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Q15811 (ITSN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 155. 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-1
Alternative name(s):
SH3 domain-containing protein 1A
SH3P17
Gene names
Name:ITSN1
Synonyms:ITSN, SH3D1A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1721 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as guanine nucleotide exchange factor (GEF) specific for the CDC42 GTPase By similarity. 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. Isoform 1 could be involved in brain-specific synaptic vesicle recycling. Inhibits ARHGAP31 activity toward RAC1. Ref.12 Ref.21

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.12 Ref.15 Ref.17 Ref.19 Ref.21 Ref.22

Subcellular location

Endomembrane system By similarity. Cell junctionsynapsesynaptosome By similarity. Cell projectionlamellipodium. Membraneclathrin-coated pit. Note: Colocalizes with SGIP1 at the plasma membrane in structures corresponding most problably to clathrin-coated pits Probable. Ref.12 Ref.17

Tissue specificity

Isoform 2 is ubiquitous in adult and fetal tissues with high expression in skeletal muscle, heart, spleen, ovary, testis and all fetal tissues tested and low expression in thymus, blood, lung, liver and pancreas. Isoform 1 is expressed almost exclusively in the brain, in all brain regions. Not expressed in the spinal cord.

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.

In an autoinhibited form the SH3 domain 5 may bind intramolecularly to the DH domain, thus blocking the CDC42-binding site By similarity.

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.

Caution

Studies in clathrin-mediated endocytosis of ITGB1 and TFR used a siRNA mixture of ISTN1 and ISTN2, and a Dab2 mutant with impaired binding to EH domain-containing proteins EPS15 and ITSN1 suggesting a partially overlapping role of the EH domain-containing proteins (Ref.21).

Sequence caution

The sequence AAC50592.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell junction
Cell projection
Coated pit
Membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
SH3 domain
   LigandCalcium
Metal-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic signaling pathway

Traceable author statement. Source: Reactome

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

regulation of GTPase activity

Non-traceable author statement Ref.1. Source: GOC

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

synaptic vesicle endocytosis

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

coated pit

Inferred from direct assay Ref.17. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.17. Source: UniProtKB

synapse

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionRho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

calcium ion binding

Non-traceable author statement Ref.1. Source: UniProtKB

guanyl-nucleotide exchange factor activity

Non-traceable author statement Ref.1. Source: UniProtKB

kinase activator activity

Inferred from electronic annotation. Source: Ensembl

proline-rich region binding

Inferred from physical interaction Ref.17. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18692052PubMed 19166927. Source: IntAct

protein complex scaffold

Inferred from direct assay Ref.17. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 13 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist. Alternative splicing affects domains involved in protein recognition and thus may play a role in selecting specific interactions.
Isoform 1 (identifier: Q15811-1)

Also known as: Long; ITSN-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: Q15811-2)

Also known as: Short; ITSN-s;

The sequence of this isoform differs from the canonical sequence as follows:
     1221-1721: Missing.
Isoform 3 (identifier: Q15811-3)

Also known as: Short 2; SH3P17;

The sequence of this isoform differs from the canonical sequence as follows:
     770-774: Missing.
     1006-1076: Missing.
     1221-1721: Missing.
Isoform 4 (identifier: Q15811-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1006-1076: Missing.
Isoform 5 (identifier: Q15811-5)

Also known as: ITSN1-22a;

The sequence of this isoform differs from the canonical sequence as follows:
     770-774: Missing.
     910-1025: GEKVEGLQAQ...SEQGDLTFQQ → PDFLLHPSMR...CFYLCLPHYL
     1026-1721: Missing.
Isoform 6 (identifier: Q15811-6)

Also known as: Long form variant 4; Short form variant 11;

The sequence of this isoform differs from the canonical sequence as follows:
     770-774: Missing.
     1006-1020: EFIAMYTYESSEQGD → GLWNCWENREFRKKT
     1021-1721: Missing.
Note: Contains a premature stop codon, potentially subjected to NMD.
Isoform 7 (identifier: Q15811-7)

Also known as: Short form variant 5;

The sequence of this isoform differs from the canonical sequence as follows:
     770-774: Missing.
     1221-1721: Missing.
Isoform 8 (identifier: Q15811-8)

Also known as: Long form variant 2;

The sequence of this isoform differs from the canonical sequence as follows:
     770-774: Missing.
Isoform 9 (identifier: Q15811-9)

Also known as: Long form variant 3;

The sequence of this isoform differs from the canonical sequence as follows:
     770-774: Missing.
     1392-1447: Missing.
Isoform 10 (identifier: Q15811-10)

Also known as: Short form variant 2;

The sequence of this isoform differs from the canonical sequence as follows:
     116-152: Missing.
     770-774: Missing.
     1221-1721: Missing.
Isoform 11 (identifier: Q15811-11)

Also known as: Short form variant 3;

The sequence of this isoform differs from the canonical sequence as follows:
     116-152: Missing.
     1006-1076: Missing.
     1221-1721: Missing.
Isoform 12 (identifier: Q15811-12)

Also known as: Short form variant 10;

The sequence of this isoform differs from the canonical sequence as follows:
     116-152: Missing.
     770-774: Missing.
     1006-1076: Missing.
     1221-1721: Missing.
Isoform 13 (identifier: Q15811-13)

Also known as: Short form variant 14;

The sequence of this isoform differs from the canonical sequence as follows:
     770-774: Missing.
     910-919: GEKVEGLQAQ → HGFWFFRESC
     920-1721: Missing.
Note: Contains a premature stop codon, potentially subjected to NMD.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17211721Intersectin-1
PRO_0000080957

Regions

Domain21 – 10989EH 1
Domain53 – 8836EF-hand 1
Domain221 – 31090EH 2
Domain254 – 28936EF-hand 2
Domain740 – 80667SH3 1
Domain913 – 97159SH3 2
Domain1002 – 106059SH3 3
Domain1074 – 113865SH3 4
Domain1155 – 121460SH3 5
Domain1237 – 1423187DH
Domain1462 – 1571110PH
Domain1583 – 167997C2
Calcium binding66 – 77121 Potential
Calcium binding267 – 278122 Potential
Region326 – 702377KLERQ
Coiled coil351 – 705355 Potential

Amino acid modifications

Modified residue2031Phosphoserine By similarity
Modified residue9021Phosphoserine Ref.13
Modified residue9041Phosphoserine Ref.13
Modified residue11371Phosphoserine By similarity

Natural variations

Alternative sequence116 – 15237Missing in isoform 10, isoform 11 and isoform 12.
VSP_053317
Alternative sequence770 – 7745Missing in isoform 3, isoform 5, isoform 6, isoform 7, isoform 8, isoform 9, isoform 10, isoform 12 and isoform 13.
VSP_004293
Alternative sequence910 – 1025116GEKVE…LTFQQ → PDFLLHPSMRLGHMQPRIVL LFPDPLQCSTSRLLPMLRPR PGVPFLRSPSCQSPSHPSRP ISDAAPSVKFTLMPPGRIHP CFLFIPAVNSRNSFLVYFIL PGGTLGCFYLCLPHYL in isoform 5.
VSP_047460
Alternative sequence910 – 91910GEKVEGLQAQ → HGFWFFRESC in isoform 13.
VSP_053318
Alternative sequence920 – 1721802Missing in isoform 13.
VSP_053319
Alternative sequence1006 – 107671Missing in isoform 3, isoform 4, isoform 11 and isoform 12.
VSP_004294
Alternative sequence1006 – 102015EFIAM…SEQGD → GLWNCWENREFRKKT in isoform 6.
VSP_053320
Alternative sequence1021 – 1721701Missing in isoform 6.
VSP_053321
Alternative sequence1026 – 1721696Missing in isoform 5.
VSP_047461
Alternative sequence1221 – 1721501Missing in isoform 2, isoform 3, isoform 7, isoform 10, isoform 11 and isoform 12.
VSP_004295
Alternative sequence1392 – 144756Missing in isoform 9.
VSP_053322
Natural variant11371S → N. Ref.1 Ref.3
Corresponds to variant rs187895245 [ dbSNP | Ensembl ].
VAR_070011

Experimental info

Mutagenesis13691M → L: Decreases specificity for CDC42; when associated with I-1376. Ref.23
Mutagenesis13761L → I: Decreases specificity for CDC42; when associated with L-1369. Ref.23
Sequence conflict1141A → P in AAC78610. Ref.1
Sequence conflict1141A → P in AAC78611. Ref.1
Sequence conflict1141A → P in ABG74695. Ref.3
Sequence conflict1141A → P in ABG74697. Ref.3
Sequence conflict1141A → P in ABG74698. Ref.3
Sequence conflict8631E → G in ABD72328. Ref.4
Sequence conflict10881T → A in AAD53183. Ref.9
Sequence conflict11091G → R in AAD53183. Ref.9
Sequence conflict13611A → E in AAC78611. Ref.1
Sequence conflict13611A → E in AAC50592. Ref.8
Sequence conflict13671K → R in AAI16187. Ref.7
Sequence conflict14741S → N in AAC78611. Ref.1
Sequence conflict14741S → N in AAC50592. Ref.8

Secondary structure

............................................................................................. 1721
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) (ITSN-l) [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: FC4DE644D8BEA2BE

FASTA1,721195,422
        10         20         30         40         50         60 
MAQFPTPFGG SLDIWAITVE ERAKHDQQFH SLKPISGFIT GDQARNFFFQ SGLPQPVLAQ 

        70         80         90        100        110        120 
IWALADMNND GRMDQVEFSI AMKLIKLKLQ GYQLPSALPP VMKQQPVAIS SAPAFGMGGI 

       130        140        150        160        170        180 
ASMPPLTAVA PVPMGSIPVV GMSPTLVSSV PTAAVPPLAN GAPPVIQPLP AFAHPAATLP 

       190        200        210        220        230        240 
KSSSFSRSGP GSQLNTKLQK AQSFDVASVP PVAEWAVPQS SRLKYRQLFN SHDKTMSGHL 

       250        260        270        280        290        300 
TGPQARTILM QSSLPQAQLA SIWNLSDIDQ DGKLTAEEFI LAMHLIDVAM SGQPLPPVLP 

       310        320        330        340        350        360 
PEYIPPSFRR VRSGSGISVI SSTSVDQRLP EEPVLEDEQQ QLEKKLPVTF EDKKRENFER 

       370        380        390        400        410        420 
GNLELEKRRQ ALLEQQRKEQ ERLAQLERAE QERKERERQE QERKRQLELE KQLEKQRELE 

       430        440        450        460        470        480 
RQREEERRKE IERREAAKRE LERQRQLEWE RNRRQELLNQ RNKEQEDIVV LKAKKKTLEF 

       490        500        510        520        530        540 
ELEALNDKKH QLEGKLQDIR CRLTTQRQEI ESTNKSRELR IAEITHLQQQ LQESQQMLGR 

       550        560        570        580        590        600 
LIPEKQILND QLKQVQQNSL HRDSLVTLKR ALEAKELARQ HLRDQLDEVE KETRSKLQEI 

       610        620        630        640        650        660 
DIFNNQLKEL REIHNKQQLQ KQKSMEAERL KQKEQERKII ELEKQKEEAQ RRAQERDKQW 

       670        680        690        700        710        720 
LEHVQQEDEH QRPRKLHEEE KLKREESVKK KDGEEKGKQE AQDKLGRLFH QHQEPAKPAV 

       730        740        750        760        770        780 
QAPWSTAEKG PLTISAQENV KVVYYRALYP FESRSHDEIT IQPGDIVMVK GEWVDESQTG 

       790        800        810        820        830        840 
EPGWLGGELK GKTGWFPANY AEKIPENEVP APVKPVTDST SAPAPKLALR ETPAPLAVTS 

       850        860        870        880        890        900 
SEPSTTPNNW ADFSSTWPTS TNEKPETDNW DAWAAQPSLT VPSAGQLRQR SAFTPATATG 

       910        920        930        940        950        960 
SSPSPVLGQG EKVEGLQAQA LYPWRAKKDN HLNFNKNDVI TVLEQQDMWW FGEVQGQKGW 

       970        980        990       1000       1010       1020 
FPKSYVKLIS GPIRKSTSMD SGSSESPASL KRVASPAAKP VVSGEEFIAM YTYESSEQGD 

      1030       1040       1050       1060       1070       1080 
LTFQQGDVIL VTKKDGDWWT GTVGDKAGVF PSNYVRLKDS EGSGTAGKTG SLGKKPEIAQ 

      1090       1100       1110       1120       1130       1140 
VIASYTATGP EQLTLAPGQL ILIRKKNPGG WWEGELQARG KKRQIGWFPA NYVKLLSPGT 

      1150       1160       1170       1180       1190       1200 
SKITPTEPPK STALAAVCQV IGMYDYTAQN DDELAFNKGQ IINVLNKEDP DWWKGEVNGQ 

      1210       1220       1230       1240       1250       1260 
VGLFPSNYVK LTTDMDPSQQ WCSDLHLLDM LTPTERKRQG YIHELIVTEE NYVNDLQLVT 

      1270       1280       1290       1300       1310       1320 
EIFQKPLMES ELLTEKEVAM IFVNWKELIM CNIKLLKALR VRKKMSGEKM PVKMIGDILS 

      1330       1340       1350       1360       1370       1380 
AQLPHMQPYI RFCSRQLNGA ALIQQKTDEA PDFKEFVKRL AMDPRCKGMP LSSFILKPMQ 

      1390       1400       1410       1420       1430       1440 
RVTRYPLIIK NILENTPENH PDHSHLKHAL EKAEELCSQV NEGVREKENS DRLEWIQAHV 

      1450       1460       1470       1480       1490       1500 
QCEGLSEQLV FNSVTNCLGP RKFLHSGKLY KAKSNKELYG FLFNDFLLLT QITKPLGSSG 

      1510       1520       1530       1540       1550       1560 
TDKVFSPKSN LQYKMYKTPI FLNEVLVKLP TDPSGDEPIF HISHIDRVYT LRAESINERT 

      1570       1580       1590       1600       1610       1620 
AWVQKIKAAS ELYIETEKKK REKAYLVRSQ RATGIGRLMV NVVEGIELKP CRSHGKSNPY 

      1630       1640       1650       1660       1670       1680 
CEVTMGSQCH ITKTIQDTLN PKWNSNCQFF IRDLEQEVLC ITVFERDQFS PDDFLGRTEI 

      1690       1700       1710       1720 
RVADIKKDQG SKGPVTKCLL LHEVPTGEIV VRLDLQLFDE P 

« Hide

Isoform 2 (Short) (ITSN-s) [UniParc].

Checksum: B09FDBEF1C06F487
Show »

FASTA1,220137,649
Isoform 3 (Short 2) (SH3P17) [UniParc].

Checksum: 8EEE8BE230C2F8C7
Show »

FASTA1,144129,416
Isoform 4 [UniParc].

Checksum: 584F3A7AD02E4434
Show »

FASTA1,650187,788
Isoform 5 (ITSN1-22a) [UniParc].

Checksum: 53D58238CDB49BB4
Show »

FASTA1,020115,873
Isoform 6 (Long form variant 4) (Short form variant 11) [UniParc].

Checksum: 7FAD870DF7E4D42E
Show »

FASTA1,015115,477
Isoform 7 (Short form variant 5) [UniParc].

Checksum: 9610DEBFC4781CED
Show »

FASTA1,215137,049
Isoform 8 (Long form variant 2) [UniParc].

Checksum: A129042F01C34A47
Show »

FASTA1,716194,822
Isoform 9 (Long form variant 3) [UniParc].

Checksum: 715F81F741A346E4
Show »

FASTA1,660188,382
Isoform 10 (Short form variant 2) [UniParc].

Checksum: A344C5964504BDB1
Show »

FASTA1,178133,560
Isoform 11 (Short form variant 3) [UniParc].

Checksum: AB25F8723B3FD22A
Show »

FASTA1,112126,526
Isoform 12 (Short form variant 10) [UniParc].

Checksum: 7724CCE4FA98098A
Show »

FASTA1,107125,926
Isoform 13 (Short form variant 14) [UniParc].

Checksum: 3788E745D07FE820
Show »

FASTA914104,194

References

« Hide 'large scale' references
[1]"Two isoforms of a human intersectin (ITSN) protein are produced by brain-specific alternative splicing in a stop codon."
Guipponi M., Scott H.S., Chen H., Schebesta A., Rossier C., Antonarakis S.E.
Genomics 53:369-376(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANT ASN-1137.
Tissue: Fetal brain.
[2]"Alu-splice cloning of human intersectin (ITSN), a putative multivalent binding protein expressed in proliferating and differentiating neurons and overexpressed in Down syndrome."
Pucharcos C., Fuentes J.-J., Casas C., de la Luna S., Alcantara S., Arbones M.L., Soriano E., Estivill X., Pritchard M.
Eur. J. Hum. Genet. 7:704-712(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]"Structural diversity and differential expression of novel human intersectin 1 isoforms."
Kropyvko S., Gerasymchuk D., Skrypkina I., Dergai M., Dergai O., Nikolaienko O., Rynditch A., Tsyba L.
Mol. Biol. Rep. 37:2789-2796(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 6; 7; 8; 9; 10; 11 AND 12), VARIANT ASN-1137, ALTERNATIVE SPLICING.
Tissue: Brain and Lung.
[4]"Identification and characterization of a novel mammalian isoform of the endocytic adaptor ITSN1."
Dergai M., Skrypkina I., Dergai O., Tsyba L., Novokhatska O., Filonenko V., Drobot L., Rynditch A.
Gene 485:120-129(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
Tissue: Kidney.
[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] (ISOFORM 7).
Tissue: Placenta.
[6]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORMS 1 AND 3).
Tissue: Embryonic stem cell.
[8]"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 620-1721 (ISOFORM 3).
Tissue: Bone marrow.
[9]"Mouse homologs of human chromosome 21 genes."
Tsyba L.O., Kvasha S.M., Skripkina I.Y., Anoprienko O.V., Slavov D., Tassone F., Rynditch A.V., Gardiner K.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 963-1721 (ISOFORM 3).
Tissue: Brain.
[10]"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.
[11]"The SH3D1A gene maps to human chromosome 21q22.1-->q22.2."
Chen H., Antonarakis S.E.
Cytogenet. Cell Genet. 78:213-215(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE MAPPING.
[12]"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: FUNCTION, INTERACTION WITH ARHGAP31, SUBCELLULAR LOCATION.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902 AND SER-904, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated pits."
Dergai O., Novokhatska O., Dergai M., Skrypkina I., Tsyba L., Moreau J., Rynditch A.
Biochem. Biophys. Res. Commun. 402:408-413(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH REPS1 AND SGIP1, SUBCELLULAR LOCATION.
[18]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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.
[20]"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].
[21]"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, INTERACTION WITH DAB2.
[22]"Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCHO1.
[23]"Structural basis for the selective activation of Rho GTPases by Dbl exchange factors."
Snyder J.T., Worthylake D.K., Rossman K.L., Betts L., Pruitt W.M., Siderovski D.P., Der C.J., Sondek J.
Nat. Struct. Biol. 9:468-475(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1229-1581 IN COMPLEX WITH CDC42, MUTAGENESIS OF MET-1369 AND LEU-1376.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF064244 mRNA. Translation: AAC78611.1.
AF064247, AF064245, AF064246 Genomic DNA. Translation: AAC80437.1.
AF064243 mRNA. Translation: AAC78610.1.
AF114488 mRNA. Translation: AAD29953.1.
AF114487 mRNA. Translation: AAD29952.1.
DQ679754 mRNA. Translation: ABG74695.1.
DQ679756 mRNA. Translation: ABG74697.1.
DQ679757 mRNA. Translation: ABG74698.1.
EU117382 mRNA. Translation: ABV21755.1.
EU140799 mRNA. Translation: ABV58335.1.
EU140800 mRNA. Translation: ABV58336.1.
EU120733 mRNA. Translation: ABV24866.1.
EU120734 mRNA. Translation: ABV24867.1.
EU120735 mRNA. Translation: ABV24868.1.
EU152331 mRNA. Translation: ABV69555.1.
DQ386455 mRNA. Translation: ABD72328.1.
AK300274 mRNA. Translation: BAG62034.1.
AP000308 Genomic DNA. No translation available.
AP000309 Genomic DNA. No translation available.
AP000310 Genomic DNA. No translation available.
AP000311 Genomic DNA. No translation available.
AP000312 Genomic DNA. No translation available.
AP000313 Genomic DNA. No translation available.
BC117560 mRNA. Translation: AAI17561.1.
BC116186 mRNA. Translation: AAI16187.1.
U61166 mRNA. Translation: AAC50592.1. Different initiation.
AF180522 mRNA. Translation: AAD53183.1.
CCDSCCDS33545.1. [Q15811-1]
CCDS33546.1. [Q15811-2]
RefSeqNP_001001132.1. NM_001001132.1. [Q15811-2]
NP_003015.2. NM_003024.2. [Q15811-1]
XP_005261083.1. XM_005261026.1. [Q15811-8]
XP_005261084.1. XM_005261027.1. [Q15811-7]
XP_005261088.1. XM_005261031.1. [Q15811-3]
UniGeneHs.160324.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KI1X-ray2.30B/D1229-1581[»]
2KGRNMR-A210-312[»]
2KHNNMR-A1-111[»]
3FIAX-ray1.45A1-111[»]
3QBVX-ray2.65B/D1229-1579[»]
4IIMX-ray1.80A/B916-970[»]
ProteinModelPortalQ15811.
SMRQ15811. Positions 1-111, 210-312, 745-835, 916-1581, 1595-1718.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112351. 120 interactions.
DIPDIP-33609N.
IntActQ15811. 43 interactions.
MINTMINT-130199.
STRING9606.ENSP00000370719.

PTM databases

PhosphoSiteQ15811.

Polymorphism databases

DMDM116242596.

Proteomic databases

MaxQBQ15811.
PaxDbQ15811.
PRIDEQ15811.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379960; ENSP00000369294; ENSG00000205726. [Q15811-13]
ENST00000381291; ENSP00000370691; ENSG00000205726. [Q15811-2]
ENST00000381318; ENSP00000370719; ENSG00000205726. [Q15811-1]
ENST00000399326; ENSP00000382265; ENSG00000205726. [Q15811-6]
ENST00000399338; ENSP00000382275; ENSG00000205726. [Q15811-5]
ENST00000399349; ENSP00000382286; ENSG00000205726. [Q15811-3]
ENST00000399352; ENSP00000382289; ENSG00000205726. [Q15811-7]
ENST00000399353; ENSP00000382290; ENSG00000205726. [Q15811-10]
ENST00000399367; ENSP00000382301; ENSG00000205726. [Q15811-8]
ENST00000437442; ENSP00000387377; ENSG00000205726. [Q15811-9]
GeneID6453.
KEGGhsa:6453.
UCSCuc002ysw.3. human. [Q15811-1]
uc002ysz.3. human. [Q15811-3]

Organism-specific databases

CTD6453.
GeneCardsGC21P035014.
HGNCHGNC:6183. ITSN1.
HPAHPA018007.
MIM602442. gene.
neXtProtNX_Q15811.
PharmGKBPA29981.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5422.
HOVERGENHBG052159.
InParanoidQ15811.
OMAVMVKGEW.
PhylomeDBQ15811.
TreeFamTF324293.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ15811.

Gene expression databases

ArrayExpressQ15811.
BgeeQ15811.
CleanExHS_ITSN1.
GenevestigatorQ15811.

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.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR001452. SH3_domain.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF00621. RhoGEF. 1 hit.
PF14604. SH3_9. 5 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.
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]
ProtoNetSearch...

Other

EvolutionaryTraceQ15811.
GeneWikiITSN1.
GenomeRNAi6453.
NextBio25083.
PROQ15811.
SOURCESearch...

Entry information

Entry nameITSN1_HUMAN
AccessionPrimary (citable) accession number: Q15811
Secondary accession number(s): A7Y322 expand/collapse secondary AC list , A8CTX8, A8CTY3, A8CTY7, A8D7D0, A8DCP3, B4DTM2, E7ERJ1, E9PE44, E9PG01, E9PHV2, O95216, Q0PW94, Q0PW95, Q0PW97, Q14BD3, Q1ED40, Q20BK3, Q9UET5, Q9UK60, Q9UNK1, Q9UNK2, Q9UQ92
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 155 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 21

Human chromosome 21: entries, gene names and cross-references to MIM