CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022637
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tight junction protein ZO-3 
Protein Synonyms/Alias
 Tight junction protein 3; Zona occludens protein 3; Zonula occludens protein 3 
Gene Name
 Tjp3 
Gene Synonyms/Alias
 Zo3 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
186DVLMRPLKSVLVKRRubiquitination[1]
653DSPSKIIKLDTVRVIubiquitination[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
  
Sequence Annotation
 DOMAIN 11 93 PDZ 1.
 DOMAIN 187 264 PDZ 2.
 DOMAIN 368 434 PDZ 3.
 DOMAIN 467 540 SH3.
 DOMAIN 573 754 Guanylate kinase-like.
 MOD_RES 111 111 Phosphoserine.
 MOD_RES 151 151 Phosphoserine.
 MOD_RES 156 156 Phosphoserine.
 MOD_RES 157 157 Phosphoserine.
 MOD_RES 161 161 Phosphoserine.
 MOD_RES 195 195 Phosphoserine.
 MOD_RES 323 323 Phosphothreonine.
 MOD_RES 557 557 Phosphoserine.
 MOD_RES 584 584 Phosphoserine.
 MOD_RES 891 891 Phosphoserine.
 MOD_RES 892 892 Phosphoserine.  
Keyword
 Cell junction; Cell membrane; Complete proteome; Membrane; Phosphoprotein; Reference proteome; Repeat; SH3 domain; Tight junction. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 905 AA 
Protein Sequence
MEELTIWEQH TATLYKDPRR GFGIAVSGGH DRASGSVVVS DVVPGSPAEG RLRTGDHIVM 60
VNGVSVENVT SAFAIQILKT CTKTANVTVK RPRRVQLPAT KASPASGHQL SDQEEADHGR 120
GYEGDSSSGS GRSWGERSRR SRAGRRGRVG SHGRRSSGGG SEANGLDLVS GYKRLPKQDV 180
LMRPLKSVLV KRRNSEEFGV KLGSQIFIKH ITESGLAARN HGLQEGDLIL QINGVSSANL 240
SLSDTRRLIE KSEGELTLLV LRDSGQFLVN IPPAVSDSDS SLMEDISDLT SELSQAPPSH 300
VPPPPLKGQR SPEDSQTDSP VETPQPRRRE RSVNSRAIAE PESPGESRYD IYRVPSRQSL 360
EDRGYSPDTR VVSFPKGASI GLRLAGGNDV GIFVSGVQAG SPADGQGIQE GDEILQVNGM 420
PFRNLTREEA VQFLLGLPPG EDMELVTQSK TGHSLRRWSQ SRVGDSFYIR THFELEPSPP 480
YGLGFTRGDV FHVVDTLYPG SGPGHGHSSH GGLWLAARMG RDLREQERGV IPNQSRAEQL 540
ASLEAAQRAA GVGPGASVGS NPRAEFWRLR SLRRGTKKAS TQRSREDLSA LTRQGHYPPY 600
ERVVLREASF KRPVVILGPV ADIAMKKLTT EMPEEFEIAE SMSRTDSPSK IIKLDTVRVI 660
AERDKHALLD VTPSAIERLN YVQYYPIVIF CAPESRPALK ALREWLAPAS RRSSRRLYAQ 720
AQKLQKHSGH LFTATIPLHG TSDSWYQEVK AVIQQQQARP IWTAEDQLNS SSEDLDLTGH 780
GLAASSGDLS CDSRTNSDYE DTDGEGAYTD REGGPQDVDE EVAPTALARS SEPVWVDDHQ 840
GLMGHGTTIT DKWETQADSH YTQDQRRQDS MRTYKHEALR KKFTRARDVE SSDDEGYDWG 900
PATDL 905 
Gene Ontology
 GO:0016324; C:apical plasma membrane; IDA:MGI.
 GO:0005923; C:tight junction; IDA:MGI.
 GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IGI:MGI. 
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.
 IPR005420; ZonOcculS3. 
Pfam
 PF00625; Guanylate_kin
 PF00595; PDZ
 PF07653; SH3_2 
SMART
 SM00072; GuKc
 SM00228; PDZ
 SM00326; SH3 
PROSITE
 PS00856; GUANYLATE_KINASE_1
 PS50052; GUANYLATE_KINASE_2
 PS50106; PDZ
 PS50002; SH3 
PRINTS
 PR01597; ZONOCCLUDNS.
 PR01600; ZONOCCLUDNS3.