CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012203
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein Shroom2 
Protein Synonyms/Alias
 Apical-like protein; Protein APXL 
Gene Name
 SHROOM2 
Gene Synonyms/Alias
 APXL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
308VWYVPDKKKAPSSPPacetylation[1]
309WYVPDKKKAPSSPPPacetylation[1]
1341LDPSVKIKTTMDLMEacetylation[2]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution (By similarity). 
Sequence Annotation
 DOMAIN 26 108 PDZ.
 DOMAIN 684 773 ASD1.
 DOMAIN 1317 1611 ASD2.
 MOD_RES 922 922 Phosphoserine (By similarity).
 MOD_RES 974 974 Phosphoserine.
 MOD_RES 1036 1036 Phosphoserine.
 MOD_RES 1039 1039 Phosphoserine.
 MOD_RES 1297 1297 Phosphoserine (By similarity).  
Keyword
 Actin-binding; Cell junction; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Membrane; Microtubule; Phosphoprotein; Polymorphism; Reference proteome; Tight junction. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1616 AA 
Protein Sequence
MEGAEPRARP ERLAEAETRA ADGGRLVEVQ LSGGAPWGFT LKGGREHGEP LVITKIEEGS 60
KAAAVDKLLA GDEIVGINDI GLSGFRQEAI CLVKGSHKTL KLVVKRRSEL GWRPHSWHAT 120
KFSDSHPELA ASPFTSTSGC PSWSGRHHAS SSSHDLSSSW EQTNLQRTLD HFSSLGSVDS 180
LDHPSSRLSV AKSNSSIDHL GSHSKRDSAY GSFSTSSSTP DHTLSKADTS SAENILYTVG 240
LWEAPRQGGR QAQAAGDPQG SEEKLSCFPP RVPGDSGKGP RPEYNAEPKL AAPGRSNFGP 300
VWYVPDKKKA PSSPPPPPPP LRSDSFAATK SHEKAQGPVF SEAAAAQHFT ALAQAQPRGD 360
RRPELTDRPW RSAHPGSLGK GSGGPGCPQE AHADGSWPPS KDGASSRLQA SLSSSDVRFP 420
QSPHSGRHPP LYSDHSPLCA DSLGQEPGAA SFQNDSPPQV RGLSSCDQKL GSGWQGPRPC 480
VQGDLQAAQL WAGCWPSDTA LGALESLPPP TVGQSPRHHL PQPEGPPDAR ETGRCYPLDK 540
GAEGCSAGAQ EPPRASRAEK ASQRLAASIT WADGESSRIC PQETPLLHSL TQEGKRRPES 600
SPEDSATRPP PFDAHVGKPT RRSDRFATTL RNEIQMHRAK LQKSRSTVAL TAAGEAEDGT 660
GRWRAGLGGG TQEGPLAGTY KDHLKEAQAR VLRATSFKRR DLDPNPGDLY PESLEHRMGD 720
PDTVPHFWEA GLAQPPSSTS GGPHPPRIGG RRRFTAEQKL KSYSEPEKMN EVGLTRGYSP 780
HQHPRTSEDT VGTFADRWKF FEETSKPVPQ RPAQKQALHG IPRDKPERPR TAGRTCEGTE 840
PWSRTTSLGD SLNAHSAAEK AGTSDLPRRL GTFAEYQASW KEQRKPLEAR SSGRCHSADD 900
ILDVSLDPQE RPQHVHGRSR SSPSTDHYKQ EASVELRRQA GDPGEPREEL PSAVRAEEGQ 960
STPRQADAQC REGSPGSQQH PPSQKAPNPP TFSELSHCRG APELPREGRG RAGTLPRDYR 1020
YSEESTPADL GPRAQSPGSP LHARGQDSWP VSSALLSKRP APQRPPPPKR EPRRYRATDG 1080
APADAPVGVL GRPFPTPSPA SLDVYVARLS LSHSPSVFSS AQPQDTPKAT VCERGSQHVS 1140
GDASRPLPEA LLPPKQQHLR LQTATMETSR SPSPQFAPQK LTDKPPLLIQ DEDSTRIERV 1200
MDNNTTVKMV PIKIVHSESQ PEKESRQSLA CPAEPPALPH GLEKDQIKTL STSEQFYSRF 1260
CLYTRQGAEP EAPHRAQPAE PQPLGTQVPP EKDRCTSPPG LSYMKAKEKT VEDLKSEELA 1320
REIVGKDKSL ADILDPSVKI KTTMDLMEGI FPKDEHLLEE AQQRRKLLPK IPSPRSTEER 1380
KEEPSVPAAV SLATNSTYYS TSAPKAELLI KMKDLQEQQE HEEDSGSDLD HDLSVKKQEL 1440
IESISRKLQV LREARESLLE DVQANTVLGA EVEAIVKGVC KPSEFDKFRM FIGDLDKVVN 1500
LLLSLSGRLA RVENALNNLD DGASPGDRQS LLEKQRVLIQ QHEDAKELKE NLDRRERIVF 1560
DILANYLSEE SLADYEHFVK MKSALIIEQR ELEDKIHLGE EQLKCLLDSL QPERGK 1616 
Gene Ontology
 GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
 GO:0005938; C:cell cortex; IEA:Compara.
 GO:0005913; C:cell-cell adherens junction; ISS:UniProtKB.
 GO:0005856; C:cytoskeleton; ISS:UniProtKB.
 GO:0031941; C:filamentous actin; IEA:Compara.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005923; C:tight junction; ISS:UniProtKB.
 GO:0051015; F:actin filament binding; ISS:UniProtKB.
 GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
 GO:0015280; F:ligand-gated sodium channel activity; TAS:ProtInc.
 GO:0045176; P:apical protein localization; ISS:HGNC.
 GO:0007420; P:brain development; ISS:HGNC.
 GO:0016477; P:cell migration; ISS:UniProtKB.
 GO:0045217; P:cell-cell junction maintenance; IEA:Compara.
 GO:0043482; P:cellular pigment accumulation; ISS:HGNC.
 GO:0043583; P:ear development; ISS:HGNC.
 GO:0032401; P:establishment of melanosome localization; ISS:HGNC.
 GO:0008057; P:eye pigment granule organization; ISS:HGNC.
 GO:0002089; P:lens morphogenesis in camera-type eye; ISS:HGNC.
 GO:0032438; P:melanosome organization; ISS:HGNC.
 GO:0030835; P:negative regulation of actin filament depolymerization; IEA:Compara. 
Interpro
 IPR014800; ASD1.
 IPR014799; ASD2.
 IPR001478; PDZ. 
Pfam
 PF08688; ASD1
 PF08687; ASD2
 PF00595; PDZ 
SMART
 SM00228; PDZ 
PROSITE
 PS51306; ASD1
 PS51307; ASD2
 PS50106; PDZ 
PRINTS