Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Alpha-internexin

Gene

INA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Class-IV neuronal intermediate filament that is able to self-assemble. It is involved in the morphogenesis of neurons. It may form an independent structural network without the involvement of other neurofilaments or it may cooperate with NF-L to form the filamentous backbone to which NF-M and NF-H attach to form the cross-bridges.

GO - Molecular functioni

  • structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-internexin
Short name:
Alpha-Inx
Alternative name(s):
66 kDa neurofilament protein
Short name:
NF-66
Short name:
Neurofilament-66
Neurofilament 5
Gene namesi
Name:INA
Synonyms:NEF5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:6057. INA.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • extracellular space Source: UniProtKB
  • intermediate filament cytoskeleton Source: HPA
  • myelin sheath Source: Ensembl
  • neurofilament Source: ProtInc
  • nuclear membrane Source: HPA
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Intermediate filament

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29867.

Polymorphism and mutation databases

BioMutaiINA.
DMDMi20141266.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Alpha-internexinPRO_0000063783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721PhosphoserineBy similarity
Modified residuei290 – 2901N6-acetyllysine1 Publication
Modified residuei335 – 3351PhosphoserineBy similarity
Modified residuei496 – 4961Phosphoserine1 Publication

Post-translational modificationi

O-glycosylated.By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ16352.
PaxDbiQ16352.
PeptideAtlasiQ16352.
PRIDEiQ16352.

PTM databases

PhosphoSiteiQ16352.

Expressioni

Tissue specificityi

Found predominantly in adult CNS.

Developmental stagei

Expressed in brain as early as the 16th week of gestation, and increased rapidly and reached a steady state level by the 18th week of gestation.

Gene expression databases

BgeeiQ16352.
CleanExiHS_INA.
ExpressionAtlasiQ16352. baseline and differential.
GenevisibleiQ16352. HS.

Organism-specific databases

HPAiCAB002059.
HPA008057.

Interactioni

Protein-protein interaction databases

BioGridi114566. 20 interactions.
IntActiQ16352. 3 interactions.
STRINGi9606.ENSP00000358865.

Structurei

3D structure databases

ProteinModelPortaliQ16352.
SMRiQ16352. Positions 91-231, 259-329, 333-402.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8787HeadAdd
BLAST
Regioni88 – 408321RodAdd
BLAST
Regioni88 – 12942Coil 1AAdd
BLAST
Regioni130 – 14213Linker 1Add
BLAST
Regioni143 – 23896Coil 1BAdd
BLAST
Regioni239 – 26224Linker 2Add
BLAST
Regioni263 – 408146Coil 2Add
BLAST
Regioni409 – 49991TailAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi449 – 4546Poly-Glu

Sequence similaritiesi

Belongs to the intermediate filament family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG149366.
GeneTreeiENSGT00760000118905.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiQ16352.
KOiK07608.
OMAiASSYRKV.
OrthoDBiEOG7FV3Q8.
PhylomeDBiQ16352.
TreeFamiTF330122.

Family and domain databases

InterProiIPR027703. Alpha-Inx.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF132. PTHR23239:SF132. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q16352-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFGSEHYLC SSSSYRKVFG DGSRLSARLS GAGGAGGFRS QSLSRSNVAS
60 70 80 90 100
SAACSSASSL GLGLAYRRPP ASDGLDLSQA AARTNEYKII RTNEKEQLQG
110 120 130 140 150
LNDRFAVFIE KVHQLETQNR ALEAELAALR QRHAEPSRVG ELFQRELRDL
160 170 180 190 200
RAQLEEASSA RSQALLERDG LAEEVQRLRA RCEEESRGRE GAERALKAQQ
210 220 230 240 250
RDVDGATLAR LDLEKKVESL LDELAFVRQV HDEEVAELLA TLQASSQAAA
260 270 280 290 300
EVDVTVAKPD LTSALREIRA QYESLAAKNL QSAEEWYKSK FANLNEQAAR
310 320 330 340 350
STEAIRASRE EIHEYRRQLQ ARTIEIEGLR GANESLERQI LELEERHSAE
360 370 380 390 400
VAGYQDSIGQ LENDLRNTKS EMARHLREYQ DLLNVKMALD IEIAAYRKLL
410 420 430 440 450
EGEETRFSTS GLSISGLNPL PNPSYLLPPR ILSATTSKVS STGLSLKKEE
460 470 480 490
EEEEASKVAS KKTSQIGESF EEILEETVIS TKKTEKSNIE ETTISSQKI
Length:499
Mass (Da):55,391
Last modified:January 23, 2002 - v2
Checksum:i4C972764E9E68D3E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 415GFRSQ → ASVE in AAB34482 (PubMed:7769995).Curated
Sequence conflicti67 – 671R → A in AAB34482 (PubMed:7769995).Curated
Sequence conflicti128 – 1325ALRQR → RCDT in AAB34482 (PubMed:7769995).Curated
Sequence conflicti141 – 1411E → Q in AAB34482 (PubMed:7769995).Curated
Sequence conflicti147 – 1526LRDLRA → PRHLP in AAB34482 (PubMed:7769995).Curated
Sequence conflicti191 – 1988GAERALKA → RRARLKR in AAB34482 (PubMed:7769995).Curated
Sequence conflicti244 – 2441A → R in AAB34482 (PubMed:7769995).Curated
Sequence conflicti263 – 2631S → A in AAB34482 (PubMed:7769995).Curated
Sequence conflicti301 – 3011S → T in AAB34482 (PubMed:7769995).Curated
Sequence conflicti310 – 3112EE → DQ in AAB34482 (PubMed:7769995).Curated
Sequence conflicti318 – 3181Missing in AAB34482 (PubMed:7769995).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti92 – 921T → S.1 Publication
Corresponds to variant rs1063455 [ dbSNP | Ensembl ].
VAR_049808
Natural varianti110 – 1101E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_036369
Natural varianti149 – 1491D → H.
Corresponds to variant rs1063456 [ dbSNP | Ensembl ].
VAR_033497

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78296 mRNA. Translation: AAB34482.1.
AL591408 Genomic DNA. Translation: CAI16744.1.
CH471066 Genomic DNA. Translation: EAW49653.1.
BC006359 mRNA. Translation: AAH06359.1.
CCDSiCCDS7545.1.
PIRiI52658.
RefSeqiNP_116116.1. NM_032727.3.
UniGeneiHs.500916.

Genome annotation databases

EnsembliENST00000369849; ENSP00000358865; ENSG00000148798.
GeneIDi9118.
KEGGihsa:9118.
UCSCiuc001kws.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S78296 mRNA. Translation: AAB34482.1.
AL591408 Genomic DNA. Translation: CAI16744.1.
CH471066 Genomic DNA. Translation: EAW49653.1.
BC006359 mRNA. Translation: AAH06359.1.
CCDSiCCDS7545.1.
PIRiI52658.
RefSeqiNP_116116.1. NM_032727.3.
UniGeneiHs.500916.

3D structure databases

ProteinModelPortaliQ16352.
SMRiQ16352. Positions 91-231, 259-329, 333-402.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114566. 20 interactions.
IntActiQ16352. 3 interactions.
STRINGi9606.ENSP00000358865.

PTM databases

PhosphoSiteiQ16352.

Polymorphism and mutation databases

BioMutaiINA.
DMDMi20141266.

Proteomic databases

MaxQBiQ16352.
PaxDbiQ16352.
PeptideAtlasiQ16352.
PRIDEiQ16352.

Protocols and materials databases

DNASUi9118.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369849; ENSP00000358865; ENSG00000148798.
GeneIDi9118.
KEGGihsa:9118.
UCSCiuc001kws.3. human.

Organism-specific databases

CTDi9118.
GeneCardsiGC10P105026.
HGNCiHGNC:6057. INA.
HPAiCAB002059.
HPA008057.
MIMi605338. gene.
neXtProtiNX_Q16352.
PharmGKBiPA29867.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG149366.
GeneTreeiENSGT00760000118905.
HOGENOMiHOG000230977.
HOVERGENiHBG013015.
InParanoidiQ16352.
KOiK07608.
OMAiASSYRKV.
OrthoDBiEOG7FV3Q8.
PhylomeDBiQ16352.
TreeFamiTF330122.

Miscellaneous databases

ChiTaRSiINA. human.
GenomeRNAii9118.
NextBioi34171.
PROiQ16352.
SOURCEiSearch...

Gene expression databases

BgeeiQ16352.
CleanExiHS_INA.
ExpressionAtlasiQ16352. baseline and differential.
GenevisibleiQ16352. HS.

Family and domain databases

InterProiIPR027703. Alpha-Inx.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERiPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF132. PTHR23239:SF132. 1 hit.
PfamiPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEiPS00226. IF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and developmental expression of human 66 kd neurofilament protein."
    Chan S.-O., Chiu F.-C.
    Brain Res. Mol. Brain Res. 29:177-184(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-92.
    Tissue: Fetal brain.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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].
    Tissue: Brain.
  5. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 46-83; 105-111; 121-130; 139-145; 216-228; 279-288; 323-330; 339-367; 378-397 AND 407-430, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-110.

Entry informationi

Entry nameiAINX_HUMAN
AccessioniPrimary (citable) accession number: Q16352
Secondary accession number(s): B1AQK0, Q9BRC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2002
Last modified: July 22, 2015
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.