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Protein Page:
ABCA3 (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
ABCA3 Plays an important role in the formation of pulmonary surfactant, probably by transporting lipids such as cholesterol. Defects in ABCA3 are the cause of pulmonary surfactant metabolism dysfunction type 3 (SMDP3); also called pulmonary alveolar proteinosis due to ABCA3 deficiency. A rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid-Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress. Belongs to the ABC transporter superfamily. ABCA family. Note: This description may include information from UniProtKB.
Protein type: Transporter, ABC family; Membrane protein, multi-pass; Membrane protein, integral; Transporter
Cellular Component: extracellular space; membrane; integral to membrane; plasma membrane
Molecular Function: ATPase activity, coupled to transmembrane movement of substances; transporter activity; ATP binding
Biological Process: response to drug; transport; transmembrane transport
Reference #:  Q99758 (UniProtKB)
Alt. Names/Synonyms: ABC transporter 3; ABC-C; ABC-C transporter; ABC3; ABCA3; ATP-binding cassette 3; ATP-binding cassette sub-family A member 3; ATP-binding cassette transporter 3; ATP-binding cassette, sub-family A (ABC1), member 3; EST111653; LBM180; MGC166979; MGC72201; SMDP3
Gene Symbols: ABCA3
Molecular weight: 191,362 Da
Basal Isoelectric point: 7.55  Predict pI for various phosphorylation states
Select Structure to View Below

ABCA3

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 5 K503 KPRAVAGKEEEDSDP
0 7 K512-u EEDSDPEkALRNEYF
0 1 K531 EDLVAGIKIKHLSKV
0 4 K640 LKGLSRQKCPEEVKQ
0 1 K646 QKCPEEVKQMLHIIG
0 1 K711 WDLLQRQKSDRTIVL
0 8 Y754 SLFLKQKYGAGYHMT
0 1 K812 RFEGLFAKLEKKQKE
0 1 K841 EVFLRVGKLVDSSMD
0 1 R1212 GAATAYTRLtIFNIL
0 2 T1214-p ATAYTRLtIFNILSG
0 1 Y1265-p GMAVSSFyENyETRR
0 1 Y1268-p VSSFyENyETRRYCT
0 1 Y1349-p RRTLTELyTRMPVLP
0 1 K1408 RLSLAVQKGECFGLL
0 1 K1422 LGFNGAGKTTTFKML
0 1 K1604 SPQHLKSKFGSGYSL
0 4 Q1620 AKVQSEGQQEALEEF
  mouse

 
K503-u NPRTVVGkEEEGSDP
K512-u EEGSDPEkALRNEYF
K531-u EDLVAGIkIKHLSKV
K640-u LKGLSLQkCPEEVkQ
K646-u QkCPEEVkQMLHILS
K711-u WDLLQQQkSDRTVLL
Y754 SLFLKQKYGAGYHMT
K812-u RFESLFAkLEKKQKE
K841-u EVFLRVGkLVDTSMD
R1212-m1 AASTAYTrLTIFNIL
T1214 STAYTrLTIFNILSG
Y1265 GMAVSNFYENYETRR
Y1268 VSNFYENYETRRYCT
Q1349 RWTLAELQNRTSVLP
K1408-u RISLAVQkGECFGLL
K1422-u LGFNGAGkTTTFKML
K1604-u SPQHLKSkFGSGYSL
K1620-u AKVRSEGkQDALEEF
  rat

 
K503 NPRTVVGKEEEGGDP
K512 EEGGDPEKAFRTEYF
K531 EDLAAGIKIKHLSKV
K640 LKGLSVQKCPEEVKQ
K646 QKCPEEVKQMLHTLG
K711 WDLLQQQKSDRTVLL
Y754-p SLFLKQKyGAGYHMT
K812 RFESLFAKLEKKQKE
K841 EVFLRVGKLVDTSMD
R1212 AASTAYTRLTIFNIL
T1214 STAYTRLTIFNILSG
Y1265 GMAVSNFYENYETRR
Y1268 VSNFYENYETRRYCT
Q1349 RWTLAELQNRTSVLP
K1408 RISLAVQKGECFGLL
K1422 LGFNGAGKTTTFKML
K1564 SPQHLKSKFGSGYSL
K1580 AKVRSEGKQEVLEEF
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