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Q9NZM3 (ITSN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1697 AA.
Sequence statusComplete.
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 (CCPs). Seems to be involved in CCPs maturation including invagination or budding. Involved in endocytosis of integrin beta-1 (ITGB1) and transferrin receptor (TFR). Ref.15 Ref.20

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. Interacts with ADAM15. Interacts with FASLG. Interacts with ANKRD54 By similarity. Interacts with FCHO2. Ref.13 Ref.14 Ref.18

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 1 EF-hand domain.

Contains 2 EH domains.

Contains 1 PH domain.

Contains 5 SH3 domains.

Caution

It is uncertain whether Met-1 or Met-2 is the initiator.

Studies in clathrin-mediated endocytosis of ITGB1 and TFR used a siRNA mixture of ISTN1 and ISTN2 suggesting a partially overlapping role of the EH domain-containing proteins (Ref.20).

Sequence caution

The sequence AAF59903.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAF59904.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAF63600.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA86570.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

K15-MQ9WNA92EBI-308689,EBI-7555439From a different organism.

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:
     622-648: Missing.
Isoform 3 (identifier: Q9NZM3-3)

Also known as: ITSN2-S1;

The sequence of this isoform differs from the canonical sequence as follows:
     1235-1249: FQKRMAESGFLTEGE → RRLLLASSRGICCLS
     1250-1697: Missing.
Isoform 4 (identifier: Q9NZM3-4)

Also known as: ITSN2-S2; SH3P18;

The sequence of this isoform differs from the canonical sequence as follows:
     1193-1697: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16971697Intersectin-2
PRO_0000080961

Regions

Domain22 – 11089EH 1
Domain54 – 8936EF-hand
Domain244 – 33390EH 2
Domain757 – 81862SH3 1
Domain898 – 95659SH3 2
Domain981 – 103959SH3 3
Domain1053 – 111765SH3 4
Domain1127 – 118660SH3 5
Domain1209 – 1395187DH
Domain1434 – 1544111PH
Domain1556 – 165297C2
Calcium binding67 – 7913 Potential
Coiled coil361 – 756396 Potential

Amino acid modifications

Modified residue2101Phosphoserine Ref.16
Modified residue2301Phosphoserine Ref.17
Modified residue5531Phosphotyrosine By similarity
Modified residue5731Phosphothreonine Ref.17
Modified residue8841Phosphoserine By similarity
Modified residue8891Phosphoserine Ref.12 Ref.16 Ref.17
Modified residue9681Phosphotyrosine Ref.9 Ref.10 Ref.16 Ref.17

Natural variations

Alternative sequence622 – 64827Missing in isoform 2.
VSP_003892
Alternative sequence1193 – 1697505Missing in isoform 4.
VSP_003895
Alternative sequence1235 – 124915FQKRM…LTEGE → RRLLLASSRGICCLS in isoform 3.
VSP_003893
Alternative sequence1250 – 1697448Missing in isoform 3.
VSP_003894
Natural variant2541T → A.
Corresponds to variant rs6744320 [ dbSNP | Ensembl ].
VAR_024287
Natural variant2911V → I. Ref.5
Corresponds to variant rs7603997 [ dbSNP | Ensembl ].
VAR_024288
Natural variant12871I → T.
Corresponds to variant rs3731625 [ dbSNP | Ensembl ].
VAR_020193
Natural variant15341A → T.
Corresponds to variant rs2303291 [ dbSNP | Ensembl ].
VAR_021937

Experimental info

Sequence conflict6791R → G in BAB13841. Ref.5
Sequence conflict823 – 8286KAVSPK → FAAAST in AAD00899. Ref.6
Sequence conflict945 – 9517WFPKSYV → EFAAAST in AAC50593. Ref.7
Sequence conflict1279 – 12857GEKMPVQ → VDAAANS in AAD00899. Ref.6
Sequence conflict15531K → Q in AAF63600. Ref.2
Sequence conflict15531K → Q in BAA86570. Ref.3
Isoform 3:
Sequence conflict12351R → W in AAF59904. Ref.1

Secondary structure

......................................................................................................... 1697
Helix Strand Turn

Details...

Sequences

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

Last modified April 20, 2010. Version 3.
Checksum: 49C41AE1E32E1BD0

FASTA1,697193,461
        10         20         30         40         50         60 
MMAQFPTAMN GGPNMWAITS EERTKHDRQF DNLKPSGGYI TGDQARNFFL QSGLPAPVLA 

        70         80         90        100        110        120 
EIWALSDLNK DGKMDQQEFS IAMKLIKLKL QGQQLPVVLP PIMKQPPMFS PLISARFGMG 

       130        140        150        160        170        180 
SMPNLSIPQP LPPAAPITSL SSATSGTNLP PLMMPTPLVP SVSTSSLPNG TASLIQPLPI 

       190        200        210        220        230        240 
PYSSSTLPHG SSYSLMMGGF GGASIQKAQS LIDLGSSSST SSTASLSGNS PKTGTSEWAV 

       250        260        270        280        290        300 
PQPTRLKYRQ KFNTLDKSMS GYLSGFQARN ALLQSNLSQT QLATIWTLAD VDGDGQLKAE 

       310        320        330        340        350        360 
EFILAMHLTD MAKAGQPLPL TLPPELVPPS FRGGKQIDSI NGTLPSYQKM QEEEPQKKLP 

       370        380        390        400        410        420 
VTFEDKRKAN YERGNMELEK RRQALMEQQQ REAERKAQKE KEEWERKQRE LQEQEWKKQL 

       430        440        450        460        470        480 
ELEKRLEKQR ELERQREEER RKDIERREAA KQELERQRRL EWERIRRQEL LNQKNREQEE 

       490        500        510        520        530        540 
IVRLNSKKKN LHLELEALNG KHQQISGRLQ DVRLKKQTQK TELEVLDKQC DLEIMEIKQL 

       550        560        570        580        590        600 
QQELQEYQNK LIYLVPEKQL LNERIKNMQF SNTPDSGVSL LHKKSLEKEE LCQRLKEQLD 

       610        620        630        640        650        660 
ALEKETASKL SEMDSFNNQL KCGNMDDSVL QCLLSLLSCL NNLFLLLKEL RETYNTQQLA 

       670        680        690        700        710        720 
LEQLYKIKRD KLKEIERKRL ELMQKKKLED EAARKAKQGK ENLWKENLRK EEEEKQKRLQ 

       730        740        750        760        770        780 
EEKTQEKIQE EERKAEEKQR KDKDTLKAEE KKRETASVLV NYRALYPFEA RNHDEMSFNS 

       790        800        810        820        830        840 
GDIIQVDEKT VGEPGWLYGS FQGNFGWFPC NYVEKMPSSE NEKAVSPKKA LLPPTVSLSA 

       850        860        870        880        890        900 
TSTSSEPLSS NQPASVTDYQ NVSFSNLTVN TSWQKKSAFT RTVSPGSVSP IHGQGQVVEN 

       910        920        930        940        950        960 
LKAQALCSWT AKKDNHLNFS KHDIITVLEQ QENWWFGEVH GGRGWFPKSY VKIIPGSEVK 

       970        980        990       1000       1010       1020 
REEPEALYAA VNKKPTSAAY SVGEEYIALY PYSSVEPGDL TFTEGEEILV TQKDGEWWTG 

      1030       1040       1050       1060       1070       1080 
SIGDRSGIFP SNYVKPKDQE SFGSASKSGA SNKKPEIAQV TSAYVASGSE QLSLAPGQLI 

      1090       1100       1110       1120       1130       1140 
LILKKNTSGW WQGELQARGK KRQKGWFPAS HVKLLGPSSE RATPAFHPVC QVIAMYDYAA 

      1150       1160       1170       1180       1190       1200 
NNEDELSFSK GQLINVMNKD DPDWWQGEIN GVTGLFPSNY VKMTTDSDPS QQWCADLQTL 

      1210       1220       1230       1240       1250       1260 
DTMQPIERKR QGYIHELIQT EERYMADLQL VVEVFQKRMA ESGFLTEGEM ALIFVNWKEL 

      1270       1280       1290       1300       1310       1320 
IMSNTKLLKA LRVRKKTGGE KMPVQMIGDI LAAELSHMQA YIRFCSCQLN GAALLQQKTD 

      1330       1340       1350       1360       1370       1380 
EDTDFKEFLK KLASDPRCKG MPLSSFLLKP MQRITRYPLL IRSILENTPE SHADHSSLKL 

      1390       1400       1410       1420       1430       1440 
ALERAEELCS QVNEGVREKE NSDRLEWIQA HVQCEGLAEQ LIFNSLTNCL GPRKLLHSGK 

      1450       1460       1470       1480       1490       1500 
LYKTKSNKEL HGFLFNDFLL LTYMVKQFAV SSGSEKLFSS KSNAQFKMYK TPIFLNEVLV 

      1510       1520       1530       1540       1550       1560 
KLPTDPSSDE PVFHISHIDR VYTLRTDNIN ERTAWVQKIK AASEQYIDTE KKKREKAYQA 

      1570       1580       1590       1600       1610       1620 
RSQKTSGIGR LMVHVIEATE LKACKPNGKS NPYCEISMGS QSYTTRTIQD TLNPKWNFNC 

      1630       1640       1650       1660       1670       1680 
QFFIKDLYQD VLCLTLFDRD QFSPDDFLGR TEIPVAKIRT EQESKGPMTR RLLLHEVPTG 

      1690 
EVWVRFDLQL FEQKTLL 

« Hide

Isoform 2 [UniParc].

Checksum: 91E65C08E5AB26F1
Show »

FASTA1,670190,496
Isoform 3 (ITSN2-S1) [UniParc].

Checksum: 271797AF71A0EB28
Show »

FASTA1,249141,820
Isoform 4 (ITSN2-S2) (SH3P18) [UniParc].

Checksum: 2DA2049587CF4082
Show »

FASTA1,192135,144

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-721 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1262-1697, VARIANT ILE-291.
Tissue: Embryo.
[6]"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 822-1285 (ISOFORM 1).
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 945-1192 (ISOFORM 4).
Tissue: Bone marrow.
[8]"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] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING.
Tissue: Brain and Fetal liver.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-968, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-968, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-889, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[14]"Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins."
Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.
J. Cell. Biochem. 108:877-885(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAM15.
[15]"Endocytic accessory proteins are functionally distinguished by their differential effects on the maturation of clathrin-coated pits."
Mettlen M., Stoeber M., Loerke D., Antonescu C.N., Danuser G., Schmid S.L.
Mol. Biol. Cell 20:3251-3260(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-889 AND TYR-968, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; THR-573; SER-889 AND TYR-968, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"The clathrin adaptor Dab2 recruits EH domain scaffold proteins to regulate integrin beta1 endocytosis."
Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.
Mol. Biol. Cell 23:2905-2916(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"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 762-1187.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF182198 mRNA. Translation: AAF59903.1. Different initiation.
AF182199 mRNA. Translation: AAF59904.1. Different initiation.
AF248540 mRNA. Translation: AAF63600.1. Different initiation.
AB033082 mRNA. Translation: BAA86570.1. Different initiation.
AC008073 Genomic DNA. No translation available.
AC009228 Genomic DNA. No translation available.
AK021545 mRNA. Translation: BAB13841.1.
AK000302 mRNA. Translation: BAA91068.1.
AF001630 mRNA. Translation: AAD00899.1.
U61167 mRNA. Translation: AAC50593.1.
CCDSCCDS1710.2. [Q9NZM3-1]
CCDS1711.2. [Q9NZM3-2]
CCDS46230.1. [Q9NZM3-3]
RefSeqNP_006268.2. NM_006277.2. [Q9NZM3-1]
NP_062541.3. NM_019595.3. [Q9NZM3-2]
NP_671494.2. NM_147152.2. [Q9NZM3-3]
UniGeneHs.432562.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J3TNMR-A898-958[»]
1UDLNMR-A1103-1187[»]
1UE9NMR-A1056-1122[»]
1UFFNMR-A762-842[»]
1UHFNMR-A983-1038[»]
3GF9X-ray2.50A1130-1406[»]
3JZYX-ray1.56A1201-1692[»]
4IIOX-ray1.70A/B901-955[»]
ProteinModelPortalQ9NZM3.
SMRQ9NZM3. Positions 2-108, 236-332, 762-845, 901-1551, 1568-1691.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119098. 79 interactions.
IntActQ9NZM3. 24 interactions.
MINTMINT-1404321.
STRING9606.ENSP00000347244.

PTM databases

PhosphoSiteQ9NZM3.

Polymorphism databases

DMDM294862505.

Proteomic databases

MaxQBQ9NZM3.
PaxDbQ9NZM3.
PRIDEQ9NZM3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355123; ENSP00000347244; ENSG00000198399. [Q9NZM3-1]
ENST00000361999; ENSP00000354561; ENSG00000198399. [Q9NZM3-2]
ENST00000406921; ENSP00000384499; ENSG00000198399. [Q9NZM3-3]
GeneID50618.
KEGGhsa:50618.
UCSCuc002rfe.2. human. [Q9NZM3-1]
uc002rff.2. human. [Q9NZM3-2]
uc002rfg.3. human. [Q9NZM3-3]

Organism-specific databases

CTD50618.
GeneCardsGC02M024425.
H-InvDBHIX0001876.
HGNCHGNC:6184. ITSN2.
HPAHPA036475.
MIM604464. gene.
neXtProtNX_Q9NZM3.
PharmGKBPA29982.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5422.
HOVERGENHBG052159.
InParanoidQ9NZM3.
OMAWQQKSAF.
OrthoDBEOG7WMCJ3.
PhylomeDBQ9NZM3.
TreeFamTF324293.

Gene expression databases

ArrayExpressQ9NZM3.
BgeeQ9NZM3.
CleanExHS_ITSN2.
GenevestigatorQ9NZM3.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
InterProIPR000008. C2_dom.
IPR000219. DH-domain.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000261. EPS15_homology.
IPR027029. Intersectin-2.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERPTHR11216:SF29. PTHR11216:SF29. 1 hit.
PfamPF00168. C2. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00018. SH3_1. 2 hits.
PF07653. SH3_2. 1 hit.
PF14604. SH3_9. 2 hits.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
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]
SUPFAMSSF48065. SSF48065. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 5 hits.
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

EvolutionaryTraceQ9NZM3.
GeneWikiITSN2.
GenomeRNAi50618.
NextBio53140.
PROQ9NZM3.
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 20, 2010
Last modified: July 9, 2014
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

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