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Protein Page:
SQSTM1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
SQSTM1 an adapter protein which binds ubiquitin, shuttling proteins to the proteasome. Co-localizes along with the E3 ubiquitin ligase, TRAF6, to aggregates from Alzheimer's disease brains but not in control brain. May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1. May play a role in titin 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. Forms ternary complexes with PKCZ and Kv-beta2 or PKCZ and GABBR3. Also interacts with KCNAB1, GABRR1, GABRR2 and GABRR3. Interacts with EBI3, LCK, RASA1, PKCZ , PKCI, NR2F2, NTRK1, NTRK2, NTRK3, NBR1, MEK5, TRIM55 and MAPKAPK5. Interacts with the proteasome subunits PSMD4 and PSMC2. Interacts with K63- polyubiquitinated MAPT/TAU. Interacts with IKBKB through PRKCZ and PRKCI. Interacts with NGFR through TRAF6 and bridges that complex to NTRK1. Forms a complex with MEK5 and PRKCZ or PRKCI. Component of a ternary complex with PAWR and PRKCZ. Upon TNF-alpha stimulation, interacts with RIPK1 problably bridging IKBKB to the TNF-R1 complex composed of TNF-R1/TNFRSF1A, TRADD and RIPK1. Forms a complex with JUB/Ajuba, PRKCZ and TRAF6. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator; Ubiquitin conjugating system; Autophagy
Cellular Component: nucleoplasm; PML body; endoplasmic reticulum; lysosome; late endosome; cytoplasm; autophagic vacuole; inclusion body; cytoplasmic vesicle; cytosol
Molecular Function: identical protein binding; protein serine/threonine kinase activity; ubiquitin binding; protein binding; protein homodimerization activity; protein kinase C binding; zinc ion binding; SH2 domain binding; receptor tyrosine kinase binding; protein kinase binding
Biological Process: ubiquitin-dependent protein catabolic process; regulation of Ras protein signal transduction; nerve growth factor receptor signaling pathway; protein heterooligomerization; positive regulation of apoptosis; immune system process; macroautophagy; endosome transport; protein amino acid phosphorylation; protein localization; response to stress; autophagy; positive regulation of transcription from RNA polymerase II promoter; positive regulation of protein amino acid phosphorylation; regulation of I-kappaB kinase/NF-kappaB cascade; cell differentiation; positive regulation of macroautophagy; negative regulation of apoptosis
Reference #:  Q13501 (UniProtKB)
Alt. Names/Synonyms: A170; EBI3-associated protein of 60 kDa; EBI3-associated protein p60; EBIAP; ORCA; OSIL; oxidative stress induced like; p60; p62; p62B; PDB3; phosphotyrosine independent ligand for the Lck SH2 domain p62; Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa; sequestosome 1; Sequestosome-1; SQSTM; SQSTM1; Ubiquitin-binding protein p62; ZIP3
Gene Symbols: SQSTM1
Molecular weight: 47,687 Da
Basal Isoelectric point: 5.1  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SQSTM1

Protein Structure Not Found.


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Sites Implicated In
autophagy, induced: S403‑p
carcinogenesis, altered: T269‑p, S272‑p
cell cycle regulation: T269‑p, S272‑p
protein degradation: T269‑p, S272‑p
ubiquitination: T269‑p, S272‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 Y9-p ASLTVKAyLLGkEDA
0 1 K13-ac VKAyLLGkEDAAREI
0 50 K13-ub VKAyLLGkEDAAREI
1 72 S24-p AREIRRFsFCCsPEP
0 11 S28-p RRFsFCCsPEPEAEA
0 2 S49-p GPCERLLsRVAALFP
0 2 Y67-p PGGFQAHyRDEDGDL
0 32 K91-ub TMAMSYVkDDIFRIY
0 36 K141-ub PVVGTRYkCSVCPDy
0 46 Y148-p kCSVCPDyDLCsVCE
0 1 S152-p CPDyDLCsVCEGkGL
0 67 K157-ub LCsVCEGkGLHRGHT
0 29 K165-ub GLHRGHTkLAFPsPF
0 5 S170-p HTkLAFPsPFGHLsE
0 4 S176-p PsPFGHLsEGFSHsR
0 3 G178 PFGHLsEGFSHsRWL
0 3 S182-p LsEGFSHsRWLRkVk
0 5 K187-ub SHsRWLRkVkHGHFG
0 12 K189-ub sRWLRkVkHGHFGWP
1 15 S207-p MGPPGNWsPRPPRAG
0 1 S224-p RPGPTAEsAsGPSED
0 2 S226-p GPTAEsAsGPSEDPs
0 2 S233-p sGPSEDPsVNFLKNV
0 2 S249-p ESVAAALsPLGIEVD
0 25 K264-ub IDVEHGGkRsRLtPV
0 18 S266-p VEHGGkRsRLtPVsP
2 164 T269-p GGkRsRLtPVsPEss
0 6 V271 kRsRLtPVsPEssst
2 305 S272-p RsRLtPVsPEssstE
0 29 S275-p LtPVsPEssstEEks
0 33 S276-p tPVsPEssstEEksS
0 42 S277-p PVsPEssstEEksSs
0 11 T278-p VsPEssstEEksSsQ
0 1 K281-ub EssstEEksSsQPss
1 4 S282-p ssstEEksSsQPssC
0 7 S284-p stEEksSsQPssCCs
0 1 S287-p EksSsQPssCCsDPs
0 4 S288-p ksSsQPssCCsDPsk
0 5 S291-p sQPssCCsDPskPGG
0 2 S294-p ssCCsDPskPGGNVE
0 23 K295-ub sCCsDPskPGGNVEG
0 2 S306-p NVEGATQsLAEQMRk
0 2 R312 QsLAEQMRkIALESE
0 18 K313-ub sLAEQMRkIALESEG
0 1 S318 MRkIALESEGRPEEQ
0 13 S328-p RPEEQMEsDNCsGGD
1 20 S332-p QMEsDNCsGGDDDWt
0 3 T339-p sGGDDDWtHLsskEV
0 4 S342-p DDDWtHLsskEVDPs
0 4 S343-p DDWtHLsskEVDPsT
0 1 K344-ac DWtHLsskEVDPsTG
4 1 S349-p sskEVDPsTGELQsL
0 11 S355-p PsTGELQsLQMPEsE
0 8 S361-p QsLQMPEsEGPssLD
0 5 S365-p MPEsEGPssLDPsQE
1 16 S366-p PEsEGPssLDPsQEG
0 6 S370-p GPssLDPsQEGPtGL
0 3 T375-p DPsQEGPtGLkEAAL
0 2 K378-ac QEGPtGLkEAALyPH
0 3 Y383-p GLkEAALyPHLPPEA
3 2 S403-p ESLSQMLsMGFSDEG
0 27 K420-ub LTRLLQTkNYDIGAA
0 1 T430-p DIGAALDtIQyskHP
0 3 Y433-p AALDtIQyskHPPPL
0 2 S434-p ALDtIQyskHPPPL_
0 99 K435-ub LDtIQyskHPPPL__
13121 : Phospho-SQSTM1/p62 (Thr269/Ser272)
13121 : Phospho-SQSTM1/p62 (Thr269/Ser272)
14354 : Phospho-SQSTM1/p62 (Ser403) Antibody
  mouse

 
Y9 ASFTVKAYLLGkEEA
K13 VKAYLLGKEEATREI
K13-ub VKAYLLGkEEATREI
S24-p TREIRRFsFCFsPEP
S28-p RRFsFCFsPEPEAEA
S49 GPCERLLSRVAVLFP
Y67 PGGFQAHYRDEDGDL
K91-ub TMAMSYVkDDIFRIY
K141-ub PVVGTRYkCSVCPDy
Y148-p kCSVCPDyDLCSVCE
S152 CPDyDLCSVCEGkGL
K157-ub LCSVCEGkGLHREHS
K165-ub GLHREHSkLIFPNPF
N170 HSkLIFPNPFGHLSD
S176 PNPFGHLSDsFSHSR
S178-p PFGHLSDsFSHSRWL
S182 LSDsFSHSRWLRKLK
K187 SHSRWLRKLKHGHFG
K189 SRWLRKLKHGHFGWP
S207-p MGPPGNWsPRPPRAG
S224 RPCPTAESASAPPED
S226 CPTAESASAPPEDPN
N233 SAPPEDPNVNFLKNV
S249 ESVAAALSPLGIEVD
K264 IDVEHGGKRsRLtPt
S266-p VEHGGKRsRLtPttP
T269-p GGKRsRLtPttPEss
T271-p KRsRLtPttPEssst
T272-p RsRLtPttPEssstG
S275-p LtPttPEssstGTED
S276-p tPttPEssstGTEDK
S277-p PttPEssstGTEDKS
T278-p ttPEssstGTEDKSN
K283 sstGTEDKSNtQPSS
S284 stGTEDKSNtQPSSC
T286-p GTEDKSNtQPSSCSS
S289 DKSNtQPSSCSSEVs
S290 KSNtQPSSCSSEVsk
S293 tQPSSCSSEVskPDG
S296-p SSCSSEVskPDGAGE
K297-ub SCSSEVskPDGAGEG
S308-p AGEGPAQsLTEQMkk
K314-ub QsLTEQMkkIALEsV
K315-ub sLTEQMkkIALEsVG
S320-p MkkIALEsVGQPEEQ
S330-p QPEEQMEsGNCsGGD
S334-p QMEsGNCsGGDDDWt
T341-p sGGDDDWtHLSsKEV
S344 DDDWtHLSsKEVDPs
S345-p DDWtHLSsKEVDPsT
K346 DWtHLSsKEVDPsTG
S351-p SsKEVDPsTGELQsL
S357-p PsTGELQsLQMPEsE
S363-p QsLQMPEsEGPssLD
S367-p MPEsEGPssLDPsQE
S368-p PEsEGPssLDPsQEG
S372-p GPssLDPsQEGPTGL
T377 DPsQEGPTGLKEAAL
K380 QEGPTGLKEAALYPH
Y385 GLKEAALYPHLPPEA
S405 ESLSQMLSMGFSDEG
K422-ub LTRLLQTkNYDIGAA
T432 DIGAALDTIQYSkHP
Y435 AALDTIQYSkHPPPL
S436 ALDTIQYSkHPPPL_
K437-ub LDTIQYSkHPPPL__
13121 : Phospho-SQSTM1/p62 (Thr269/Ser272)
13121 : Phospho-SQSTM1/p62 (Thr269/Ser272)
14354 : Phospho-SQSTM1/p62 (Ser403) Antibody
  rat

 
Y9 ASLTVKAYLLGKEEA
K13 VKAYLLGKEEAAREI
K13 VKAYLLGKEEAAREI
S24-p AREIRRFsFCFSPEP
S28 RRFsFCFSPEPEAEA
S47 GPCERLLSRVAVLFP
Y65 PGGFQAHYRDEDGDL
K89 TMAMSYVKDDIFRIY
K138 PVVGTRYKCSVCPDY
Y145 KCSVCPDYDLCSVCE
S149 CPDYDLCSVCEGKGL
K154 LCSVCEGKGLHREHS
K162 GLHREHSKLIFPNPF
N167 HSKLIFPNPFGHLSD
S173 PNPFGHLSDSFSHSR
S175 PFGHLSDSFSHSRWL
S179 LSDSFSHSRWLRKLK
K184 SHSRWLRKLKHGHFG
K186 SRWLRKLKHGHFGWP
S204 MGPPGNWSPRPPRAG
S221 RPCPTAESASAPSED
S223 CPTAESASAPSEDPN
N230 SAPSEDPNVNFLKNV
S246 ESVAAALSPLGIEVD
K261 IDVEHGGKRSRLtPT
S263 VEHGGKRSRLtPTSA
T266-p GGKRSRLtPTSAESS
T268 KRSRLtPTSAESSST
S269 RSRLtPTSAESSSTG
S272 LtPTSAESSSTGTED
S273 tPTSAESSSTGTEDK
S274 PTSAESSSTGTEDKS
T275 TSAESSSTGTEDKSG
K280 SSTGTEDKSGTQPSS
S281 STGTEDKSGTQPSSC
T283 GTEDKSGTQPSSCSS
S286 DKSGTQPSSCSSEVS
S287 KSGTQPSSCSSEVSK
S290 TQPSSCSSEVSKPDG
S293 SSCSSEVSKPDGAGE
K294 SCSSEVSKPDGAGEG
S305 AGEGPAQSLTEQMKK
K311 QSLTEQMKKIALESV
K312 SLTEQMKKIALESVG
S317 MKKIALESVGQPEEL
S327 QPEELMESDNCSGGD
S331 LMESDNCSGGDDDWT
T338 SGGDDDWTHLSSKEV
S341 DDDWTHLSSKEVDPS
S342 DDWTHLSSKEVDPST
K343 DWTHLSSKEVDPSTG
S348 SSKEVDPSTGELQsL
S354-p PSTGELQsLQMPEsE
S360-p QsLQMPEsEGPSsLD
S364 MPEsEGPSsLDPSQE
S365-p PEsEGPSsLDPSQEG
S369 GPSsLDPSQEGPTGL
T374 DPSQEGPTGLKEAAL
K377 QEGPTGLKEAALYPH
Y382 GLKEAALYPHLPPEA
S402 ESLSQMLSMGFSDEG
K419 LTRLLQTKNYDIGAA
T429 DIGAALDTIQYSKHP
Y432 AALDTIQYSKHPPPL
S433 ALDTIQYSKHPPPL_
K434 LDTIQYSKHPPPL__
13121 : Phospho-SQSTM1/p62 (Thr269/Ser272)
13121 : Phospho-SQSTM1/p62 (Thr269/Ser272)
14354 : Phospho-SQSTM1/p62 (Ser403) Antibody
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