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Protein Page:
SAE2 (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
SAE2 a protein of the ubiquitin-activating E1 family. Acts as a UBL1 E1 ligase. Mediates ATP-dependent activation of UBL1 and formation of a thiolester with a conserved cysteine residue on SAE2. Note: This description may include information from UniProtKB.
Protein type: EC 6.3.2.-; Ubiquitin conjugating system; Ligase; EC 6.3.2.19; Motility/polarity/chemotaxis; Ubiquitin ligase
Cellular Component: nucleoplasm; cytoplasm
Molecular Function: SUMO activating enzyme activity; protein binding; protein heterodimerization activity; metal ion binding; enzyme activator activity; transcription factor binding; ATP binding; ligase activity
Biological Process: positive regulation of catalytic activity; cellular protein metabolic process; protein sumoylation; post-translational protein modification
Reference #:  Q9UBT2 (UniProtKB)
Alt. Names/Synonyms: Anthracycline-associated resistance ARX; ARX; FLJ13058; HRIHFB2115; SAE2; SUMO-1 activating enzyme subunit 2; SUMO-activating enzyme subunit 2; SUMO1 activating enzyme subunit 2; UBA2; UBA2, ubiquitin-activating enzyme E1 homolog; Ubiquitin-like 1-activating enzyme E1B; ubiquitin-like modifier activating enzyme 2; UBLE1B
Gene Symbols: UBA2
Molecular weight: 71,224 Da
Basal Isoelectric point: 5.15  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SAE2

Protein Structure Not Found.


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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 R5 ___MALSRGLPRELA
0 2 K65-u NRQFLFQkKHVGRSK
0 1 K77-u RSKAQVAkESVLQFY
0 2 K152-u LGQVTTIkKGVTECY
1 0 K190-s IHCIVWAkYLFNQLF
0 4 S207-p EDADQEVsPDRADPE
0 1 K236-a SNEDGDIkRISTkEW
2 0 K236-s SNEDGDIkRISTkEW
0 1 K241-a DIkRISTkEWAkSTG
0 1 K241-u DIkRISTkEWAkSTG
0 2 K245-u ISTkEWAkSTGYDPV
0 14 K253-a STGYDPVkLFTkLFK
0 2 K253-u STGYDPVkLFTkLFK
0 2 K257-u DPVkLFTkLFKDDIR
2 0 K257-s DPVkLFTkLFKDDIR
0 1 Y265-p LFKDDIRyLLTMDkL
0 1 K271-a RyLLTMDkLWRkRKP
0 1 K271-m1 RyLLTMDkLWRkRKP
0 1 K271-u RyLLTMDkLWRkRKP
2 0 K271-s RyLLTMDkLWRkRKP
1 0 K275-s TMDkLWRkRKPPVPL
0 8 S289-p LDWAEVQsQGEETNA
0 2 K316-u DQQVLDVkSYARLFS
0 1 K324-a SYARLFSkSIETLRV
0 2 K324-u SYARLFSkSIETLRV
0 2 K336-u LRVHLAEkGDGAELI
0 1 K420-u CRTIFLNkQPNPRKK
0 1 K467 TVLTLQDKIVKEkFA
0 1 K472-u QDKIVKEkFAMVAPD
0 1 K505 TEANNHKKLsEFGIR
0 2 S507-p ANNHKKLsEFGIRNG
0 1 K540-s LHSEDLGkDVEFEVV
0 10 A550 EFEVVGDAPEKVGPK
0 1 S577-p SDDGAQPstSTAQEQ
0 1 T578-p DDGAQPstSTAQEQD
0 1 T580 GAQPstSTAQEQDDV
0 8 S592-p DDVLIVDsDEEDSsN
0 1 S598-p DsDEEDSsNNADVSE
1 0 K611-s SEEERSRkRkLDEkE
1 0 K613-s EERSRkRkLDEkENL
0 1 K617-a RkRkLDEkENLSAkR
1 0 K617-s RkRkLDEkENLSAkR
0 86 K623-a EkENLSAkRSRIEQk
2 0 K623-s EkENLSAkRSRIEQk
2 0 K630-s kRSRIEQkEELDDVI
  mouse

 
R5-m1 ___MALSrGLPRELA
K65-u NRQFLFQkKHVGRSK
K77 RSKAQVAKESVLQFH
K152 LGQVTTIKKGVTECY
K190 IHCIVWAKYLFNQLF
S207-p EDADQEVsPDRADPE
K236 SNEDGDIKRISTKEW
K236 SNEDGDIKRISTKEW
K241 DIKRISTKEWAkSTG
K241 DIKRISTKEWAkSTG
K245-u ISTKEWAkSTGYDPV
K253 STGYDPVKLFTkLFK
K253-u STGYDPVkLFTkLFK
K257-u DPVkLFTkLFKDDIR
K257 DPVkLFTKLFKDDIR
Y265 LFKDDIRYLLTMDKL
K271 RYLLTMDKLWRKRKP
K271 RYLLTMDKLWRKRKP
K271 RYLLTMDKLWRKRKP
K271 RYLLTMDKLWRKRKP
K275 TMDKLWRKRKPPVPL
S289 LDWAEVQSQGEANAD
K314 DQQVLDVKSYASLFS
K322 SYASLFSKSIETLRV
K322-u SYASLFSkSIETLRV
K334-u LRVHLAEkGDGAELI
K418 CRTIFLNKQPNPRKK
K465-u TVLTLQDkIVKEKFA
K470 QDkIVKEKFAMVAPD
K503-u TEANNPKkLSDFGIR
S505 ANNPKkLSDFGIRNG
K538 LHSEDLGKDVEFEVV
S548-p EFEVVGDsPEKVGPK
S575-p SDDGAQPsTStAQEQ
T576 DDGAQPsTStAQEQD
T578-p GAQPsTStAQEQDDV
S590-p DDVLIVDsDEEGPSN
S596 DsDEEGPSNSTDCSG
K609 SGDDKARKRKLEENE
K611 DDKARKRKLEENEAA
N615 RKRKLEENEAASTkK
N615 RKRKLEENEAASTkK
K621-a ENEAASTkKCRLEQM
K621 ENEAASTKKCRLEQM
M628 kKCRLEQMEDPDDVI
  rat

 
R5 ___MSLSRGLPRELA
K65 NRQFLFQKKHVGRSK
K77 RSKAQVAKESVLQFH
K152 LGQVTTIKKGVTECY
K190 IHCIVWAKYLFNQLF
S207 EDADQEVSPDRADPE
K236 SNEDGDIKRISTKEW
K236 SNEDGDIKRISTKEW
K241 DIKRISTKEWAKSTG
K241 DIKRISTKEWAKSTG
K245 ISTKEWAKSTGYDPV
K253 STGYDPVKLFTKLFK
K253 STGYDPVKLFTKLFK
K257 DPVKLFTKLFKDDIR
K257 DPVKLFTKLFKDDIR
Y265 LFKDDIRYLLTMDKL
K271 RYLLTMDKLWRKRKP
K271 RYLLTMDKLWRKRKP
K271 RYLLTMDKLWRKRKP
K271 RYLLTMDKLWRKRKP
K275 TMDKLWRKRKPPVPL
S289 LDWAEVQSQGEEANA
K315 DQQVLDVKSYASLFS
K323 SYASLFSKSIETLRV
K323 SYASLFSKSIETLRV
K335 LRVRLAEKGDGAELI
K419 CRTIFLNKQPNPRKK
K466 TVLTLQDKIVKEKFA
K471 QDKIVKEKFAMVAPD
K504 TEANNPKKLSDFGIR
S506 ANNPKKLSDFGIRNG
K539 LHSEDLGKDVEFEVV
T549-p EFEVVGDtPEKVGPK
S576 SDDGAQPSTSTAQEQ
T577 DDGAQPSTSTAQEQD
T579 GAQPSTSTAQEQDDV
S591-p DDVLIVDsDEEGPSN
S597 DsDEEGPSNSADGSR
K610 SRDDRTRKRKLEENE
K612 DDRTRKRKLEENEGA
N616 RKRKLEENEGASTKK
N616 RKRKLEENEGASTKK
K622 ENEGASTKKSRLEQV
K622 ENEGASTKKSRLEQV
V629 KKSRLEQVEDQDDVI
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