CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014609
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sequestosome-1 
Protein Synonyms/Alias
 STONE14; Ubiquitin-binding protein p62 
Gene Name
 Sqstm1 
Gene Synonyms/Alias
 A170; STAP 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
13VKAYLLGKEEATREIubiquitination[1]
141PVVGTRYKCSVCPDYubiquitination[1]
157LCSVCEGKGLHREHSubiquitination[1]
165GLHREHSKLIFPNPFubiquitination[1]
297SCSSEVSKPDGAGEGubiquitination[1]
314QSLTEQMKKIALESVubiquitination[1]
315SLTEQMKKIALESVGubiquitination[1]
422LTRLLQTKNYDIGAAubiquitination[1]
437LDTIQYSKHPPPL**ubiquitination[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
 Required both for the formation and autophagic degradation of polyubiquitin-containing bodies, called ALIS (aggresome-like induced structures). Links ALIS to the autophagic machinery via direct interaction with MAP1 LC3 family members. May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role in titin/TTN downstream signaling in muscle cells. May regulate signaling cascades through ubiquitination. May be involved in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Adapter that mediates the interaction between TRAF6 and CYLD. 
Sequence Annotation
 DOMAIN 20 102 OPR.
 DOMAIN 391 436 UBA.
 ZN_FING 122 167 ZZ-type.
 REGION 1 50 Interaction with LCK (By similarity).
 REGION 43 107 Interaction with PRKCZ and dimerization
 REGION 50 80 Interaction with PAWR (By similarity).
 REGION 122 224 Interaction with GABRR3 (By similarity).
 REGION 170 220 LIM protein-binding (By similarity).
 REGION 269 442 Interaction with NTRK1 (By similarity).
 REGION 323 344 MAP1LC3B-binding (By similarity).
 MOTIF 228 233 TRAF6-binding (By similarity).
 MOD_RES 24 24 Phosphoserine.
 MOD_RES 148 148 Phosphotyrosine (By similarity).
 MOD_RES 178 178 Phosphoserine.
 MOD_RES 207 207 Phosphoserine (By similarity).
 MOD_RES 249 249 Phosphoserine (By similarity).
 MOD_RES 266 266 Phosphoserine (By similarity).
 MOD_RES 269 269 Phosphothreonine.
 MOD_RES 272 272 Phosphothreonine.
 MOD_RES 330 330 Phosphoserine (By similarity).
 MOD_RES 334 334 Phosphoserine.
 MOD_RES 357 357 Phosphoserine (By similarity).
 MOD_RES 363 363 Phosphoserine (By similarity).
 MOD_RES 367 367 Phosphoserine.
 MOD_RES 368 368 Phosphoserine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Apoptosis; Autophagy; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Differentiation; Endoplasmic reticulum; Endosome; Immunity; Lysosome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 442 AA 
Protein Sequence
MASFTVKAYL LGKEEATREI RRFSFCFSPE PEAEAQAAAG PGPCERLLSR VAVLFPTLRP 60
GGFQAHYRDE DGDLVAFSSD EELTMAMSYV KDDIFRIYIK EKKECRREHR PPCAQEAPRN 120
MVHPNVICDG CNGPVVGTRY KCSVCPDYDL CSVCEGKGLH REHSKLIFPN PFGHLSDSFS 180
HSRWLRKLKH GHFGWPGWEM GPPGNWSPRP PRAGDGRPCP TAESASAPPE DPNVNFLKNV 240
GESVAAALSP LGIEVDIDVE HGGKRSRLTP TTPESSSTGT EDKSNTQPSS CSSEVSKPDG 300
AGEGPAQSLT EQMKKIALES VGQPEEQMES GNCSGGDDDW THLSSKEVDP STGELQSLQM 360
PESEGPSSLD PSQEGPTGLK EAALYPHLPP EADPRLIESL SQMLSMGFSD EGGWLTRLLQ 420
TKNYDIGAAL DTIQYSKHPP PL 442 
Gene Ontology
 GO:0016235; C:aggresome; IDA:MGI.
 GO:0005776; C:autophagic vacuole; ISS:UniProtKB.
 GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
 GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
 GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
 GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
 GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0000407; C:pre-autophagosomal structure; IDA:MGI.
 GO:0042802; F:identical protein binding; IDA:MGI.
 GO:0070530; F:K63-linked polyubiquitin binding; IDA:UniProtKB.
 GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
 GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
 GO:0003712; F:transcription cofactor activity; TAS:MGI.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0016236; P:macroautophagy; ISS:UniProtKB.
 GO:0001934; P:positive regulation of protein phosphorylation; IEA:Compara.
 GO:0051291; P:protein heterooligomerization; IEA:Compara.
 GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB cascade; ISS:UniProtKB. 
Interpro
 IPR000270; OPR_PB1.
 IPR009060; UBA-like.
 IPR015940; UBA/transl_elong_EF1B_N_euk.
 IPR000433; Znf_ZZ. 
Pfam
 PF00564; PB1
 PF00569; ZZ 
SMART
 SM00666; PB1
 SM00165; UBA
 SM00291; ZnF_ZZ 
PROSITE
 PS50030; UBA
 PS01357; ZF_ZZ_1
 PS50135; ZF_ZZ_2 
PRINTS