| Tag | Content |
|---|
| CPLM ID | CPLM-001306 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Multiple PDZ domain protein |
Protein Synonyms/Alias | Multi-PDZ domain protein 1 |
Gene Name | MPDZ |
Gene Synonyms/Alias | MUPP1 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 741 | VPGGIAEKDGRLLPG | ubiquitination | [1, 2] |
|
Reference | [1] 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] [2] 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] |
Functional Description | Interacts with HTR2C and provokes its clustering at the cell surface (By similarity). Member of the NMDAR signaling complex that may play a role in control of AMPAR potentiation and synaptic plasticity in excitatory synapses. |
Sequence Annotation | DOMAIN 1 63 L27.
DOMAIN 137 224 PDZ 1.
DOMAIN 257 337 PDZ 2.
DOMAIN 377 463 PDZ 3.
DOMAIN 553 634 PDZ 4.
DOMAIN 700 786 PDZ 5.
DOMAIN 1008 1089 PDZ 6.
DOMAIN 1151 1243 PDZ 7.
DOMAIN 1350 1433 PDZ 8.
DOMAIN 1483 1564 PDZ 9.
DOMAIN 1629 1712 PDZ 10.
DOMAIN 1725 1807 PDZ 11.
DOMAIN 1862 1948 PDZ 12.
DOMAIN 1987 2070 PDZ 13.
MOD_RES 230 230 Phosphoserine.
MOD_RES 483 483 Phosphoserine. |
Keyword | 3D-structure; Alternative splicing; Cell junction; Cell membrane; Cell projection; Complete proteome; Host-virus interaction; Membrane; Phosphoprotein; Polymorphism; Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; Synaptosome; Tight junction. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 2070 AA |
Protein Sequence | MLEAIDKNRA LHAAERLQTK LRERGDVANE DKLSLLKSVL QSPLFSQILS LQTSVQQLKD 60
QVNIATSATS NIEYAHVPHL SPAVIPTLQN ESFLLSPNNG NLEALTGPGI PHINGKPACD 120
EFDQLIKNMA QGRHVEVFEL LKPPSGGLGF SVVGLRSENR GELGIFVQEI QEGSVAHRDG 180
RLKETDQILA INGQALDQTI THQQAISILQ KAKDTVQLVI ARGSLPQLVS PIVSRSPSAA 240
STISAHSNPV HWQHMETIEL VNDGSGLGFG IIGGKATGVI VKTILPGGVA DQHGRLCSGD 300
HILKIGDTDL AGMSSEQVAQ VLRQCGNRVK LMIARGAIEE RTAPTALGIT LSSSPTSTPE 360
LRVDASTQKG EESETFDVEL TKNVQGLGIT IAGYIGDKKL EPSGIFVKSI TKSSAVEHDG 420
RIQIGDQIIA VDGTNLQGFT NQQAVEVLRH TGQTVLLTLM RRGMKQEAEL MSREDVTKDA 480
DLSPVNASII KENYEKDEDF LSSTRNTNIL PTEEEGYPLL SAEIEEIEDA QKQEAALLTK 540
WQRIMGINYE IVVAHVSKFS ENSGLGISLE ATVGHHFIRS VLPEGPVGHS GKLFSGDELL 600
EVNGITLLGE NHQDVVNILK ELPIEVTMVC CRRTVPPTTQ SELDSLDLCD IELTEKPHVD 660
LGEFIGSSET EDPVLAMTDA GQSTEEVQAP LAMWEAGIQH IELEKGSKGL GFSILDYQDP 720
IDPASTVIII RSLVPGGIAE KDGRLLPGDR LMFVNDVNLE NSSLEEAVEA LKGAPSGTVR 780
IGVAKPLPLS PEEGYVSAKE DSFLYPPHSC EEAGLADKPL FRADLALVGT NDADLVDEST 840
FESPYSPEND SIYSTQASIL SLHGSSCGDG LNYGSSLPSS PPKDVIENSC DPVLDLHMSL 900
EELYTQNLLQ RQDENTPSVD ISMGPASGFT INDYTPANAI EQQYECENTI VWTESHLPSE 960
VISSAELPSV LPDSAGKGSE YLLEQSSLAC NAECVMLQNV SKESFERTIN IAKGNSSLGM 1020
TVSANKDGLG MIVRSIIHGG AISRDGRIAI GDCILSINEE STISVTNAQA RAMLRRHSLI 1080
GPDIKITYVP AEHLEEFKIS LGQQSGRVMA LDIFSSYTGR DIPELPEREE GEGEESELQN 1140
TAYSNWNQPR RVELWREPSK SLGISIVGGR GMGSRLSNGE VMRGIFIKHV LEDSPAGKNG 1200
TLKPGDRIVE VDGMDLRDAS HEQAVEAIRK AGNPVVFMVQ SIINRPRKSP LPSLLHNLYP 1260
KYNFSSTNPF ADSLQINADK APSQSESEPE KAPLCSVPPP PPSAFAEMGS DHTQSSASKI 1320
SQDVDKEDEF GYSWKNIRER YGTLTGELHM IELEKGHSGL GLSLAGNKDR SRMSVFIVGI 1380
DPNGAAGKDG RLQIADELLE INGQILYGRS HQNASSIIKC APSKVKIIFI RNKDAVNQMA 1440
VCPGNAVEPL PSNSENLQNK ETEPTVTTSD AAVDLSSFKN VQHLELPKDQ GGLGIAISEE 1500
DTLSGVIIKS LTEHGVAATD GRLKVGDQIL AVDDEIVVGY PIEKFISLLK TAKMTVKLTI 1560
HAENPDSQAV PSAAGAASGE KKNSSQSLMV PQSGSPEPES IRNTSRSSTP AIFASDPATC 1620
PIIPGCETTI EISKGRTGLG LSIVGGSDTL LGAIIIHEVY EEGAACKDGR LWAGDQILEV 1680
NGIDLRKATH DEAINVLRQT PQRVRLTLYR DEAPYKEEEV CDTLTIELQK KPGKGLGLSI 1740
VGKRNDTGVF VSDIVKGGIA DADGRLMQGD QILMVNGEDV RNATQEAVAA LLKCSLGTVT 1800
LEVGRIKAGP FHSERRPSQS SQVSEGSLSS FTFPLSGSST SESLESSSKK NALASEIQGL 1860
RTVEMKKGPT DSLGISIAGG VGSPLGDVPI FIAMMHPTGV AAQTQKLRVG DRIVTICGTS 1920
TEGMTHTQAV NLLKNASGSI EMQVVAGGDV SVVTGHQQEP ASSSLSFTGL TSSSIFQDDL 1980
GPPQCKSITL ERGPDGLGFS IVGGYGSPHG DLPIYVKTVF AKGAASEDGR LKRGDQIIAV 2040
NGQSLEGVTH EEAVAILKRT KGTVTLMVLS 2070 |
Gene Ontology | GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB. GO:0005737; C:cytoplasm; IDA:UniProtKB. GO:0031410; C:cytoplasmic vesicle; IEA:Compara. GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell. GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW. GO:0043220; C:Schmidt-Lanterman incisure; IEA:Compara. GO:0005923; C:tight junction; IEA:UniProtKB-SubCell. GO:0007155; P:cell adhesion; IEA:Compara. GO:0042552; P:myelination; IEA:Compara. GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. |
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Pfam | |
SMART | |
PROSITE | |
PRINTS | |