CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007141
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
183VASSQPAKPTKVTLVubiquitination[1]
194VTLVKSRKNEEYGLRubiquitination[1]
348REEERMSKPGAISTPubiquitination[1]
374VEEVTVEKNEKQTPTubiquitination[1]
553VDTLYNGKLGSWLAIubiquitination[1]
1005DPAKVYRKEPYSEEMubiquitination[1]
1097QWSYYDDKQPYQPRPubiquitination[1]
1188GPKSSEPKQYFDQYPubiquitination[1]
1356EDEEYYRKQLSYFDRubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
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 (By similarity). 
Sequence Annotation
 DOMAIN 23 110 PDZ 1.
 DOMAIN 186 264 PDZ 2.
 DOMAIN 421 502 PDZ 3.
 DOMAIN 516 584 SH3.
 DOMAIN 610 791 Guanylate kinase-like.
 DOMAIN 1629 1721 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 (By similarity).
 MOD_RES 277 277 Phosphoserine (By similarity).
 MOD_RES 284 284 Phosphoserine.
 MOD_RES 297 297 Phosphoserine.
 MOD_RES 300 300 Phosphoserine.
 MOD_RES 329 329 Phosphoserine (By similarity).
 MOD_RES 334 334 Phosphoserine (By similarity).
 MOD_RES 337 337 Phosphoserine (By similarity).
 MOD_RES 353 353 Phosphoserine (By similarity).
 MOD_RES 617 617 Phosphoserine.
 MOD_RES 622 622 Phosphoserine (By similarity).
 MOD_RES 912 912 Phosphoserine.
 MOD_RES 1139 1139 Phosphotyrosine.
 MOD_RES 1164 1164 Phosphotyrosine.
 MOD_RES 1353 1353 Phosphotyrosine.
 MOD_RES 1365 1365 Phosphoserine (By similarity).
 MOD_RES 1542 1542 Phosphoserine (By similarity).
 MOD_RES 1614 1614 Phosphoserine (By similarity).  
Keyword
 3D-structure; Calmodulin-binding; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Gap junction; Membrane; Phosphoprotein; Reference proteome; Repeat; SH3 domain; Tight junction. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1745 AA 
Protein Sequence
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL 60
KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSHPD 120
PEPVSDNEDD SYDEEVHDPR AGRGALANRR SEKSWARDRS ASRERSLSPR SDRRSVASSQ 180
PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM 240
SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 300
GRSHDRPPRR SQSRSPDQRS EPSDHSTQSP QQPSNGSLRS REEERMSKPG AISTPVKHVD 360
DHPPKAVEEV TVEKNEKQTP TLPEPKPVYA QVGQPDVDLP VSPSDGALPN SAHEDGILRP 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 TDHRSSGIIR 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
QAQPQAIHRI DSPGLKPASQ QKAEASSPVP YLSPETTPAS SASAVNHNVS VTNVSLEEPA 960
PAPPTSHASQ PGCLGAPSAE AAHVVLRGEG PPLPPHADPA KVYRKEPYSE EMMRQNHILK 1020
QPALGHPGQR PDKEPNLAYE PQLPYIEKQA SRDLEQPSYR YEVSSYTDQF SRNYDHRLRF 1080
EDRIPTYEDQ WSYYDDKQPY QPRPFENQHP RDLDSRQHPE EASERGYFQR FEEPAPLSYD 1140
SRTRYEQLPR TSTLRHEEQP APAYEVHNRY RPEAQPYSST GPKSSEPKQY FDQYPRSYEQ 1200
VPPPGFTSKT GHYEPLHGAA VVPPLIPSSQ QKPEVLPSAT KPQPPPPTLT EEEEDPAMKP 1260
QSVLTRVKMF ENKRSASLEN KKDVNDTASF KPPEVASKPP GASLAGPKPV PQSQFSEHDK 1320
TLYRLPEPQK PQVKPPEDIV RSNHYDPEED EEYYRKQLSY FDRRSFESKP SAHLPAGHHS 1380
EPAKPVHSQS QPNFSSYSSK GKPETDAVDR SFSEKRYDPA QATPPPPPLP SQYSQPAPPL 1440
SSSSLHIHSK GAQGEGNSVS LDFQNSYMSK PDPPPSQSKP ATFRPPTRED PPQTFYPQKS 1500
FPDKAPVNGA EQTQKTITPV YNRFTPKPYT SSARPFERKF ESPKFNHNLL PSETVHKPEL 1560
SSKTPTSPKT LMKAHSSTQP PEFDSGVETF SVHTDKPKYQ MNNISTMPKA VPVSPSAVEE 1620
DEDEDGHTVV ATARGIFNSN GGVLSSIETG VSIIIPQGAI PEGIEQEIYF KVCRDNSILP 1680
PLDKEKGETL LSPLVMCGPH GLKFLKPVEL RLPHCDPKTW QNKCLPGDPN YLVGANCVSV 1740
LIDHF 1745 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IDA:MGI.
 GO:0016327; C:apicolateral plasma membrane; IDA:MGI.
 GO:0016323; C:basolateral plasma membrane; ISO:MGI.
 GO:0009986; C:cell surface; ISO:MGI.
 GO:0005913; C:cell-cell adherens junction; IDA:MGI.
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
 GO:0031674; C:I band; IEA:UniProtKB-SubCell.
 GO:0014704; C:intercalated disc; IDA:MGI.
 GO:0046581; C:intercellular canaliculus; IDA:MGI.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0005923; C:tight junction; IDA:UniProtKB.
 GO:0001825; P:blastocyst formation; IMP:MGI.
 GO:0071333; P:cellular response to glucose stimulus; IEA:Compara.
 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.