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Protein Page:
DNAJC5 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DNAJC5 a cysteine string protein that inhibits N-type calcium channels which is blocked by huntingtin mutants. May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings. Modulates the maturation of cystic fibrosis transmembrane conductance regulator. Two splice-variant isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Vesicle
Chromosomal Location of Human Ortholog: 20q13.33
Cellular Component: cytosol; lysosomal membrane; melanosome; membrane; mitochondrion; plasma membrane; synaptic vesicle; terminal button
Molecular Function: ATP-dependent protein binding; glycoprotein binding
Biological Process: exocytosis; negative regulation of neuron apoptosis; neurotransmitter secretion; regulated secretory pathway; synaptic vesicle exocytosis
Reference #:  Q9H3Z4 (UniProtKB)
Gene Symbols: DNAJC5
Molecular weight: 22,149 Da
Basal Isoelectric point: 4.93  Predict pI for various phosphorylation states
Select Structure to View Below

DNAJC5

Protein Structure Not Found.
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Sites Implicated In
exocytosis, induced: S10‑p
molecular association, regulation: S10‑p

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


 LTP 

LTP: 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.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 128 S8‑p MADQRQRsLstsGEs
4 401 S10‑p DQRQRsLstsGEsLy
0 63 T11‑p QRQRsLstsGEsLyH
0 32 S12‑p RQRsLstsGEsLyHV
0 39 S15‑p sLstsGEsLyHVLGL
0 14 Y17‑p stsGEsLyHVLGLDK
0 1 S34‑p TSDDIKKsYRKLALk
0 8 K41‑ub sYRKLALkyHPDkNP
0 1 Y42‑p YRKLALkyHPDkNPD
0 1 K46‑ub ALkyHPDkNPDNPEA
0 2 K56‑ac DNPEAADkFkEINNA
0 2 K56‑ub DNPEAADkFkEINNA
0 2 K58‑ub PEAADkFkEINNAHA
0 7 K72‑ub AILTDATkRNIYDKY
0 7 Y149‑p EGEETEFyVSPEDLE
0 4 S151 EETEFyVSPEDLEAQ
0 1 S161 DLEAQLQSDEREATD
1 1 T169 DEREATDTPIVIQPA
0 1 S188 TTQLTADSHPSyHTD
0 9 Y192‑p TADSHPSyHTDGFN_
  DNAJC5 iso2  
S8 MADQRQRSLSTSGES
S10 DQRQRSLSTSGESLY
T11 QRQRSLSTSGESLYH
S12 RQRSLSTSGESLYHV
S15 SLSTSGESLYHVLGL
Y17 STSGESLYHVLGLDK
S34 TSDDIKKSYRKLALK
K41 SYRKLALKYHPDKNP
Y42 YRKLALKYHPDKNPD
K46 ALKYHPDKNPDNPEA
K56 DNPEAADKFKEINNA
K56 DNPEAADKFKEINNA
K58 PEAADKFKEINNAHA
K72 AILTDATKRNIYDKY
Y149 EGEETEFYVSPEDLE
S151 EETEFYVSPEDLEAQ
S161 DLEAQLQSDERGGH_
- gap
- gap
- gap
  mouse

 
S8‑p MADQRQRsLstsGEs
S10‑p DQRQRsLstsGEsLy
T11‑p QRQRsLstsGEsLyH
S12‑p RQRsLstsGEsLyHV
S15‑p sLstsGEsLyHVLGL
Y17‑p stsGEsLyHVLGLDK
S34 TSDDIKKSYRKLALk
K41‑ub SYRKLALkYHPDKNP
Y42 YRKLALkYHPDKNPD
K46 ALkYHPDKNPDNPEA
K56 DNPEAADKFkEINNA
K56‑ub DNPEAADkFkEINNA
K58‑ub PEAADkFkEINNAHA
K72‑ub AILTDATkRNIYDKY
Y149 EGEETEFYVsPEDLE
S151‑p EETEFYVsPEDLEAQ
S161‑p DLEAQLQsDEREATD
T169 DEREATDTPIVIQPA
S188‑p TTQLTADsHPSYHTD
Y192 TADsHPSYHTDGFN_
  rat

 
S8‑p MADQRQRsLsTsGEs
S10‑p DQRQRsLsTsGEsLY
T11 QRQRsLsTsGEsLYH
S12‑p RQRsLsTsGEsLYHV
S15‑p sLsTsGEsLYHVLGL
Y17 sTsGEsLYHVLGLDK
S34 TSDDIKKSYRKLALk
K41‑ub SYRKLALkYHPDKNP
Y42 YRKLALkYHPDKNPD
K46 ALkYHPDKNPDNPEA
K56‑ac DNPEAADkFKEINNA
K56 DNPEAADKFKEINNA
K58 PEAADkFKEINNAHA
K72 AILTDATKRNIYDKY
Y149 EGEETEFYVsPEDLE
S151‑p EETEFYVsPEDLEAQ
S161 DLEAQLQSDEREATD
T169‑p DEREATDtPIVIQPA
S188 TTQLTADSHPSYHTD
Y192 TADSHPSYHTDGFN_
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