CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011484
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tight junction protein ZO-1 
Protein Synonyms/Alias
 Tight junction protein 1; Zona occludens protein 1; Zonula occludens protein 1 
Gene Name
 TJP1 
Gene Synonyms/Alias
 ZO1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
183VASSQPAKPTKVTLVubiquitination[1]
348RDEERISKPGAVSTPubiquitination[1]
553VDTLYNGKLGSWLAIubiquitination[2, 3]
592SVQYTLPKTAGGDRAubiquitination[1]
695IIRLHTIKQIIDQDKubiquitination[2, 3]
702KQIIDQDKHALLDVTubiquitination[2, 3]
1189GPKPAESKQYFEQYSubiquitination[2, 3]
1417VDRSFGEKRYEPIQAacetylation[4]
1601SIHAEKPKYQINNISubiquitination[2, 3]
Reference
 [1] 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]
 [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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330] 
Functional Description
 The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells. 
Sequence Annotation
 DOMAIN 23 110 PDZ 1.
 DOMAIN 186 264 PDZ 2.
 DOMAIN 421 502 PDZ 3.
 DOMAIN 516 584 SH3.
 DOMAIN 598 779 Guanylate kinase-like.
 DOMAIN 1632 1724 ZU5.
 MOD_RES 125 125 Phosphoserine.
 MOD_RES 175 175 Phosphoserine.
 MOD_RES 178 178 Phosphoserine.
 MOD_RES 179 179 Phosphoserine.
 MOD_RES 185 185 Phosphothreonine.
 MOD_RES 277 277 Phosphoserine.
 MOD_RES 284 284 Phosphoserine (By similarity).
 MOD_RES 297 297 Phosphoserine.
 MOD_RES 300 300 Phosphoserine.
 MOD_RES 329 329 Phosphoserine.
 MOD_RES 334 334 Phosphoserine.
 MOD_RES 337 337 Phosphoserine.
 MOD_RES 353 353 Phosphoserine.
 MOD_RES 617 617 Phosphoserine.
 MOD_RES 622 622 Phosphoserine.
 MOD_RES 912 912 Phosphoserine.
 MOD_RES 968 968 Phosphoserine.
 MOD_RES 1140 1140 Phosphotyrosine (By similarity).
 MOD_RES 1165 1165 Phosphotyrosine (By similarity).
 MOD_RES 1354 1354 Phosphotyrosine (By similarity).
 MOD_RES 1366 1366 Phosphoserine.
 MOD_RES 1545 1545 Phosphoserine.
 MOD_RES 1617 1617 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Calmodulin-binding; Cell junction; Cell membrane; Complete proteome; Gap junction; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3 domain; Tight junction. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1748 AA 
Protein Sequence
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL 60
KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSRPD 120
PEPVSDNEED SYDEEIHDPR SGRSGVVNRR SEKIWPRDRS ASRERSLSPR SDRRSVASSQ 180
PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM 240
SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 300
GRSHDRPPRR SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG AVSTPVKHAD 360
DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP VSPSDGVLPN STHEDGILRP 420
SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR 480
EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG 540
EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 600
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK 660
LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ 720
WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND 780
GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT 840
SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 900
QAQPQPIHRI DSPGFKPASQ QKAEASSPVP YLSPETNPAS STSAVNHNVN LTNVRLEEPT 960
PAPSTSYSPQ ADSLRTPSTE AAHIMLRDQE PSLSSHVDPT KVYRKDPYPE EMMRQNHVLK 1020
QPAVSHPGHR PDKEPNLTYE PQLPYVEKQA SRDLEQPTYR YESSSYTDQF SRNYEHRLRY 1080
EDRVPMYEEQ WSYYDDKQPY PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY 1140
DSRPRYEQAP RASALRHEEQ PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE 1200
QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ TEEEEDPAMK 1260
PQSVLTRVKM FENKRSASLE TKKDVNDTGS FKPPEVASKP SGAPIIGPKP TSQNQFSEHD 1320
KTLYRIPEPQ KPQLKPPEDI VRSNHYDPEE DEEYYRKQLS YFDRRSFENK PPAHIAASHL 1380
SEPAKPAHSQ NQSNFSSYSS KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ 1440
PVTSASLHIH SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP 1500
QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK PYTSSARPFE RKFESPKFNH NLLPSETAHK 1560
PDLSSKTPTS PKTLVKSHSL AQPPEFDSGV ETFSIHAEKP KYQINNISTV PKAIPVSPSA 1620
VEEDEDEDGH TVVATARGIF NSNGGVLSSI ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS 1680
ILPPLDKEKG ETLLSPLVMC GPHGLKFLKP VELRLPHCDP KTWQNKCLPG DPNYLVGANC 1740
VSVLIDHF 1748 
Gene Ontology
 GO:0045177; C:apical part of cell; IDA:MGI.
 GO:0016327; C:apicolateral plasma membrane; IEA:Compara.
 GO:0016323; C:basolateral plasma membrane; IDA:MGI.
 GO:0005913; C:cell-cell adherens junction; TAS:ProtInc.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
 GO:0014704; C:intercalated disc; IEA:Compara.
 GO:0046581; C:intercellular canaliculus; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005923; C:tight junction; IDA:UniProtKB.
 GO:0001825; P:blastocyst formation; IEA:Compara.
 GO:0007043; P:cell-cell junction assembly; TAS:ProtInc.
 GO:1901350; P:cell-cell signaling involved in cell-cell junction organization; NAS:UniProtKB.
 GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
 GO:0071333; P:cellular response to glucose stimulus; IEA:Compara.
 GO:0035329; P:hippo signaling cascade; TAS:Reactome.
 GO:0043116; P:negative regulation of vascular permeability; IEA:Compara.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0045471; P:response to ethanol; IEA:Compara.
 GO:0032496; P:response to lipopolysaccharide; IEA:Compara.
 GO:0071000; P:response to magnetism; IEA:Compara. 
Interpro
 IPR008144; Guanylate_kin.
 IPR008145; Guanylate_kin/L-typ_Ca_channel.
 IPR027417; P-loop_NTPase.
 IPR001478; PDZ.
 IPR011511; SH3_2.
 IPR001452; SH3_domain.
 IPR005417; ZonOcculdens.
 IPR005418; ZonOcculS1.
 IPR000906; ZU5. 
Pfam
 PF00625; Guanylate_kin
 PF00595; PDZ
 PF07653; SH3_2
 PF00791; ZU5 
SMART
 SM00072; GuKc
 SM00228; PDZ
 SM00326; SH3
 SM00218; ZU5 
PROSITE
 PS00856; GUANYLATE_KINASE_1
 PS50052; GUANYLATE_KINASE_2
 PS50106; PDZ
 PS50002; SH3
 PS51145; ZU5 
PRINTS
 PR01597; ZONOCCLUDNS.
 PR01598; ZONOCCLUDNS1.