CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022452
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Intersectin-2 
Protein Synonyms/Alias
 SH3 domain-containing protein 1B; SH3P18; SH3P18-like WASP-associated protein 
Gene Name
 ITSN2 
Gene Synonyms/Alias
 KIAA1256; SH3D1B; SWAP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
89AMKLIKLKLQGQQLPubiquitination[1]
566QLLNERIKNMQFSNTubiquitination[1, 2, 3]
583SGVSLLHKKSLEKEEubiquitination[2, 4, 5, 6]
584GVSLLHKKSLEKEELubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661
Functional Description
 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). 
Sequence Annotation
 DOMAIN 22 110 EH 1.
 DOMAIN 54 89 EF-hand.
 DOMAIN 244 333 EH 2.
 DOMAIN 757 818 SH3 1.
 DOMAIN 898 956 SH3 2.
 DOMAIN 981 1039 SH3 3.
 DOMAIN 1053 1117 SH3 4.
 DOMAIN 1127 1186 SH3 5.
 DOMAIN 1209 1395 DH.
 DOMAIN 1434 1544 PH.
 DOMAIN 1556 1652 C2.
 MOD_RES 210 210 Phosphoserine.
 MOD_RES 230 230 Phosphoserine.
 MOD_RES 553 553 Phosphotyrosine (By similarity).
 MOD_RES 573 573 Phosphothreonine.
 MOD_RES 889 889 Phosphoserine.
 MOD_RES 968 968 Phosphotyrosine.  
Keyword
 3D-structure; Alternative splicing; Calcium; Coiled coil; Complete proteome; Cytoplasm; Endocytosis; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1697 AA 
Protein Sequence
MMAQFPTAMN GGPNMWAITS EERTKHDRQF DNLKPSGGYI TGDQARNFFL QSGLPAPVLA 60
EIWALSDLNK DGKMDQQEFS IAMKLIKLKL QGQQLPVVLP PIMKQPPMFS PLISARFGMG 120
SMPNLSIPQP LPPAAPITSL SSATSGTNLP PLMMPTPLVP SVSTSSLPNG TASLIQPLPI 180
PYSSSTLPHG SSYSLMMGGF GGASIQKAQS LIDLGSSSST SSTASLSGNS PKTGTSEWAV 240
PQPTRLKYRQ KFNTLDKSMS GYLSGFQARN ALLQSNLSQT QLATIWTLAD VDGDGQLKAE 300
EFILAMHLTD MAKAGQPLPL TLPPELVPPS FRGGKQIDSI NGTLPSYQKM QEEEPQKKLP 360
VTFEDKRKAN YERGNMELEK RRQALMEQQQ REAERKAQKE KEEWERKQRE LQEQEWKKQL 420
ELEKRLEKQR ELERQREEER RKDIERREAA KQELERQRRL EWERIRRQEL LNQKNREQEE 480
IVRLNSKKKN LHLELEALNG KHQQISGRLQ DVRLKKQTQK TELEVLDKQC DLEIMEIKQL 540
QQELQEYQNK LIYLVPEKQL LNERIKNMQF SNTPDSGVSL LHKKSLEKEE LCQRLKEQLD 600
ALEKETASKL SEMDSFNNQL KCGNMDDSVL QCLLSLLSCL NNLFLLLKEL RETYNTQQLA 660
LEQLYKIKRD KLKEIERKRL ELMQKKKLED EAARKAKQGK ENLWKENLRK EEEEKQKRLQ 720
EEKTQEKIQE EERKAEEKQR KDKDTLKAEE KKRETASVLV NYRALYPFEA RNHDEMSFNS 780
GDIIQVDEKT VGEPGWLYGS FQGNFGWFPC NYVEKMPSSE NEKAVSPKKA LLPPTVSLSA 840
TSTSSEPLSS NQPASVTDYQ NVSFSNLTVN TSWQKKSAFT RTVSPGSVSP IHGQGQVVEN 900
LKAQALCSWT AKKDNHLNFS KHDIITVLEQ QENWWFGEVH GGRGWFPKSY VKIIPGSEVK 960
REEPEALYAA VNKKPTSAAY SVGEEYIALY PYSSVEPGDL TFTEGEEILV TQKDGEWWTG 1020
SIGDRSGIFP SNYVKPKDQE SFGSASKSGA SNKKPEIAQV TSAYVASGSE QLSLAPGQLI 1080
LILKKNTSGW WQGELQARGK KRQKGWFPAS HVKLLGPSSE RATPAFHPVC QVIAMYDYAA 1140
NNEDELSFSK GQLINVMNKD DPDWWQGEIN GVTGLFPSNY VKMTTDSDPS QQWCADLQTL 1200
DTMQPIERKR QGYIHELIQT EERYMADLQL VVEVFQKRMA ESGFLTEGEM ALIFVNWKEL 1260
IMSNTKLLKA LRVRKKTGGE KMPVQMIGDI LAAELSHMQA YIRFCSCQLN GAALLQQKTD 1320
EDTDFKEFLK KLASDPRCKG MPLSSFLLKP MQRITRYPLL IRSILENTPE SHADHSSLKL 1380
ALERAEELCS QVNEGVREKE NSDRLEWIQA HVQCEGLAEQ LIFNSLTNCL GPRKLLHSGK 1440
LYKTKSNKEL HGFLFNDFLL LTYMVKQFAV SSGSEKLFSS KSNAQFKMYK TPIFLNEVLV 1500
KLPTDPSSDE PVFHISHIDR VYTLRTDNIN ERTAWVQKIK AASEQYIDTE KKKREKAYQA 1560
RSQKTSGIGR LMVHVIEATE LKACKPNGKS NPYCEISMGS QSYTTRTIQD TLNPKWNFNC 1620
QFFIKDLYQD VLCLTLFDRD QFSPDDFLGR TEIPVAKIRT EQESKGPMTR RLLLHEVPTG 1680
EVWVRFDLQL FEQKTLL 1697 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
 GO:0005070; F:SH3/SH2 adaptor activity; TAS:ProtInc.
 GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR018029; C2_membr_targeting.
 IPR000219; DH-domain.
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR000261; EPS15_homology.
 IPR027029; Intersectin-2.
 IPR000108; p67phox.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR011511; SH3_2.
 IPR001452; SH3_domain. 
Pfam
 PF00168; C2
 PF00621; RhoGEF
 PF00018; SH3_1
 PF07653; SH3_2 
SMART
 SM00239; C2
 SM00054; EFh
 SM00027; EH
 SM00233; PH
 SM00325; RhoGEF
 SM00326; SH3 
PROSITE
 PS50004; C2
 PS50010; DH_2
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS50031; EH
 PS50003; PH_DOMAIN
 PS50002; SH3 
PRINTS
 PR00499; P67PHOX.
 PR00452; SH3DOMAIN.