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Protein Page:
SEC24D (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
SEC24D Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex. COPII is composed of at least five proteins: the Sec23/24 complex, the Sec13/31 complex and Sar1. Interacts with TMED2 and TMED10. Ubiquitously expressed, with higher amounts in placenta, pancreas, heart and liver. Belongs to the SEC23/SEC24 family. SEC24 subfamily. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Cellular Component: Golgi membrane; endoplasmic reticulum membrane; COPII vesicle coat; perinuclear region of cytoplasm; cytosol
Molecular Function: zinc ion binding
Biological Process: COPII coating of Golgi vesicle; intracellular protein transport; ER to Golgi vesicle-mediated transport; antigen processing and presentation of peptide antigen via MHC class I; cellular protein metabolic process; antigen processing and presentation of exogenous peptide antigen via MHC class II; protein amino acid N-linked glycosylation via asparagine; post-translational protein modification
Reference #:  O94855 (UniProtKB)
Alt. Names/Synonyms: FLJ43974; KIAA0755; Protein transport protein Sec24D; SC24D; SEC24 family, member D (S. cerevisiae); SEC24 related gene family, member D; SEC24-related protein D; SEC24D
Gene Symbols: SEC24D
Molecular weight: 113,010 Da
Basal Isoelectric point: 6.91  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SEC24D

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 T176 QVLPPPPTTLNGPGA
0 1 K258 GPPQPQKKLDPDSIP
0 3 S266-p LDPDSIPsPIQVIEN
0 2 Y283-p ASRGGQVyATNTRGQ
0 1 K594-ub AEAPGKLkNRDDKKL
0 1 K608 LVNTDKEKILFQPQT
0 1 S779-p QLADLYKsCETDALI
0 4 K791-ub ALINFFAkSAFkAVL
0 2 K795-ub FFAkSAFkAVLHQPL
0 1 K803 AVLHQPLKVIREILV
0 1 T813 REILVNQTAHMLACY
0 1 S826-p CYRKNCAsPSAAsQL
0 1 S831-p CAsPSAAsQLILPDS
0 1 K840 LILPDSMKVLPVYMN
0 1 S899-p IHTLDVKsTMLPAAV
0 1 S911-p AAVRCSEsRLSEEGI
0 1 T988-p RPYSMKLtIVKQREQ
  mouse

 
T174-p QVPPPPPtALNGPGA
K258-ub PAPQLQRkLDPDSIP
S266-p LDPDSIPsPIQVIEN
Y283 ATRGGQVYTTNTRGQ
K594 AEAPGKLKNRDDKKL
K608-ub LVNTDKEkILFQPQT
S779 QLADLYKSCETDALI
K791 ALINFFAKSAFkAVL
K795-ub FFAKSAFkAVLNQPL
K803-ub AVLNQPLkAIREILV
T813 REILVNQTAHMLACY
S826 CYRKHCASPSAASQL
S831 CASPSAASQLILPDS
K840-ub LILPDSMkVLPVYMN
S899 IHTLDVKSAALPPAV
S911 PAVRCSESRLSEEGI
I988 KPYSMKLIVVKQREQ
  rat

 
- gap
- gap
- gap
- gap
K131 AEAPGKLKNRDDKKL
K145 LVNTDKEKILFQPQT
S316 QLADLYKSCETDALI
K328 ALINFFAKSAFKAVL
K332 FFAKSAFKAVLNQPL
K340 AVLNQPLKTIREILV
T350-p REILVNQtAHMLACY
S363 CYRKHCASPSAASQL
S368 CASPSAASQLILPDS
K377 LILPDSMKVLPVYMN
S436 IHTLDVKSAALPPAV
S448 PAVRCSESRLSEEGI
I525 KPYSMKLIIVKQREQ
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