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Q9NZM3

- ITSN2_HUMAN

UniProt

Q9NZM3 - ITSN2_HUMAN

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Protein

Intersectin-2

Gene

ITSN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi67 – 7913PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. Rho guanyl-nucleotide exchange factor activity Source: InterPro
  3. SH3/SH2 adaptor activity Source: ProtInc

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. positive regulation of signal transduction Source: GOC
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Intersectin-2
Alternative name(s):
SH3 domain-containing protein 1B
SH3P18
SH3P18-like WASP-associated protein
Gene namesi
Name:ITSN2
Synonyms:KIAA1256, SH3D1B, SWAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6184. ITSN2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29982.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16971697Intersectin-2PRO_0000080961Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei210 – 2101Phosphoserine1 Publication
Modified residuei230 – 2301Phosphoserine1 Publication
Modified residuei553 – 5531PhosphotyrosineBy similarity
Modified residuei573 – 5731Phosphothreonine1 Publication
Modified residuei884 – 8841PhosphoserineBy similarity
Modified residuei889 – 8891Phosphoserine3 Publications
Modified residuei968 – 9681Phosphotyrosine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NZM3.
PaxDbiQ9NZM3.
PRIDEiQ9NZM3.

PTM databases

PhosphoSiteiQ9NZM3.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9NZM3.
CleanExiHS_ITSN2.
ExpressionAtlasiQ9NZM3. baseline and differential.
GenevestigatoriQ9NZM3.

Organism-specific databases

HPAiHPA036475.

Interactioni

Subunit structurei

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.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
K15-MQ9WNA92EBI-308689,EBI-7555439From a different organism.

Protein-protein interaction databases

BioGridi119098. 80 interactions.
IntActiQ9NZM3. 25 interactions.
MINTiMINT-1404321.
STRINGi9606.ENSP00000347244.

Structurei

Secondary structure

1
1697
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi762 – 7665Combined sources
Beta strandi772 – 7743Combined sources
Beta strandi783 – 7864Combined sources
Beta strandi793 – 8019Combined sources
Beta strandi804 – 8096Combined sources
Beta strandi812 – 8154Combined sources
Beta strandi818 – 8214Combined sources
Beta strandi901 – 9077Combined sources
Beta strandi924 – 9318Combined sources
Beta strandi934 – 9396Combined sources
Beta strandi942 – 9476Combined sources
Helixi948 – 9503Combined sources
Beta strandi951 – 9544Combined sources
Beta strandi983 – 9875Combined sources
Beta strandi995 – 9995Combined sources
Beta strandi1007 – 10104Combined sources
Beta strandi1012 – 10143Combined sources
Beta strandi1017 – 10204Combined sources
Beta strandi1027 – 10293Combined sources
Helixi1031 – 10333Combined sources
Beta strandi1056 – 10605Combined sources
Beta strandi1079 – 10857Combined sources
Beta strandi1087 – 10959Combined sources
Beta strandi1104 – 11085Combined sources
Beta strandi1111 – 11144Combined sources
Beta strandi1129 – 11368Combined sources
Beta strandi1153 – 11564Combined sources
Beta strandi1161 – 11666Combined sources
Beta strandi1168 – 11714Combined sources
Beta strandi1180 – 11834Combined sources
Helixi1207 – 123428Combined sources
Helixi1236 – 12427Combined sources
Beta strandi1243 – 12453Combined sources
Helixi1247 – 12548Combined sources
Helixi1257 – 127216Combined sources
Helixi1288 – 12947Combined sources
Helixi1299 – 132123Combined sources
Helixi1323 – 133311Combined sources
Turni1336 – 13405Combined sources
Helixi1343 – 13464Combined sources
Helixi1349 – 136618Combined sources
Helixi1375 – 139319Combined sources
Beta strandi1569 – 158012Combined sources
Beta strandi1592 – 15987Combined sources
Beta strandi1601 – 16044Combined sources
Beta strandi1615 – 162511Combined sources
Turni1627 – 16293Combined sources
Beta strandi1631 – 16388Combined sources
Beta strandi1641 – 16444Combined sources
Beta strandi1647 – 16548Combined sources
Helixi1655 – 166511Combined sources
Beta strandi1670 – 16734Combined sources
Beta strandi1675 – 16795Combined sources
Beta strandi1681 – 169010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9NZM3.
SMRiQ9NZM3. Positions 2-108, 236-332, 762-845, 901-1551, 1568-1691.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZM3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 11089EH 1PROSITE-ProRule annotationAdd
BLAST
Domaini54 – 8936EF-handPROSITE-ProRule annotationAdd
BLAST
Domaini244 – 33390EH 2PROSITE-ProRule annotationAdd
BLAST
Domaini757 – 81862SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini898 – 95659SH3 2PROSITE-ProRule annotationAdd
BLAST
Domaini981 – 103959SH3 3PROSITE-ProRule annotationAdd
BLAST
Domaini1053 – 111765SH3 4PROSITE-ProRule annotationAdd
BLAST
Domaini1127 – 118660SH3 5PROSITE-ProRule annotationAdd
BLAST
Domaini1209 – 1395187DHPROSITE-ProRule annotationAdd
BLAST
Domaini1434 – 1544111PHPROSITE-ProRule annotationAdd
BLAST
Domaini1556 – 165297C2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili361 – 756396Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 2 EH domains.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 5 SH3 domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, SH3 domain

Phylogenomic databases

eggNOGiCOG5422.
GeneTreeiENSGT00760000118985.
HOVERGENiHBG052159.
InParanoidiQ9NZM3.
OMAiWQQKSAF.
OrthoDBiEOG7WMCJ3.
PhylomeDBiQ9NZM3.
TreeFamiTF324293.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
InterProiIPR000008. 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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR11216:SF29. PTHR11216:SF29. 1 hit.
PfamiPF00168. C2. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00018. SH3_1. 2 hits.
PF07653. SH3_2. 1 hit.
PF14604. SH3_9. 2 hits.
[Graphical view]
PRINTSiPR00452. SH3DOMAIN.
SMARTiSM00239. 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]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 5 hits.
PROSITEiPS50004. 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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9NZM3-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MMAQFPTAMN GGPNMWAITS EERTKHDRQF DNLKPSGGYI TGDQARNFFL
60 70 80 90 100
QSGLPAPVLA EIWALSDLNK DGKMDQQEFS IAMKLIKLKL QGQQLPVVLP
110 120 130 140 150
PIMKQPPMFS PLISARFGMG SMPNLSIPQP LPPAAPITSL SSATSGTNLP
160 170 180 190 200
PLMMPTPLVP SVSTSSLPNG TASLIQPLPI PYSSSTLPHG SSYSLMMGGF
210 220 230 240 250
GGASIQKAQS LIDLGSSSST SSTASLSGNS PKTGTSEWAV PQPTRLKYRQ
260 270 280 290 300
KFNTLDKSMS GYLSGFQARN ALLQSNLSQT QLATIWTLAD VDGDGQLKAE
310 320 330 340 350
EFILAMHLTD MAKAGQPLPL TLPPELVPPS FRGGKQIDSI NGTLPSYQKM
360 370 380 390 400
QEEEPQKKLP VTFEDKRKAN YERGNMELEK RRQALMEQQQ REAERKAQKE
410 420 430 440 450
KEEWERKQRE LQEQEWKKQL ELEKRLEKQR ELERQREEER RKDIERREAA
460 470 480 490 500
KQELERQRRL EWERIRRQEL LNQKNREQEE IVRLNSKKKN LHLELEALNG
510 520 530 540 550
KHQQISGRLQ DVRLKKQTQK TELEVLDKQC DLEIMEIKQL QQELQEYQNK
560 570 580 590 600
LIYLVPEKQL LNERIKNMQF SNTPDSGVSL LHKKSLEKEE LCQRLKEQLD
610 620 630 640 650
ALEKETASKL SEMDSFNNQL KCGNMDDSVL QCLLSLLSCL NNLFLLLKEL
660 670 680 690 700
RETYNTQQLA LEQLYKIKRD KLKEIERKRL ELMQKKKLED EAARKAKQGK
710 720 730 740 750
ENLWKENLRK EEEEKQKRLQ EEKTQEKIQE EERKAEEKQR KDKDTLKAEE
760 770 780 790 800
KKRETASVLV NYRALYPFEA RNHDEMSFNS GDIIQVDEKT VGEPGWLYGS
810 820 830 840 850
FQGNFGWFPC NYVEKMPSSE NEKAVSPKKA LLPPTVSLSA TSTSSEPLSS
860 870 880 890 900
NQPASVTDYQ NVSFSNLTVN TSWQKKSAFT RTVSPGSVSP IHGQGQVVEN
910 920 930 940 950
LKAQALCSWT AKKDNHLNFS KHDIITVLEQ QENWWFGEVH GGRGWFPKSY
960 970 980 990 1000
VKIIPGSEVK REEPEALYAA VNKKPTSAAY SVGEEYIALY PYSSVEPGDL
1010 1020 1030 1040 1050
TFTEGEEILV TQKDGEWWTG SIGDRSGIFP SNYVKPKDQE SFGSASKSGA
1060 1070 1080 1090 1100
SNKKPEIAQV TSAYVASGSE QLSLAPGQLI LILKKNTSGW WQGELQARGK
1110 1120 1130 1140 1150
KRQKGWFPAS HVKLLGPSSE RATPAFHPVC QVIAMYDYAA NNEDELSFSK
1160 1170 1180 1190 1200
GQLINVMNKD DPDWWQGEIN GVTGLFPSNY VKMTTDSDPS QQWCADLQTL
1210 1220 1230 1240 1250
DTMQPIERKR QGYIHELIQT EERYMADLQL VVEVFQKRMA ESGFLTEGEM
1260 1270 1280 1290 1300
ALIFVNWKEL IMSNTKLLKA LRVRKKTGGE KMPVQMIGDI LAAELSHMQA
1310 1320 1330 1340 1350
YIRFCSCQLN GAALLQQKTD EDTDFKEFLK KLASDPRCKG MPLSSFLLKP
1360 1370 1380 1390 1400
MQRITRYPLL IRSILENTPE SHADHSSLKL ALERAEELCS QVNEGVREKE
1410 1420 1430 1440 1450
NSDRLEWIQA HVQCEGLAEQ LIFNSLTNCL GPRKLLHSGK LYKTKSNKEL
1460 1470 1480 1490 1500
HGFLFNDFLL LTYMVKQFAV SSGSEKLFSS KSNAQFKMYK TPIFLNEVLV
1510 1520 1530 1540 1550
KLPTDPSSDE PVFHISHIDR VYTLRTDNIN ERTAWVQKIK AASEQYIDTE
1560 1570 1580 1590 1600
KKKREKAYQA RSQKTSGIGR LMVHVIEATE LKACKPNGKS NPYCEISMGS
1610 1620 1630 1640 1650
QSYTTRTIQD TLNPKWNFNC QFFIKDLYQD VLCLTLFDRD QFSPDDFLGR
1660 1670 1680 1690
TEIPVAKIRT EQESKGPMTR RLLLHEVPTG EVWVRFDLQL FEQKTLL
Length:1,697
Mass (Da):193,461
Last modified:April 20, 2010 - v3
Checksum:i49C41AE1E32E1BD0
GO
Isoform 2 (identifier: Q9NZM3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     622-648: Missing.

Show »
Length:1,670
Mass (Da):190,496
Checksum:i91E65C08E5AB26F1
GO
Isoform 3 (identifier: Q9NZM3-3) [UniParc]FASTAAdd to Basket

Also known as: ITSN2-S1

The sequence of this isoform differs from the canonical sequence as follows:
     1235-1249: FQKRMAESGFLTEGE → RRLLLASSRGICCLS
     1250-1697: Missing.

Show »
Length:1,249
Mass (Da):141,820
Checksum:i271797AF71A0EB28
GO
Isoform 4 (identifier: Q9NZM3-4) [UniParc]FASTAAdd to Basket

Also known as: ITSN2-S2, SH3P18

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

Show »
Length:1,192
Mass (Da):135,144
Checksum:i2DA2049587CF4082
GO

Sequence cautioni

The sequence AAF59903.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAF59904.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAF63600.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA86570.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti679 – 6791R → G in BAB13841. (PubMed:14702039)Curated
Sequence conflicti823 – 8286KAVSPK → FAAAST in AAD00899. 1 PublicationCurated
Sequence conflicti945 – 9517WFPKSYV → EFAAAST in AAC50593. (PubMed:9630982)Curated
Sequence conflicti1279 – 12857GEKMPVQ → VDAAANS in AAD00899. 1 PublicationCurated
Sequence conflicti1553 – 15531K → Q in AAF63600. 1 PublicationCurated
Sequence conflicti1553 – 15531K → Q in BAA86570. (PubMed:10574462)Curated
Isoform 3 (identifier: Q9NZM3-3)
Sequence conflicti1235 – 12351R → W in AAF59904. (PubMed:10922467)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti254 – 2541T → A.
Corresponds to variant rs6744320 [ dbSNP | Ensembl ].
VAR_024287
Natural varianti291 – 2911V → I.1 Publication
Corresponds to variant rs7603997 [ dbSNP | Ensembl ].
VAR_024288
Natural varianti1287 – 12871I → T.
Corresponds to variant rs3731625 [ dbSNP | Ensembl ].
VAR_020193
Natural varianti1534 – 15341A → T.
Corresponds to variant rs2303291 [ dbSNP | Ensembl ].
VAR_021937

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei622 – 64827Missing in isoform 2. 3 PublicationsVSP_003892Add
BLAST
Alternative sequencei1193 – 1697505Missing in isoform 4. 1 PublicationVSP_003895Add
BLAST
Alternative sequencei1235 – 124915FQKRM…LTEGE → RRLLLASSRGICCLS in isoform 3. 1 PublicationVSP_003893Add
BLAST
Alternative sequencei1250 – 1697448Missing in isoform 3. 1 PublicationVSP_003894Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS1710.2. [Q9NZM3-1]
CCDS1711.2. [Q9NZM3-2]
CCDS46230.1. [Q9NZM3-3]
RefSeqiNP_006268.2. NM_006277.2. [Q9NZM3-1]
NP_062541.3. NM_019595.3. [Q9NZM3-2]
NP_671494.2. NM_147152.2. [Q9NZM3-3]
UniGeneiHs.432562.

Genome annotation databases

EnsembliENST00000355123; ENSP00000347244; ENSG00000198399. [Q9NZM3-1]
ENST00000361999; ENSP00000354561; ENSG00000198399. [Q9NZM3-2]
ENST00000406921; ENSP00000384499; ENSG00000198399. [Q9NZM3-3]
GeneIDi50618.
KEGGihsa:50618.
UCSCiuc002rfe.2. human. [Q9NZM3-1]
uc002rff.2. human. [Q9NZM3-2]
uc002rfg.3. human. [Q9NZM3-3]

Polymorphism databases

DMDMi294862505.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS1710.2. [Q9NZM3-1 ]
CCDS1711.2. [Q9NZM3-2 ]
CCDS46230.1. [Q9NZM3-3 ]
RefSeqi NP_006268.2. NM_006277.2. [Q9NZM3-1 ]
NP_062541.3. NM_019595.3. [Q9NZM3-2 ]
NP_671494.2. NM_147152.2. [Q9NZM3-3 ]
UniGenei Hs.432562.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J3T NMR - A 898-958 [» ]
1UDL NMR - A 1103-1187 [» ]
1UE9 NMR - A 1056-1122 [» ]
1UFF NMR - A 762-842 [» ]
1UHF NMR - A 983-1038 [» ]
3GF9 X-ray 2.50 A 1130-1406 [» ]
3JZY X-ray 1.56 A 1201-1692 [» ]
4IIO X-ray 1.70 A/B 901-955 [» ]
ProteinModelPortali Q9NZM3.
SMRi Q9NZM3. Positions 2-108, 236-332, 762-845, 901-1551, 1568-1691.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119098. 80 interactions.
IntActi Q9NZM3. 25 interactions.
MINTi MINT-1404321.
STRINGi 9606.ENSP00000347244.

PTM databases

PhosphoSitei Q9NZM3.

Polymorphism databases

DMDMi 294862505.

Proteomic databases

MaxQBi Q9NZM3.
PaxDbi Q9NZM3.
PRIDEi Q9NZM3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355123 ; ENSP00000347244 ; ENSG00000198399 . [Q9NZM3-1 ]
ENST00000361999 ; ENSP00000354561 ; ENSG00000198399 . [Q9NZM3-2 ]
ENST00000406921 ; ENSP00000384499 ; ENSG00000198399 . [Q9NZM3-3 ]
GeneIDi 50618.
KEGGi hsa:50618.
UCSCi uc002rfe.2. human. [Q9NZM3-1 ]
uc002rff.2. human. [Q9NZM3-2 ]
uc002rfg.3. human. [Q9NZM3-3 ]

Organism-specific databases

CTDi 50618.
GeneCardsi GC02M024425.
H-InvDB HIX0001876.
HGNCi HGNC:6184. ITSN2.
HPAi HPA036475.
MIMi 604464. gene.
neXtProti NX_Q9NZM3.
PharmGKBi PA29982.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5422.
GeneTreei ENSGT00760000118985.
HOVERGENi HBG052159.
InParanoidi Q9NZM3.
OMAi WQQKSAF.
OrthoDBi EOG7WMCJ3.
PhylomeDBi Q9NZM3.
TreeFami TF324293.

Miscellaneous databases

ChiTaRSi ITSN2. human.
EvolutionaryTracei Q9NZM3.
GeneWikii ITSN2.
GenomeRNAii 50618.
NextBioi 53140.
PROi Q9NZM3.
SOURCEi Search...

Gene expression databases

Bgeei Q9NZM3.
CleanExi HS_ITSN2.
ExpressionAtlasi Q9NZM3. baseline and differential.
Genevestigatori Q9NZM3.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
InterProi IPR000008. 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.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR011511. SH3_2.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR11216:SF29. PTHR11216:SF29. 1 hit.
Pfami PF00168. C2. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00018. SH3_1. 2 hits.
PF07653. SH3_2. 1 hit.
PF14604. SH3_9. 2 hits.
[Graphical view ]
PRINTSi PR00452. SH3DOMAIN.
SMARTi 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 ]
SUPFAMi SSF48065. SSF48065. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 5 hits.
PROSITEi PS50004. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiITSN2_HUMAN
AccessioniPrimary (citable) accession number: Q9NZM3
Secondary accession number(s): O95062
, Q15812, Q9HAK4, Q9NXE6, Q9NYG0, Q9NZM2, Q9ULG4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: April 20, 2010
Last modified: November 26, 2014
This is version 164 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Overexpression results in the inhibition of the transferrin uptake and the blockage of the clathrin-mediated endocytosis.

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3