTAVQPAV CQVIGMYDYT AQNDDELAFS KGQIINVLNK EDPDWWKGEV SGQVGLFPSN 1210 YVKLTTDMDP SQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The EH and SH3 domain Ese proteins regulate endocytosis by linking to dynamin and Eps15." Sengar A.S., Wang W., Bishay J., Cohen S., Egan S.E. EMBO J. 18:1159-1171(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"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.
[3]	"Mouse homologues of human chromosome 21 genes." Skripkina I.Y., Tsyba L.O., Anoprienko O.V., Slavov D., Tassone F., Rynditch A.V., Gardiner K. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 966-1714, NUCLEOTIDE SEQUENCE [MRNA] OF 545-599 (ISOFORMS 1 AND 2). Strain: 129/Ola. Tissue: Spleen.
[4]	"The activity of the GTPase-activating protein CdGAP is regulated by the endocytic protein intersectin." Jenna S., Hussain N.K., Danek E.I., Triki I., Wasiak S., McPherson P.S., Lamarche-Vane N. J. Biol. Chem. 277:6366-6373(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARHGAP31.
[5]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-335 AND SER-895, MASS SPECTROMETRY. Tissue: Embryonic brain.
[6]	"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-1130, MASS SPECTROMETRY. Tissue: Brain.
[7]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, MASS SPECTROMETRY. Tissue: Liver.
[8]	"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 THR-970, MASS SPECTROMETRY. Tissue: Brain cortex.
[9]	"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-313; SER-318; SER-334; SER-335; SER-895; SER-897 AND THR-977, MASS SPECTROMETRY. Tissue: Liver.
[10]	"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-335, MASS SPECTROMETRY. Tissue: Liver.
[11]	"FCHo proteins are nucleators of clathrin-mediated endocytosis." Henne W.M., Boucrot E., Meinecke M., Evergren E., Vallis Y., Mittal R., McMahon H.T. Science 328:1281-1284(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FCHO2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF132481 mRNA. Translation: AAD19749.1.
AF132478 mRNA. Translation: AAD19746.1.
AC126053 Genomic DNA. No translation available.
AC131691 Genomic DNA. No translation available.
AC134837 Genomic DNA. No translation available.
AF169621 mRNA. Translation: AAD48848.1.
AF356517 Genomic DNA. Translation: AAK40228.1.

IPI

IPI00129356.
IPI00222409.

RefSeq

NP_001103745.1. NM_001110275.1.
NP_034717.2. NM_010587.2.

UniGene

Mm.40546.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3HS8	X-ray	1.90	P	840-851	[»]
3JV3	X-ray	2.40	A/B	1151-1431	[»]

ProteinModelPortal

Q9Z0R4.

SMR

Q9Z0R4. Positions 1-111, 210-312, 906-964, 998-1053, 1063-1574, 1588-1711.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Z0R4. 6 interactions.

MINT

MINT-86500.

STRING

10090.ENSMUSP00000066361.

PTM databases

PhosphoSite

Q9Z0R4.

Proteomic databases

PaxDb

Q9Z0R4.

PRIDE

Q9Z0R4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000056482; ENSMUSP00000056011; ENSMUSG00000022957.
ENSMUST00000114002; ENSMUSP00000109635; ENSMUSG00000022957.

GeneID

16443.

KEGG

mmu:16443.

UCSC

uc007zyj.1. mouse.

Organism-specific databases

CTD

6453.

MGI

MGI:1338069. Itsn1.

Phylogenomic databases

eggNOG

COG5422.

GeneTree

ENSGT00700000104202.

HOGENOM

HOG000010175.

HOVERGEN

HBG052159.

OrthoDB

EOG46Q6RS.

Gene expression databases

CleanEx

MM_ITSN1.

Genevestigator

Q9Z0R4.

GermOnline

ENSMUSG00000022957. Mus musculus.

Family and domain databases

Gene3D

1.10.238.10. 2 hits.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.

InterPro

IPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR000219. DH-domain.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
IPR001331. GDS_CDC24_CS.
IPR026813. ITSN1.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]

PANTHER

PTHR11216:SF28. PTHR11216:SF28. 1 hit.

Pfam

PF00168. C2. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00018. SH3_1. 4 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.

SMART

SM00239. C2. 1 hit.
SM00054. EFh. 2 hits.
SM00027. EH. 2 hits.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00326. SH3. 5 hits.
[Graphical view]

SUPFAM

SSF49562. C2_CaLB. 1 hit.
SSF48065. DH-domain. 1 hit.
SSF50044. SH3. 5 hits.

PROSITE

PS50004. C2. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 2 hits.
PS50031. EH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ITSN1. mouse.

EvolutionaryTrace

Q9Z0R4.

NextBio

289695.

SOURCE

Search...

Entry information

Entry name

ITSN1_MOUSE

Accession

Primary (citable) accession number: Q9Z0R4
Secondary accession number(s): F8VQE5, Q9R143

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	October 3, 2012
Last modified:	May 29, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program