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Protein Page:
NEXN (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
NEXN Involved in regulating cell migration through association with the actin cytoskeleton. Has an essential role in the maintenance of Z line and sarcomere integrity. Defects in NEXN are the cause of cardiomyopathy dilated type 1CC (CMD1CC). A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Defects in NEXN are the cause of familial hypertrophic cardiomyopathy type 20 (CMH20). CMH20 is a hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis
Cellular Component: cytoskeleton; Z disc; cell-substrate adherens junction
Molecular Function: actin filament binding; structural constituent of muscle
Biological Process: regulation of cell migration; regulation of cytoskeleton organization and biogenesis
Reference #:  Q0ZGT2 (UniProtKB)
Alt. Names/Synonyms: F-actin-binding protein; MGC104234; MGC138865; MGC138866; Nelin; Nexilin; nexilin (F actin binding protein); NEXN
Gene Symbols: NEXN
Molecular weight: 80,658 Da
Basal Isoelectric point: 5.31  Predict pI for various phosphorylation states
Select Structure to View Below

NEXN

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


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

► Hide Isoforms
 
0 29 S80-p EIKEMLAsDDEEDVS
0 3 S87 sDDEEDVSSKVEKAY
0 1 T156 QIEDINNTGTEsASE
0 1 S160-p INNTGTEsASEEGDD
0 1 K203-a REEKERIkYEEDKRI
0 1 S218-p RYEEQRPsLKEAKCL
0 2 S241-p ESEAKKEsLsPGKLK
0 1 S243-p EAKKEsLsPGKLKLT
0 2 T298-p EDEENQDtAKIFKGY
0 1 S313 RPGKLKLSFEEMERQ
0 3 N350 AFAEARRNMVVDDDs
0 6 S357-p NMVVDDDsPEMYKtI
0 8 T363-p DsPEMYKtIsQEFLt
0 44 S365-p PEMYKtIsQEFLtPG
0 3 F368 YKtIsQEFLtPGKLE
0 5 T370-p tIsQEFLtPGKLEIN
0 1 K405-a KHKLEMEkQEFEQLR
0 2 S442-p IKLKRSGsIQAkNLK
0 1 K446-a RSGsIQAkNLKSKFE
0 3 A505 RPARKSEAPFTHKVN
0 7 S564-p EEEEEEGsIMNGsTA
0 3 S569-p EGsIMNGsTAEDEEQ
0 1 R545 LRMQFEQREIDAALQ
0 2 A571 sIMNGsTAEDEEQTR
0 1 S592 KKPLKNTSVVDSEPV
0 1 T602-p DSEPVRFtVKVTGEP
  NEXN iso4  
S16-p EIKEMLAsDDEEDVS
S23 sDDEEDVSSKVEKAY
T92 QIEDINNTGTESASE
S96 INNTGTESASEEGDD
K139 REEKERIKYEEDKRI
S154 RYEEQRPSLKEAKCL
S177 ESEAKKESLSPRKLK
S179 EAKKESLSPRKLKLT
T234 EDEENQDTAKIFKGY
S249 RPGKLKLSFEEMERQ
N286 AFAEARRNMVVDDDF
F293 NMVVDDDFPKMY___
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- under review  
- gap
- gap
- gap
  mouse

 
S16-p EIKEMLAsDDEEESs
S23-p sDDEEESsPKIEKAY
T92-p QIEDINNtGTESASE
S96 INNtGTESASEEGDD
N137 EEGNGRTNHEEDKMR
V151 RYEEECRVLKEAKCL
S172 ETEAKKESHFPGKLK
F174 EAKKESHFPGKLKST
R229 EEDENQDRETVFKEY
S244-p RPGKLKLsFEEIERQ
S281-p AFAEARRsMVLDDDs
S288-p sMVLDDDsPEIYKTV
T294 DsPEIYKTVsQEsLt
S296-p PEIYKTVsQEsLtPG
S299-p YKTVsQEsLtPGKLE
T301-p TVsQEsLtPGKLEIN
K336 RHKLEMEKQEFEQLR
S373 IKLKRSGSIQAKNLK
K377 RSGSIQAKNLKSKFE
S436-p RPAKKSEsPFTHKVN
S495-p DEEEEEGsIVNGsTt
S500-p EGsIVNGsTtEDEEQ
K476-u LRMQFEQkEIDAALQ
T502-p sIVNGsTtEDEEQTR
S523-p KKPLRNTsVVDSEPV
T533 DSEPVRFTVKVTGEP
  rat

 
S80-p EIKDMLAsDEEEEPS
S87 sDEEEEPSKVEKAYV
- gap
- gap
S186 EHRNGRVSQEEEKTR
A200 RHEEECRALKEAKCL
S221 ETEAKKESRFPGKLK
F223 EAKKESRFPGKLKST
T278 EEDESQDTETVFKEY
S293 RPGKLRLSFEEIERQ
S330 AFAEARRSMVLDDDS
S337 SMVLDDDSPEIYKAV
A343 DSPEIYKAVsQESLT
S345-p PEIYKAVsQESLTPG
S348 YKAVsQESLTPGKLE
T350 AVsQESLTPGKLEIN
K385 RQKLEMEKQEFEQLR
S422 IKLKRSGSIQAKNLK
K426 RSGSIQAKNLKSKFE
S485 KPAKKSESPFTHKVN
S544 DDEEEEGSIVNGSTT
S549 EGSIVNGSTTEDEEQ
K525 LRMQFEQKEIDAALQ
T551 SIVNGSTTEDEEQTR
S572 KKPLRNTSVVDSEPV
T582 DSEPVRFTVKVTGEP
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