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Q0ZGT2 (NEXN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nexilin
Alternative name(s):
F-actin-binding protein
Nelin
Gene names
Name:NEXN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length675 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in regulating cell migration through association with the actin cytoskeleton. Has an essential role in the maintenance of Z line and sarcomere integrity. Ref.1 Ref.5 Ref.7

Subunit structure

Interacts with F-actin. Ref.7

Subcellular location

Cytoplasmcytoskeleton By similarity. Cell junctionadherens junction By similarity. CytoplasmmyofibrilsarcomereZ line By similarity. Note: Localizes to the cell-matrix AJ. Not found at the cell-cell AJ By similarity. Ref.7

Tissue specificity

Abundantly expressed in heart and skeletal muscle, and at lower levels in placenta, lung, liver and pancreas. Also expressed in HeLaS3 and MOLT-4 cell lines. Ref.1 Ref.5 Ref.7

Involvement in disease

Cardiomyopathy, dilated 1CC (CMD1CC) [MIM:613122]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1

Cardiomyopathy, familial hypertrophic 20 (CMH20) [MIM:613876]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Contains 1 Ig-like (immunoglobulin-like) domain.

Sequence caution

The sequence AAH17827.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH55084.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH55084.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAI11396.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAI14445.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAI14446.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB71622.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.6 (identifier: Q0ZGT2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.4 (identifier: Q0ZGT2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     150-163: Missing.
     673-675: SKN → TDDY
Note: No experimental confirmation available.
Isoform 3 Ref.2 (identifier: Q0ZGT2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     237-298: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q0ZGT2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     9-72: Missing.
Note: No experimental confirmation available. Contains a phosphoserine at position 16.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 675675Nexilin
PRO_0000302085

Regions

Domain582 – 67089Ig-like
Compositional bias43 – 575533Glu-rich

Amino acid modifications

Modified residue801Phosphoserine Ref.5 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13
Modified residue2411Phosphoserine Ref.12
Modified residue3571Phosphoserine Ref.10 Ref.12
Modified residue3651Phosphoserine Ref.5 Ref.13
Modified residue3701Phosphothreonine Ref.9 Ref.12

Natural variations

Alternative sequence9 – 7264Missing in isoform 4.
VSP_043439
Alternative sequence150 – 16314Missing in isoform 2. Ref.4
VSP_052541
Alternative sequence237 – 29862Missing in isoform 3. Ref.2
VSP_052542
Alternative sequence673 – 6753SKN → TDDY in isoform 2. Ref.4
VSP_052543
Natural variant1311Q → E in CMH20; affects interaction with ACTA1 and F-actin. Ref.14
VAR_065477
Natural variant2451G → R. Ref.1 Ref.4 Ref.5
Corresponds to variant rs1166698 [ dbSNP | Ensembl ].
VAR_049963
Natural variant2791R → C in CMH20; the mutant protein accumulates in the cytoplasm but binding to ACTA1 is not altered. Ref.14
Corresponds to variant rs146245480 [ dbSNP | Ensembl ].
VAR_065478
Natural variant3351R → K.
Corresponds to variant rs9660322 [ dbSNP | Ensembl ].
VAR_059414
Natural variant6111P → T in CMD1CC; affects cardiac Z line integrity; no effect on protein expression and stability. Ref.1
VAR_063009
Natural variant6501Missing in CMD1CC; affects cardiac Z-disk integrity; no effect on protein expression and stability. Ref.1
VAR_063010
Natural variant6521Y → C in CMD1CC; affects cardiac Z line integrity; no effect on protein expression and stability. Ref.1
VAR_063011

Experimental info

Sequence conflict94 – 1018YVPKLTGT → NLPFTVP in AAD29607. Ref.4
Sequence conflict3281K → E in AAI14446. Ref.5
Sequence conflict4291R → K in AAD29607. Ref.4
Sequence conflict4481L → Q in AAH17827. Ref.5
Sequence conflict4761A → T in BAB71622. Ref.2
Sequence conflict6371Y → H in BAB71622. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 18D6336E62503E7F

FASTA67580,658
        10         20         30         40         50         60 
MNDISQKAEI LLSSSKPVPK TYVPKLGKGD VKDKFEAMQR AREERNQRRS RDEKQRRKEQ 

        70         80         90        100        110        120 
YIREREWNRR KQEIKEMLAS DDEEDVSSKV EKAYVPKLTG TVKGRFAEME KQRQEEQRKR 

       130        140        150        160        170        180 
TEEERKRRIE QDMLEKRKIQ RELAKRAEQI EDINNTGTES ASEEGDDSLL ITVVPVKSYK 

       190        200        210        220        230        240 
TSGKMKKNFE DLEKEREEKE RIKYEEDKRI RYEEQRPSLK EAKCLSLVMD DEIESEAKKE 

       250        260        270        280        290        300 
SLSPGKLKLT FEELERQRQE NRKKQAEEEA RKRLEEEKRA FEEARRQMVN EDEENQDTAK 

       310        320        330        340        350        360 
IFKGYRPGKL KLSFEEMERQ RREDEKRKAE EEARRRIEEE KKAFAEARRN MVVDDDSPEM 

       370        380        390        400        410        420 
YKTISQEFLT PGKLEINFEE LLKQKMEEEK RRTEEERKHK LEMEKQEFEQ LRQEMGEEEE 

       430        440        450        460        470        480 
ENETFGLSRE YEELIKLKRS GSIQAKNLKS KFEKIGQLSE KEIQKKIEEE RARRRAIDLE 

       490        500        510        520        530        540 
IKEREAENFH EEDDVDVRPA RKSEAPFTHK VNMKARFEQM AKAREEEEQR RIEEQKLLRM 

       550        560        570        580        590        600 
QFEQREIDAA LQKKREEEEE EEGSIMNGST AEDEEQTRSG APWFKKPLKN TSVVDSEPVR 

       610        620        630        640        650        660 
FTVKVTGEPK PEITWWFEGE ILQDGEDYQY IERGETYCLY LPETFPEDGG EYMCKAVNNK 

       670 
GSAASTCILT IESKN 

« Hide

Isoform 2 [UniParc].

Checksum: E91BF5E00A8016D4
Show »

FASTA66279,362
Isoform 3 [UniParc].

Checksum: 90EC363A14C50E7B
Show »

FASTA61373,128
Isoform 4 [UniParc].

Checksum: D7A8A66A2BEF4255
Show »

FASTA61172,732

References

« Hide 'large scale' references
[1]"Nexilin mutations destabilize cardiac Z-disks and lead to dilated cardiomyopathy."
Hassel D., Dahme T., Erdmann J., Meder B., Huge A., Stoll M., Just S., Hess A., Ehlermann P., Weichenhan D., Grimmler M., Liptau H., Hetzer R., Regitz-Zagrosek V., Fischer C., Nurnberg P., Schunkert H., Katus H.A., Rottbauer W.
Nat. Med. 15:1281-1288(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANTS CMD1CC THR-611; GLY-650 DEL AND CYS-652, VARIANT ARG-245, CHARACTERIZATION OF VARIANTS CMD1CC THR-611; GLY-650 DEL AND CYS-652.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-675 (ISOFORM 3).
Tissue: Gastric mucosa.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-675 (ISOFORM 1), VARIANT ARG-245.
Tissue: Skeletal muscle.
[5]"Molecular cloning of NELIN, a putative human cytoskeleton regulation gene."
Zhao Y., Wei Y.-J., Cao H.-Q., Ding J.-F.
Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 33:19-24(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 91-675 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT ARG-245.
Tissue: Heart.
[6]"Muscle autoantigens in thyroid associated ophthalmopathy: the limits of molecular genetics."
Elisei R., Weightman D., Kendall-Taylor P., Vassart G., Ludgate M.
J. Endocrinol. Invest. 16:533-540(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 108-454 (ISOFORM 1).
[7]"NELIN, a new F-actin associated protein, stimulates HeLa cell migration and adhesion."
Wang W., Zhang W., Han Y., Chen J., Wang Y., Zhang Z., Hui R.
Biochem. Biophys. Res. Commun. 330:1127-1131(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH F-ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-357, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-241; SER-357 AND THR-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Mutations in NEXN, a Z-disc gene, are associated with hypertrophic cardiomyopathy."
Wang H., Li Z., Wang J., Sun K., Cui Q., Song L., Zou Y., Wang X., Liu X., Hui R., Fan Y.
Am. J. Hum. Genet. 87:687-693(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMH20 GLU-131 AND CYS-279, CHARACTERIZATION OF VARIANTS CMH20 GLU-131 AND CYS-279.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ464902 mRNA. Translation: ABE97925.1.
AK057954 mRNA. Translation: BAB71622.1. Different initiation.
AK298565 mRNA. Translation: BAG60759.1.
AC096948 Genomic DNA. No translation available.
AC138392 Genomic DNA. No translation available.
BC055084 mRNA. Translation: AAH55084.1. Sequence problems.
BC017827 mRNA. Translation: AAH17827.1. Sequence problems.
BC111395 mRNA. Translation: AAI11396.1. Different initiation.
BC114444 mRNA. Translation: AAI14445.1. Different initiation.
BC114445 mRNA. Translation: AAI14446.1. Different initiation.
AF114264 mRNA. Translation: AAD29607.1.
S67069 mRNA. Translation: AAB28815.1.
CCDSCCDS41351.1. [Q0ZGT2-1]
CCDS53335.1. [Q0ZGT2-4]
RefSeqNP_001165780.1. NM_001172309.1. [Q0ZGT2-4]
NP_653174.3. NM_144573.3. [Q0ZGT2-1]
XP_005271380.1. XM_005271323.1. [Q0ZGT2-2]
UniGeneHs.612385.

3D structure databases

ProteinModelPortalQ0ZGT2.
SMRQ0ZGT2. Positions 563-672.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124855. 7 interactions.
IntActQ0ZGT2. 6 interactions.
MINTMINT-8187852.

PTM databases

PhosphoSiteQ0ZGT2.

Polymorphism databases

DMDM121945484.

Proteomic databases

MaxQBQ0ZGT2.
PaxDbQ0ZGT2.
PRIDEQ0ZGT2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330010; ENSP00000327363; ENSG00000162614. [Q0ZGT2-4]
ENST00000334785; ENSP00000333938; ENSG00000162614. [Q0ZGT2-1]
ENST00000457030; ENSP00000388048; ENSG00000162614. [Q0ZGT2-2]
GeneID91624.
KEGGhsa:91624.
UCSCuc001dia.3. human. [Q0ZGT2-2]
uc001dib.4. human. [Q0ZGT2-4]
uc001dic.4. human. [Q0ZGT2-1]

Organism-specific databases

CTD91624.
GeneCardsGC01P078354.
GeneReviewsNEXN.
HGNCHGNC:29557. NEXN.
HPAHPA011185.
MIM613121. gene.
613122. phenotype.
613876. phenotype.
neXtProtNX_Q0ZGT2.
Orphanet154. Familial isolated dilated cardiomyopathy.
155. Familial isolated hypertrophic cardiomyopathy.
PharmGKBPA134974801.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147699.
HOVERGENHBG066529.
InParanoidQ0ZGT2.
OMANFHEEED.
OrthoDBEOG7TBC1Z.
PhylomeDBQ0ZGT2.
TreeFamTF328960.

Gene expression databases

ArrayExpressQ0ZGT2.
BgeeQ0ZGT2.
CleanExHS_NEXN.
GenevestigatorQ0ZGT2.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR020675. Myosin_light_ch_kinase-rel.
[Graphical view]
PANTHERPTHR22964. PTHR22964. 1 hit.
PfamPF07679. I-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi91624.
NextBio77345.
PROQ0ZGT2.
SOURCESearch...

Entry information

Entry nameNEXN_HUMAN
AccessionPrimary (citable) accession number: Q0ZGT2
Secondary accession number(s): A0PJ84 expand/collapse secondary AC list , B4DPZ7, Q0D2H2, Q14CC2, Q14CC3, Q16081, Q7Z2X0, Q96DL0, Q9Y2V1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: August 22, 2006
Last modified: July 9, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM