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PhosphoSitePlus
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Protein Page:
SSB (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
SSB a nuclear protein that plays a role in the transcription of RNA polymerase III. It is most probably a transcription termination factor. Binds to the 3' termini of virtually all nascent polymerase III transcripts. It is associated with precursor forms of RNA polymerase III transcripts including tRNA and 4.5S, 5s, 7s, and 7-2 RNAs. Note: This description may include information from UniProtKB.
Protein type: Transcription initiation complex
Cellular Component: nucleus; ribonucleoprotein complex
Molecular Function: mRNA binding; protein binding; nucleotide binding; tRNA binding
Biological Process: histone mRNA metabolic process; tRNA modification
Reference #:  P05455 (UniProtKB)
Alt. Names/Synonyms: autoantigen La; La; La autoantigen; La ribonucleoprotein; La ribonucleoprotein domain family, member 3; LARP3; Lupus La protein; Sjoegren syndrome type B antigen; Sjogren syndrome antigen B (autoantigen La); SS-B; SS-B/La protein; SSB
Gene Symbols: SSB
Molecular weight: 46,837 Da
Basal Isoelectric point: 6.68  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SSB

Protein Structure Not Found.


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Sites Implicated In
transcription, induced: S366‑p
transcription, inhibited: S366‑p
activity, induced: S366‑p
activity, inhibited: S366‑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 1 K9-u AENGDNEkMAALEAK
0 4 Y23-p KICHQIEyyFGDFNL
0 2 Y24-p ICHQIEyyFGDFNLP
1 0 K41-s KFLKEQIkLDEGWVP
0 5 K74-u VIVEALSkSkAELME
0 9 K76-u VEALSkSkAELMEIS
0 6 S92-p DKTKIRRsPskPLPE
0 4 S94-p TKIRRsPskPLPEVT
0 1 K95-u KIRRsPskPLPEVTD
0 2 Y104-p LPEVTDEyKNDVKNR
0 1 K116-a KNRSVYIkGFPtDAT
0 2 K116-u KNRSVYIkGFPtDAT
0 1 T120-p VYIkGFPtDATLDDI
0 1 K128-a DATLDDIkEWLEDKG
0 1 K165 FDSIESAKKFVETPG
0 2 K174-u FVETPGQkYkEtDLL
0 1 K176-u ETPGQkYkEtDLLIL
0 2 T178-p PGQkYkEtDLLILFk
0 3 K185-a tDLLILFkDDyFAKK
0 38 Y188-p LILFkDDyFAKKNEE
1 0 N199 KNEERKQNKVEAKLR
0 1 K216-u QEQEAKQkLEEDAEM
0 1 K224-u LEEDAEMksLEEkIG
0 1 S225-p EEDAEMksLEEkIGC
0 2 K229-u EMksLEEkIGCLLKF
0 3 K285-a KAKEALGkAkDANNG
0 2 K287-u KEALGkAkDANNGNL
1 1 T302-p QLRNKEVtWEVLEGE
0 1 E304 RNKEVtWEVLEGEVE
0 1 K312 VLEGEVEKEALKKII
0 1 S325-p IIEDQQEsLNkWKSK
0 6 K328-a DQQEsLNkWKSKGRR
0 43 K328-u DQQEsLNkWKSKGRR
0 1 - gap
0 15 K354-a QPGSGKGkVQFQGkk
0 3 K354 QPGSGKGKVQFQGkk
0 1 K354 QPGSGKGKVQFQGkk
0 103 K360-a GkVQFQGkktKFAsD
0 3 K361-a kVQFQGkktKFAsDD
0 6 T362-p VQFQGkktKFAsDDE
8 148 S366-p GkktKFAsDDEHDEH
0 1 T379-p EHDENGAtGPVKRAR
0 138 T389-p VKRAREEtDkEEPAS
0 4 K391-a RAREEtDkEEPASkQ
0 4 K397-u DkEEPASkQQKTENG
  mouse

 
K9 AENGDNEKMTALEAK
Y23 KICHQIEYYFGDFNL
Y24 ICHQIEYYFGDFNLP
K41 KFLKEQIKLDEGWVP
K74 VIVQALSKSKAKLME
K76 VQALSKSKAKLMEVS
S92-p DKTKIRRsPsRPLPE
S94-p TKIRRsPsRPLPEVT
R95 KIRRsPsRPLPEVTD
Y104 LPEVTDEYKNDVKNR
K116 KNRSVYIKGFPTDAT
K116-u KNRSVYIkGFPTDAT
T120 VYIkGFPTDATLDDI
K128 DATLDDIKEWLDDKG
K165-u FDSIQSAkKFVEIPG
K174 FVEIPGQKYKDTNLL
K176 EIPGQKYKDTNLLIL
T178 PGQKYKDTNLLILFK
K185 TNLLILFKEDYFAKK
Y188 LILFKEDYFAKKNEE
S199-p KNEERKQsKVEAKLK
K216 QEHEGRHKPGSTETR
R223 KPGSTETRALEGkMG
A224 PGSTETRALEGkMGC
K228-u ETRALEGkMGCLLKF
K284 KAKEALEKARNANNG
R286 KEALEKARNANNGNL
T301-p LLRNKKVtWkVLEGH
K303-u RNKKVtWkVLEGHAE
K311-u VLEGHAEkEALKKIT
S324 ITDDQQESLNkWKSK
K327 DQQESLNKWKSKGGH
K327-u DQQESLNkWKSKGGH
K340-u GHAGGRFkGSHVFTA
R369 YAGAPKGRGQFHGRR
R369-m1 YAGAPKGrGQFHGRR
R369-m2 YAGAPKGrGQFHGRR
R375 GrGQFHGRRTRFDDD
R376 rGQFHGRRTRFDDDD
T377 GQFHGRRTRFDDDDR
- gap
- gap
R396 MKRGRDGRDREEPAS
R398 RGRDGRDREEPASKH
K404 DREEPASKHKKRENG
  rat

 
K9 AENGDNEKMAALEAK
Y23 KICHQIEYYFGDFNL
Y24 ICHQIEYYFGDFNLP
K41 KFLKEQIKLDEGWVP
K74 VIVQALSKSKANLME
K76 VQALSKSKANLMEVS
S92 DKTKIRRSPSRPLPE
S94 TKIRRSPSRPLPEVT
R95 KIRRSPSRPLPEVTD
Y104 LPEVTDEYKNDVKNR
K116 KNRSVYIKGFPTDAT
K116 KNRSVYIKGFPTDAT
T120 VYIKGFPTDATLDDI
K128 DATLDDIKEWLDDKG
K165 FDSIQSAKKFVDTPG
K174 FVDTPGQKYKDTNLL
K176 DTPGQKYKDTNLLIL
T178 PGQKYKDTNLLILFK
K185 TNLLILFKEDYFAKK
Y188 LILFKEDYFAKKNEE
S199 KNEERKQSKVEAKLK
K216 QEHEGRHKPGSTETR
R223 KPGSTETRALEGKMG
A224 PGSTETRALEGKMGC
K228 ETRALEGKMGCLLKF
K284 KAKDALEKARSANNG
R286 KDALEKARSANNGNL
T301 LLRNKKVTWKVLEGH
K303 RNKKVTWKVLEGHAE
K311 VLEGHAEKDAMKKIT
S324 ITDDQQESLNKWKSK
K327 DQQESLNKWKSKGGH
K327 DQQESLNKWKSKGGH
K340 GHAARRFKGSHVFTA
R369 YAGAPKGRGQFQGRR
R369 YAGAPKGRGQFQGRR
R369 YAGAPKGRGQFQGRR
R375 GRGQFQGRRTRFDDD
R376 RGQFQGRRTRFDDDD
T377 GQFQGRRTRFDDDDH
- gap
- gap
R396 VKRGIDGRDREEPAS
R398 RGIDGRDREEPASKH
K404 DREEPASKHKKRENG
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