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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
g O-GlcNAc
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 6.3.2.19; Ubiquitin ligase; Ligase; EC 6.3.2.-; Ubiquitin conjugating system; Motility/polarity/chemotaxis
Cellular Component: nucleus
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; protein sumoylation
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 1 R9 ALSRGLPRELAEAVA
0 2 K65-u NRQFLFQkKHVGRSK
0 1 K77-u RSKAQVAkESVLQFY
0 1 K86-u SVLQFYPkANIVAYH
0 2 K152-u LGQVTTIkkGVTECY
0 1 K153-u GQVTTIkkGVTECYE
0 3 S207-p EDADQEVsPDRADPE
0 1 K236-a SNEDGDIkRISTkEW
1 0 K236-s SNEDGDIkRISTkEW
0 1 K241-a DIkRISTkEWAkSTG
0 1 K241-u DIkRISTkEWAkSTG
0 2 K245-u ISTkEWAkSTGyDPV
0 1 Y249-p EWAkSTGyDPVkLFT
0 14 K253-a STGyDPVkLFTkLFK
0 2 K253-u STGyDPVkLFTkLFK
0 2 K257-u DPVkLFTkLFKDDIR
1 0 K257-s DPVkLFTkLFKDDIR
0 1 Y265-p LFKDDIRyLLTMDkL
0 1 K271-a RyLLTMDkLWRKRKP
0 1 K271-u RyLLTMDkLWRKRKP
1 0 K271-s RyLLTMDkLWRKRKP
0 8 S289-p LDWAEVQsQGEEtNA
0 1 T294-p VQsQGEEtNASDQQN
0 2 K316-u DQQVLDVkSYARLFS
0 1 K324-a SYARLFSkSIEtLRV
0 2 K324-u SYARLFSkSIEtLRV
0 1 T328-p LFSkSIEtLRVHLAE
0 1 K336-a LRVHLAEkGDGAELI
0 2 K336-u LRVHLAEkGDGAELI
0 1 K420-u CRTIFLNkQPNPRKK
0 1 K467 TVLTLQDKIVKEkFA
0 1 K472-u QDKIVKEkFAMVAPD
0 1 K505 TEANNHKKLsEFGIR
0 1 S507-p ANNHKKLsEFGIRNG
0 1 K540-s LHSEDLGkDVEFEVV
0 8 A550 EFEVVGDAPEKVGPK
0 1 S577 SDDGAQPStSTAQEQ
0 1 T578-p DDGAQPStSTAQEQD
0 6 S592-p DDVLIVDsDEEDSsN
0 1 S598-p DsDEEDSsNNADVSE
0 1 K617-a RKRKLDEkENLSAkR
0 1 S621 LDEkENLSAkRSRIE
0 86 K623-a EkENLSAkRSRIEQk
1 0 K623-s EkENLSAkRSRIEQk
1 0 K630-s kRSRIEQkEELDDVI
  mouse

 
R5-m1 ___MALSrGLPrELA
R9-m1 ALSrGLPrELAEAVS
K65-u NRQFLFQkKHVGRSK
K77 RSKAQVAKESVLQFH
Q86 SVLQFHPQANIEAHH
K152 LGQVTTIKKGVTECY
K153 GQVTTIKKGVTECYE
S207-p EDADQEVsPDRADPE
K236 SNEDGDIKRISTKEW
K236 SNEDGDIKRISTKEW
K241 DIKRISTKEWAkSTG
K241 DIKRISTKEWAkSTG
K245-u ISTKEWAkSTGYDPV
Y249 EWAkSTGYDPVkLFT
K253 STGYDPVKLFTkLFK
K253-u STGYDPVkLFTkLFK
K257-u DPVkLFTkLFKDDIR
K257 DPVkLFTKLFKDDIR
Y265 LFKDDIRYLLTMDKL
K271 RYLLTMDKLWRKRKP
K271 RYLLTMDKLWRKRKP
K271 RYLLTMDKLWRKRKP
S289 LDWAEVQSQGEANAD
N294 VQSQGEANADQQNEP
K314 DQQVLDVKSYASLFS
K322 SYASLFSKSIETLRV
K322-u SYASLFSkSIETLRV
T326 LFSkSIETLRVHLAE
K334 LRVHLAEKGDGAELI
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
S590-p DDVLIVDsDEEGPSN
S596 DsDEEGPSNSTDCSG
N615 RKRKLEENEAAsTkK
S619-p LEENEAAsTkKCRLE
K621-a ENEAAsTkKCRLEQM
K621 ENEAAsTKKCRLEQM
M628 kKCRLEQMEDPDDVI
  rat

 
R5 ___MSLSRGLPRELA
R9 SLSRGLPRELAEAVS
K65 NRQFLFQKKHVGRSK
K77 RSKAQVAKESVLQFH
Q86 SVLQFHPQANIEAHH
K152 LGQVTTIKKGVTECY
K153 GQVTTIKKGVTECYE
S207 EDADQEVSPDRADPE
K236 SNEDGDIKRISTKEW
K236 SNEDGDIKRISTKEW
K241 DIKRISTKEWAKSTG
K241 DIKRISTKEWAKSTG
K245 ISTKEWAKSTGYDPV
Y249 EWAKSTGYDPVKLFT
K253 STGYDPVKLFTKLFK
K253 STGYDPVKLFTKLFK
K257 DPVKLFTKLFKDDIR
K257 DPVKLFTKLFKDDIR
Y265 LFKDDIRYLLTMDKL
K271 RYLLTMDKLWRKRKP
K271 RYLLTMDKLWRKRKP
K271 RYLLTMDKLWRKRKP
S289 LDWAEVQSQGEEANA
A294 VQSQGEEANADQQSE
K315 DQQVLDVKSYASLFS
K323 SYASLFSKSIETLRV
K323 SYASLFSKSIETLRV
T327 LFSKSIETLRVRLAE
K335 LRVRLAEKGDGAELI
K335 LRVRLAEKGDGAELI
K419 CRTIFLNKQPNPRKK
K466 TVLTLQDKIVKEKFA
K471 QDKIVKEKFAMVAPD
K504 TEANNPKKLSDFGIR
S506 ANNPKKLSDFGIRNG
K539 LHSEDLGKDVEFEVV
T549 EFEVVGDTPEKVGPK
S576 SDDGAQPSTSTAQEQ
T577 DDGAQPSTSTAQEQD
S591 DDVLIVDSDEEGPSN
S597 DSDEEGPSNSADGSR
N616 RKRKLEENEGASTKK
S620 LEENEGASTKKSRLE
K622 ENEGASTKKSRLEQV
K622 ENEGASTKKSRLEQV
V629 KKSRLEQVEDQDDVI
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