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Protein Page:
SHMT2 (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
SHMT2 Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Interconversion of serine and glycine. Associates with mitochondrial DNA. Belongs to the SHMT family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 2.1.2.1; Amino Acid Metabolism - glycine, serine and threonine; Methyltransferase; Energy Metabolism - methane; Cofactor and Vitamin Metabolism - one carbon pool by folate; Other Amino Acids Metabolism - cyanoamino acid; Mitochondrial
Cellular Component: microtubule cytoskeleton; mitochondrion; mitochondrial matrix; mitochondrial inner membrane; mitochondrial intermembrane space
Molecular Function: L-allo-threonine aldolase activity; amino acid binding; identical protein binding; glycine hydroxymethyltransferase activity; chromatin binding; pyridoxal phosphate binding
Biological Process: L-serine biosynthetic process; positive regulation of cell proliferation; one-carbon compound metabolic process; glycine biosynthetic process from serine; protein homotetramerization
Reference #:  P34897 (UniProtKB)
Alt. Names/Synonyms: GLY A+; GLYA; glycine auxotroph A, human complement for hamster; Glycine hydroxymethyltransferase; GLYM; serine aldolase; serine hydroxymethylase; serine hydroxymethyltransferase 2 (mitochondrial); Serine hydroxymethyltransferase, mitochondrial; Serine methylase; SHMT; SHMT2; threonine aldolase
Gene Symbols: SHMT2
Molecular weight: 55,993 Da
Basal Isoelectric point: 8.76  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SHMT2

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 1 Y3-p _____MLyFSLFWAA
0 2 S90-p AALEALGsCLNNkyS
0 7 K95-ac LGsCLNNkySEGyPG
0 2 K95-ub LGsCLNNkySEGyPG
0 3 Y96-p GsCLNNkySEGyPGk
0 1 Y100-p NNkySEGyPGkRYYG
0 54 K103-ac ySEGyPGkRYYGGAE
0 1 K103-ub ySEGyPGkRYYGGAE
0 1 K103-sc ySEGyPGkRYYGGAE
0 42 K181-ac HGYMSDVkRISATSI
0 2 K181-ub HGYMSDVkRISATSI
0 1 K181 HGYMSDVKRISATSI
0 1 K196-ac FFESMPYkLNPkTGL
0 7 K200-ub MPYkLNPkTGLIDYN
0 1 K200-sc MPYkLNPkTGLIDYN
0 2 K200-ac MPYkLNPkTGLIDYN
0 3 Y228-p IIAGTSAyARLIDYA
0 5 K245-ac REVCDEVkAHLLADM
0 2 K269-ac KVIPSPFkHADIVTT
0 1 K269-sc KVIPSPFkHADIVTT
0 1 K280-ub IVTTTTHkTLRGARS
0 1 K297-ac IFYRKGVkAVDPkTG
0 1 K302-ac GVkAVDPkTGREIPY
0 1 K302-sc GVkAVDPkTGREIPY
0 1 R305 AVDPkTGREIPYTFE
0 1 R305 AVDPkTGREIPYTFE
0 1 K356-ac EYSLQVLkNARAMAD
0 1 K356-sc EYSLQVLkNARAMAD
0 18 E367 AMADALLERGYSLVS
0 1 E367 AMADALLERGYSLVS
0 1 E367 AMADALLERGYSLVS
0 1 S404-p ERVLELVsITANkNT
0 1 K409-ac LVsITANkNTCPGDR
0 1 K409-sc LVsITANkNTCPGDR
0 1 S417 NTCPGDRSAItPGGL
0 4 T420-p PGDRSAItPGGLRLG
0 1 K459 VNIGLEVKSKTAkLQ
0 3 K464-ac EVKSKTAkLQDFksF
0 1 K464-sc EVKSKTAkLQDFksF
0 149 K469-ac TAkLQDFksFLLkDS
0 2 K469-m2 TAkLQDFksFLLkDS
0 3 K469-ub TAkLQDFksFLLkDS
0 1 K469-sc TAkLQDFksFLLkDS
0 1 S470-p AkLQDFksFLLkDSE
0 10 K474-ac DFksFLLkDSETSQR
0 3 K474-ub DFksFLLkDSETSQR
0 1 K474-sc DFksFLLkDSETSQR
  mouse

 
S3 _____MVSFSLLRTT
S90 AALEALGSCLNNkYS
K95 LGSCLNNKYSEGYPG
K95-ub LGSCLNNkYSEGYPG
Y96 GSCLNNkYSEGYPGk
Y100 NNkYSEGYPGkRYYG
K103-ac YSEGYPGkRYYGGAE
K103 YSEGYPGKRYYGGAE
K103-sc YSEGYPGkRYYGGAE
K181-ac HGYMSDVkRISATSI
K181-ub HGYMSDVkRISATSI
K181-sc HGYMSDVkRISATSI
K196 FFESMPYKLNPQTGL
Q200 MPYKLNPQTGLIDYD
Q200 MPYKLNPQTGLIDYD
Q200 MPYKLNPQTGLIDYD
Y228 IIAGTSAYARLIDYA
R245 REVCDEVRAHLLADM
K269-ac KVIPSPFkYADVVTT
K269-sc KVIPSPFkYADVVTT
K280 VVTTTTHKTLRGARS
R297 IFYRKGVRTVDPKTG
K302 GVRTVDPKTGkEIPY
K302 GVRTVDPKTGkEIPY
K305-ac TVDPKTGkEIPYTFE
K305-sc TVDPKTGkEIPYTFE
R356 EYSLQVLRNAQAMAD
R356 EYSLQVLRNAQAMAD
K367-ac AMADALLkRGYSLVS
K367-ub AMADALLkRGYSLVS
K367-sc AMADALLkRGYSLVS
S404 ERVLELVSITANKNT
K409 LVSITANKNTCPGDR
K409 LVSITANKNTCPGDR
S417-p NTCPGDRsAItPGGL
T420-p PGDRsAItPGGLRLG
K459-sc VNIGLEVkRKTAkLQ
K464-ac EVkRKTAkLQDFkSF
K464 EVkRKTAKLQDFkSF
K469-ac TAkLQDFkSFLLkDP
K469 TAkLQDFKSFLLkDP
K469-ub TAkLQDFkSFLLkDP
K469-sc TAkLQDFkSFLLkDP
S470 AkLQDFkSFLLkDPE
K474-ac DFkSFLLkDPETSQR
K474-ub DFkSFLLkDPETSQR
K474-sc DFkSFLLkDPETSQR
  rat

 
P3 _____MVPFSLLRTT
S90 AALEALGSCLNNKYS
K95 LGSCLNNKYSEGYPG
K95 LGSCLNNKYSEGYPG
Y96 GSCLNNKYSEGYPGk
Y100 NNKYSEGYPGkRYYG
K103-ac YSEGYPGkRYYGGAE
K103 YSEGYPGKRYYGGAE
K103 YSEGYPGKRYYGGAE
K181-ac HGYMSDVkRISATSI
K181 HGYMSDVKRISATSI
K181 HGYMSDVKRISATSI
K196 FFESMPYKLNPQTGL
Q200 MPYKLNPQTGLIDYD
Q200 MPYKLNPQTGLIDYD
Q200 MPYKLNPQTGLIDYD
Y228 IIAGTSAYARLIDYA
K245 REVCDEVKAHLLADM
K269-ac KVIPSPFkYADIVTT
K269 KVIPSPFKYADIVTT
K280 IVTTTTHKTLRGARS
R297 IFYRKGVRTVDPkTG
K302-ac GVRTVDPkTGQEIPY
K302 GVRTVDPKTGQEIPY
Q305 TVDPkTGQEIPYTFE
Q305 TVDPkTGQEIPYTFE
R356 EYSLQVLRNAQAMAD
R356 EYSLQVLRNAQAMAD
K367-ac AMADALLkRGYSLVS
K367 AMADALLKRGYSLVS
K367 AMADALLKRGYSLVS
S404 ERVLELVSITANKNT
K409 LVSITANKNTCPGDR
K409 LVSITANKNTCPGDR
S417 NTCPGDRSAITPGGL
T420 PGDRSAITPGGLRLG
K459 VNIGLEVKRKTAkLQ
K464-ac EVKRKTAkLQDFkSF
K464 EVKRKTAKLQDFkSF
K469-ac TAkLQDFkSFLLkDP
K469 TAkLQDFKSFLLkDP
K469 TAkLQDFKSFLLkDP
K469 TAkLQDFKSFLLkDP
S470 AkLQDFkSFLLkDPE
K474-ac DFkSFLLkDPETSQR
K474 DFkSFLLKDPETSQR
K474 DFkSFLLKDPETSQR
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