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Protein

Nexilin

Gene

Nexn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in regulating cell migration through association with the actin cytoskeleton. Has an essential role in the maintenance of Z line and sarcomere integrity.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nexilin
Alternative name(s):
F-actin-binding protein
Gene namesi
Name:NexnImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1916060. Nexn.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 607607NexilinPRO_0000302086Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161PhosphoserineCombined sources
Modified residuei172 – 1721PhosphoserineBy similarity
Modified residuei281 – 2811PhosphoserineCombined sources
Modified residuei288 – 2881PhosphoserineCombined sources
Modified residuei296 – 2961PhosphoserineBy similarity
Modified residuei301 – 3011PhosphothreonineBy similarity
Modified residuei495 – 4951PhosphoserineCombined sources
Modified residuei500 – 5001PhosphoserineBy similarity
Modified residuei502 – 5021PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ7TPW1.
PaxDbiQ7TPW1.
PRIDEiQ7TPW1.

PTM databases

iPTMnetiQ7TPW1.
PhosphoSiteiQ7TPW1.

Expressioni

Gene expression databases

BgeeiQ7TPW1.
CleanExiMM_NEXN.
ExpressionAtlasiQ7TPW1. baseline and differential.
GenevisibleiQ7TPW1. MM.

Interactioni

Subunit structurei

Interacts with F-actin.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi213062. 1 interaction.
STRINGi10090.ENSMUSP00000037120.

Structurei

3D structure databases

ProteinModelPortaliQ7TPW1.
SMRiQ7TPW1. Positions 512-604.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini513 – 60189Ig-likeSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 506498Glu-richSequence analysisAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Immunoglobulin domain

Phylogenomic databases

eggNOGiENOG410IF6R. Eukaryota.
ENOG4110P6X. LUCA.
GeneTreeiENSGT00730000111176.
HOGENOMiHOG000285935.
HOVERGENiHBG066529.
InParanoidiQ7TPW1.
OrthoDBiEOG7TBC1Z.
TreeFamiTF328960.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
[Graphical view]
PfamiPF07679. I-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7TPW1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDVSQKAEI KEMLASDDEE ESSPKIEKAY VPKLTGTVKG KFDEMEKHRQ
60 70 80 90 100
EEQRKRTEEE RKRRIEQDLL EKRKIQRELA KRAEQIEDIN NTGTESASEE
110 120 130 140 150
GDDSLLITVV PAKSYKTPGK TKDPEDLDRE EGNGRTNHEE DKMRYEEECR
160 170 180 190 200
VLKEAKCLSL VMDDETEAKK ESHFPGKLKS TFEELERQRQ ENRKKQAEEE
210 220 230 240 250
ARRRLEEERR SFEEARRHMV NEEDENQDRE TVFKEYRPGK LKLSFEEIER
260 270 280 290 300
QRREDEKRKA EEEARRRIEE EKAAFAEARR SMVLDDDSPE IYKTVSQESL
310 320 330 340 350
TPGKLEINFE QLLRQKMEEE RRRTEEERRH KLEMEKQEFE QLRQEMGKEE
360 370 380 390 400
EENESFGLSR EYEELIKLKR SGSIQAKNLK SKFEKIGQLS EKEVQKKIEE
410 420 430 440 450
ERAKRRAIDL EIKEREAENF HEDDDVDVRP AKKSESPFTH KVNMKARFEQ
460 470 480 490 500
MAKAREEEEQ RRIEEQKLLR MQFEQKEIDA ALQKKREDEE EEEGSIVNGS
510 520 530 540 550
TTEDEEQTRS GAPWFKKPLR NTSVVDSEPV RFTVKVTGEP KPEITWWFEG
560 570 580 590 600
EILQDGEDYQ YIERGETYCL YLPETFPEDG GEYMCKAVNN KGSAASTCIL

TIEMDDY
Length:607
Mass (Da):72,108
Last modified:July 27, 2011 - v3
Checksum:iAFD6488C345F28E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 1231D → N in AAH52878 (PubMed:15489334).Curated
Sequence conflicti268 – 2681I → L in AAH52878 (PubMed:15489334).Curated
Sequence conflicti454 – 4541A → T in AAH52878 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC123075 Genomic DNA. No translation available.
BC052878 mRNA. Translation: AAH52878.1.
AK135919 mRNA. Translation: BAE22724.1.
AK136097 mRNA. Translation: BAE22818.1.
AK136102 mRNA. Translation: BAE22822.1.
AK163414 mRNA. Translation: BAE37339.1.
CCDSiCCDS38673.1.
RefSeqiNP_955759.2. NM_199465.2.
XP_006502061.1. XM_006501998.2.
UniGeneiMm.200188.

Genome annotation databases

EnsembliENSMUST00000046045; ENSMUSP00000037120; ENSMUSG00000039103.
GeneIDi68810.
KEGGimmu:68810.
UCSCiuc008rtb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC123075 Genomic DNA. No translation available.
BC052878 mRNA. Translation: AAH52878.1.
AK135919 mRNA. Translation: BAE22724.1.
AK136097 mRNA. Translation: BAE22818.1.
AK136102 mRNA. Translation: BAE22822.1.
AK163414 mRNA. Translation: BAE37339.1.
CCDSiCCDS38673.1.
RefSeqiNP_955759.2. NM_199465.2.
XP_006502061.1. XM_006501998.2.
UniGeneiMm.200188.

3D structure databases

ProteinModelPortaliQ7TPW1.
SMRiQ7TPW1. Positions 512-604.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213062. 1 interaction.
STRINGi10090.ENSMUSP00000037120.

PTM databases

iPTMnetiQ7TPW1.
PhosphoSiteiQ7TPW1.

Proteomic databases

MaxQBiQ7TPW1.
PaxDbiQ7TPW1.
PRIDEiQ7TPW1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000046045; ENSMUSP00000037120; ENSMUSG00000039103.
GeneIDi68810.
KEGGimmu:68810.
UCSCiuc008rtb.2. mouse.

Organism-specific databases

CTDi91624.
MGIiMGI:1916060. Nexn.

Phylogenomic databases

eggNOGiENOG410IF6R. Eukaryota.
ENOG4110P6X. LUCA.
GeneTreeiENSGT00730000111176.
HOGENOMiHOG000285935.
HOVERGENiHBG066529.
InParanoidiQ7TPW1.
OrthoDBiEOG7TBC1Z.
TreeFamiTF328960.

Miscellaneous databases

ChiTaRSiNexn. mouse.
NextBioi327979.
PROiQ7TPW1.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TPW1.
CleanExiMM_NEXN.
ExpressionAtlasiQ7TPW1. baseline and differential.
GenevisibleiQ7TPW1. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
[Graphical view]
PfamiPF07679. I-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "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].
    Strain: C57BL/6JImported.
    Tissue: EggImported.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-314 AND 386-607.
    Strain: C57BL/6JImported.
    Tissue: EggImported.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-281; SER-288 AND SER-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiNEXN_MOUSE
AccessioniPrimary (citable) accession number: Q7TPW1
Secondary accession number(s): E9QJX5
, Q3TQP3, Q3UWU2, Q3UWU6, Q3UX39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.