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Reviewed, UniProtKB/Swiss-Prot Q9NZM3 (ITSN2_HUMAN)

Last modified July 7, 2009. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Intersectin-2
Alternative name(s):
    SH3 domain-containing protein 1B
    SH3P18
    SH3P18-like WASP-associated protein
Gene names
Name: ITSN2
Synonyms: KIAA1256, SH3D1B, SWAP
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1696 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Subunit structure

Belongs to a complex that may contain multimers of ITSN1, ITSN2 and EPS15, and different partners according to the step in the endocytic process.

Subcellular location

Cytoplasm.

Tissue specificity

Ubiquitous. Isoform 1 is primarily expressed in adult heart and liver.

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 processEndocytosis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
SH3 domain
   LigandCalcium
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processendocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of Rho protein signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionRho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

SH3/SH2 adaptor activity Ref.6

Traceable author statement. Source: ProtInc

calcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LSM8O957771EBI-308689,EBI-347779

Alternative products

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

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q9NZM3-1)

Also known as: ITSN2-L;

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: Q9NZM3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     621-647: Missing.
Isoform 3 (identifier: Q9NZM3-3)

Also known as: ITSN2-S1;

The sequence of this isoform differs from the canonical sequence as follows:
     1234-1248: FQKRMAESGFLTEGE → WRLLLASSRGICCLS
     1249-1696: Missing.
Isoform 4 (identifier: Q9NZM3-4)

Also known as: ITSN2-S2; SH3P18;

The sequence of this isoform differs from the canonical sequence as follows:
     1192-1696: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16961696Intersectin-2
PRO_0000080961

Regions

Domain21 – 10989EH 1
Domain53 – 8836EF-hand 1
Domain243 – 33290EH 2
Domain756 – 81762SH3 1
Domain897 – 95559SH3 2
Domain980 – 103859SH3 3
Domain1052 – 111665SH3 4
Domain1126 – 118560SH3 5
Domain1208 – 1394187DH
Domain1433 – 1543111PH
Domain1555 – 165197C2
Calcium binding66 – 7813 Potential
Coiled coil360 – 755396 Potential

Amino acid modifications

Modified residue2091Phosphoserine By similarity
Modified residue5521Phosphotyrosine Ref.9 Ref.11
Modified residue8581Phosphotyrosine Ref.10
Modified residue8831Phosphoserine Ref.12 Ref.13
Modified residue8881Phosphoserine Ref.12 Ref.13
Modified residue9671Phosphotyrosine Ref.10 Ref.8

Natural variations

Alternative sequence621 – 64727Missing in isoform 2.
VSP_003892
Alternative sequence1192 – 1696505Missing in isoform 4.
VSP_003895
Alternative sequence1234 – 124815FQKRM…LTEGE → WRLLLASSRGICCLS in isoform 3.
VSP_003893
Alternative sequence1249 – 1696448Missing in isoform 3.
VSP_003894
Natural variant2531T → A: dbSNP rs6744320.
VAR_024287
Natural variant2901V → I: dbSNP rs7603997. Ref.4
VAR_024288
Natural variant12861I → T: dbSNP rs3731625.
VAR_020193
Natural variant15331A → T: dbSNP rs2303291.
VAR_021937

Experimental info

Sequence conflict6781R → G Ref.4
Sequence conflict822 – 8276KAVSPK → FAAAST Ref.5
Sequence conflict944 – 9507WFPKSYV → EFAAAST Ref.6
Sequence conflict1278 – 12847GEKMPVQ → VDAAANS Ref.5
Sequence conflict15521K → Q Ref.2
Sequence conflict15521K → Q Ref.3

Secondary structure

................................................. 1696
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ITSN2-L) [UniParc].

Last modified April 3, 2002. Version 2.
Checksum: 17B5C8629BBCFF9B

FASTA1,696193,330
        10         20         30         40         50         60 
MAQFPTAMNG GPNMWAITSE ERTKHDRQFD NLKPSGGYIT GDQARNFFLQ SGLPAPVLAE 

        70         80         90        100        110        120 
IWALSDLNKD GKMDQQEFSI AMKLIKLKLQ GQQLPVVLPP IMKQPPMFSP LISARFGMGS 

       130        140        150        160        170        180 
MPNLSIPQPL PPAAPITSLS SATSGTNLPP LMMPTPLVPS VSTSSLPNGT ASLIQPLPIP 

       190        200        210        220        230        240 
YSSSTLPHGS SYSLMMGGFG GASIQKAQSL IDLGSSSSTS STASLSGNSP KTGTSEWAVP 

       250        260        270        280        290        300 
QPTRLKYRQK FNTLDKSMSG YLSGFQARNA LLQSNLSQTQ LATIWTLADV DGDGQLKAEE 

       310        320        330        340        350        360 
FILAMHLTDM AKAGQPLPLT LPPELVPPSF RGGKQIDSIN GTLPSYQKMQ EEEPQKKLPV 

       370        380        390        400        410        420 
TFEDKRKANY ERGNMELEKR RQALMEQQQR EAERKAQKEK EEWERKQREL QEQEWKKQLE 

       430        440        450        460        470        480 
LEKRLEKQRE LERQREEERR KDIERREAAK QELERQRRLE WERIRRQELL NQKNREQEEI 

       490        500        510        520        530        540 
VRLNSKKKNL HLELEALNGK HQQISGRLQD VRLKKQTQKT ELEVLDKQCD LEIMEIKQLQ 

       550        560        570        580        590        600 
QELQEYQNKL IYLVPEKQLL NERIKNMQFS NTPDSGVSLL HKKSLEKEEL CQRLKEQLDA 

       610        620        630        640        650        660 
LEKETASKLS EMDSFNNQLK CGNMDDSVLQ CLLSLLSCLN NLFLLLKELR ETYNTQQLAL 

       670        680        690        700        710        720 
EQLYKIKRDK LKEIERKRLE LMQKKKLEDE AARKAKQGKE NLWKENLRKE EEEKQKRLQE 

       730        740        750        760        770        780 
EKTQEKIQEE ERKAEEKQRK DKDTLKAEEK KRETASVLVN YRALYPFEAR NHDEMSFNSG 

       790        800        810        820        830        840 
DIIQVDEKTV GEPGWLYGSF QGNFGWFPCN YVEKMPSSEN EKAVSPKKAL LPPTVSLSAT 

       850        860        870        880        890        900 
STSSEPLSSN QPASVTDYQN VSFSNLTVNT SWQKKSAFTR TVSPGSVSPI HGQGQVVENL 

       910        920        930        940        950        960 
KAQALCSWTA KKDNHLNFSK HDIITVLEQQ ENWWFGEVHG GRGWFPKSYV KIIPGSEVKR 

       970        980        990       1000       1010       1020 
EEPEALYAAV NKKPTSAAYS VGEEYIALYP YSSVEPGDLT FTEGEEILVT QKDGEWWTGS 

      1030       1040       1050       1060       1070       1080 
IGDRSGIFPS NYVKPKDQES FGSASKSGAS NKKPEIAQVT SAYVASGSEQ LSLAPGQLIL 

      1090       1100       1110       1120       1130       1140 
ILKKNTSGWW QGELQARGKK RQKGWFPASH VKLLGPSSER ATPAFHPVCQ VIAMYDYAAN 

      1150       1160       1170       1180       1190       1200 
NEDELSFSKG QLINVMNKDD PDWWQGEING VTGLFPSNYV KMTTDSDPSQ QWCADLQTLD 

      1210       1220       1230       1240       1250       1260 
TMQPIERKRQ GYIHELIQTE ERYMADLQLV VEVFQKRMAE SGFLTEGEMA LIFVNWKELI 

      1270       1280       1290       1300       1310       1320 
MSNTKLLKAL RVRKKTGGEK MPVQMIGDIL AAELSHMQAY IRFCSCQLNG AALLQQKTDE 

      1330       1340       1350       1360       1370       1380 
DTDFKEFLKK LASDPRCKGM PLSSFLLKPM QRITRYPLLI RSILENTPES HADHSSLKLA 

      1390       1400       1410       1420       1430       1440 
LERAEELCSQ VNEGVREKEN SDRLEWIQAH VQCEGLAEQL IFNSLTNCLG PRKLLHSGKL 

      1450       1460       1470       1480       1490       1500 
YKTKSNKELH GFLFNDFLLL TYMVKQFAVS SGSEKLFSSK SNAQFKMYKT PIFLNEVLVK 

      1510       1520       1530       1540       1550       1560 
LPTDPSSDEP VFHISHIDRV YTLRTDNINE RTAWVQKIKA ASEQYIDTEK KKREKAYQAR 

      1570       1580       1590       1600       1610       1620 
SQKTSGIGRL MVHVIEATEL KACKPNGKSN PYCEISMGSQ SYTTRTIQDT LNPKWNFNCQ 

      1630       1640       1650       1660       1670       1680 
FFIKDLYQDV LCLTLFDRDQ FSPDDFLGRT EIPVAKIRTE QESKGPMTRR LLLHEVPTGE 

      1690 
VWVRFDLQLF EQKTLL 

« Hide

Isoform 2.

Checksum: DB55C4E85BAE5EF1
Show »

FASTA1,669190,365
Isoform 3 (ITSN2-S1).

Checksum: A325BC186C76A97D
Show »

FASTA1,248141,719
Isoform 4 (ITSN2-S2) (SH3P18).

Checksum: 1334FA0B1BF2BB3F
Show »

FASTA1,191135,013

References

« Hide 'large scale' references
[1]"Intersectin 2, a new multimodular protein involved in clathrin-mediated endocytosis."
Pucharcos C., Estivill X., de la Luna S.
FEBS Lett. 478:43-51(2000) [PubMed: 10922467] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
Tissue: Fetal brain and Fetal liver.
[2]"Intersectin 2 (SH3D1B), human homolog of mouse Ese2 protein."
Seifert M., Engel M., Welter C.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed: 10574462] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-720 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1261-1696, VARIANT ILE-290.
Tissue: Embryo.
[5]"SH3P18-like wasp associated protein (SWAP): a multiple SH3 domain containing protein that interacts with WASP."
Wilson L.A., Fields D., Cruz L., Friesen J., Siminovitch K.A.
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 821-1284 (ISOFORM 1).
[6]"Cloning of ligand targets: systematic isolation of SH3 domain-containing proteins."
Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.
Nat. Biotechnol. 14:741-744(1996) [PubMed: 9630982] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 944-1191 (ISOFORM 4).
Tissue: Bone marrow.
[7]"The human intersectin genes and their spliced variants are differentially expressed."
Pucharcos C., Casas C., Nadal M., Estivill X., de la Luna S.
Biochim. Biophys. Acta 1521:1-11(2001) [PubMed: 11690630] [Abstract]
Cited for: ALTERNATIVE SPLICING.
Tissue: Brain and Fetal liver.
[8]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-967, MASS SPECTROMETRY.
Tissue: T-cell.
[9]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-552, MASS SPECTROMETRY.
Tissue: Epithelium.
[10]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-858 AND TYR-967, MASS SPECTROMETRY.
[11]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-552, MASS SPECTROMETRY.
[12]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883 AND SER-888, MASS SPECTROMETRY.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883 AND SER-888, MASS SPECTROMETRY.
[14]"Solution structure of SH3 domains of human intersectin 2 (KIAA1256)."
RIKEN structural genomics initiative (RSGI)
Submitted (AUG-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 761-1186.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF182198 mRNA. Translation: AAF59903.1.
AF182199 mRNA. Translation: AAF59904.1.
AF248540 mRNA. Translation: AAF63600.1. Different initiation.
AB033082 mRNA. Translation: BAA86570.1. Different initiation.
AK021545 mRNA. Translation: BAB13841.1.
AK000302 mRNA. Translation: BAA91068.1.
AF001630 mRNA. Translation: AAD00899.1.
U61167 mRNA. Translation: AAC50593.1.
IPIIPI00216423.
IPI00396534.
IPI00414027.
IPI00892957.
RefSeqNP_006268.2.
NP_062541.3.
NP_671494.2.
UniGeneHs.432562

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1J3TNMR-A897-957[»]
1UDLNMR-A1102-1186[»]
1UE9NMR-A1055-1121[»]
1UFFNMR-A761-841[»]
1UHFNMR-A982-1037[»]
3GF9X-ray2.50A1129-1405[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9NZM3. 9 interactions.

PTM databases

PhosphoSiteQ9NZM3.

Proteomic databases

PRIDEQ9NZM3.

Genome annotation databases

EnsemblENSG00000198399. Homo sapiens. [Contig view]
GeneID50618.
KEGGhsa:50618.
UCSCuc002rfe.1. human.
uc002rff.1. human.
uc002rfg.1. human.

Organism-specific databases

GeneCardsGC02M024337.
H-InvDBHIX0001876.
HGNCHGNC:6184. ITSN2.
MIM604464. gene.
PharmGKBPA29982.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9NZM3.
OMAQ9NZM3. LTVNTSW.

Gene expression databases

ArrayExpressQ9NZM3.
BgeeQ9NZM3.
CleanExHS_ITSN2.
GermOnlineENSG00000198399. Homo sapiens.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR018029. C2_membr_targeting.
IPR000219. DH-domain.
IPR011992. EF-Hand_type.
IPR018248. EF_hand.
IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR000261. EPS15_homology.
IPR000108. Neu_cyt_fact_2.
IPR011993. PH_type.
IPR001849. Pleckstrin_homology.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 2 hits.
G3DSA:2.30.29.30. PH_type. 1 hit.
G3DSA:1.20.900.10. RhoGEF. 1 hit.
PfamPF00168. C2. 1 hit.
PF00036. efhand. 2 hits.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00018. SH3_1. 4 hits.
PF07653. SH3_2. 1 hit.
[Graphical view]
PRINTSPR00499. P67PHOX.
ProDomPD000012. EF-hand. 1 hit.
PD000066. SH3. 5 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00239. 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]
PROSITEPS50004. C2. 1 hit.
PS50010. DH_2. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS50031. EH. 2 hits.
PS50003. PH_DOMAIN. 1 hit.
PS50002. SH3. 5 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio53140.
SOURCESearch...

Entry information

Entry nameITSN2_HUMAN
AccessionPrimary (citable) accession number: Q9NZM3
Secondary accession number(s): O95062 expand/collapse secondary AC list , Q15812, Q9HAK4, Q9NXE6, Q9NYG0, Q9NZM2, Q9ULG4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: April 3, 2002
Last modified: July 7, 2009
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents