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Protein Page:
SLC19A1 (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
SLC19A1 a transporter protein. Transports reduced folate, antitumor agents and folate antagonists such as methotrexate. Apparently involved in methotrexate resistance in various cancers and neural tube defects. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; Transporter
Cellular Component: membrane; integral to plasma membrane; plasma membrane
Molecular Function: folic acid transporter activity; methotrexate transporter activity; reduced folate carrier activity; folic acid binding
Biological Process: methotrexate transport; vitamin metabolic process; folic acid metabolic process; water-soluble vitamin metabolic process; folic acid transport
Reference #:  P41440 (UniProtKB)
Alt. Names/Synonyms: CHMD; FLOT1; Folate transporter 1; FOLT; IFC-1; IFC1; intestinal folate carrier; Intestinal folate carrier 1; Placental folate transporter; Reduced folate carrier protein; REFC; RFC; RFC1; S19A1; SLC19A1; solute carrier family 19 (folate transporter), member 1; Solute carrier family 19 member 1
Gene Symbols: SLC19A1
Molecular weight: 64,868 Da
Basal Isoelectric point: 9.15  Predict pI for various phosphorylation states
Select Structure to View Below

SLC19A1
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 K10-u PSSPAVEkQVPVEPG
0 1 Y35-p LVCYLCFyGFMAQIR
0 1 Y51-p GESFITPyLLGPDKN
0 1 Y136 TMAARIAYSSYIFSL
0 1 S137 MAARIAYSSYIFSLV
0 1 A147 IFSLVRPARYQRVAG
0 25 T222-p DDRGRCEtsAsELER
0 1 S223-p DRGRCEtsAsELERM
0 15 S225-p GRCEtsAsELERMNP
0 5 K237-u MNPGPGGkLGHALRV
0 1 Y305-p TTNSARVyNGAADAA
0 1 S335-p KIRWARWsKLLIAGV
0 1 S474-p PPAQGLRsAAEEkAA
0 1 K479 LRsAAEEKAAQALSV
0 50 K479-u LRsAAEEkAAQALSV
0 1 A480 RsAAEEkAAQALSVQ
0 2 S485 EkAAQALSVQDkGLG
0 2 K489-u QALSVQDkGLGGLQP
0 1 S499-p GGLQPAQsPPLsPED
0 1 S503-p PAQsPPLsPEDSLGA
0 1 P504 AQsPPLsPEDSLGAV
0 1 S515-p LGAVGPAsLEQRQsD
0 1 S521-p AsLEQRQsDPyLAQA
0 5 Y524-p EQRQsDPyLAQAPAP
0 1 S583-p LGLQCLPsDGVQNVN
  mouse

 
K10 PTGQVAEKQAYEEPR
F35 LVFYLCFFGFMAQLR
F51 GESFITPFLLERKFT
Y134-p TMAARIAysSYIFSL
S135-p MAARIAysSYIFSLV
S145-p IFSLVHPsRYQRMAS
A219 RSTLARGALPCELDQ
L220 STLARGALPCELDQM
C222 LARGALPCELDQMHP
K238 PDRPETRKLDRMLGT
Y301 STDSSLSYNGAVDAA
S331 SIRWTLWSKLVIAGV
S467-p AQAQELRsPLEtsVQ
T471-p ELRsPLEtsVQAIsL
T471 ELRsPLETsVQAIsL
S472-p LRsPLEtsVQAIsLQ
S477-p EtsVQAIsLQDGDLR
G481 QAIsLQDGDLRGPQP
A490 LRGPQPSAPQLLsED
L494 QPSAPQLLsEDGMED
S495-p PSAPQLLsEDGMEDD
G498 PQLLsEDGMEDDRGD
G504 DGMEDDRGDLRVEAK
L506 MEDDRGDLRVEAKA_
- gap
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