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Q16352 (AINX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:INA
Synonyms:NEF5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Tissue specificity

Found predominantly in adult CNS.

Developmental stage

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.

Post-translational modification

O-glycosylated By similarity.

Sequence similarities

Belongs to the intermediate filament family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Alpha-internexin
PRO_0000063783

Regions

Region1 – 8787Head
Region88 – 408321Rod
Region88 – 12942Coil 1A
Region130 – 14213Linker 1
Region143 – 23896Coil 1B
Region239 – 26224Linker 2
Region263 – 408146Coil 2
Region409 – 49991Tail
Compositional bias449 – 4546Poly-Glu

Amino acid modifications

Modified residue721Phosphoserine By similarity
Modified residue2901N6-acetyllysine Ref.7
Modified residue3351Phosphoserine By similarity
Modified residue4961Phosphoserine Ref.6

Natural variations

Natural variant921T → S. Ref.1
Corresponds to variant rs1063455 [ dbSNP | Ensembl ].
VAR_049808
Natural variant1101E → Q in a breast cancer sample; somatic mutation. Ref.8
VAR_036369
Natural variant1491D → H.
Corresponds to variant rs1063456 [ dbSNP | Ensembl ].
VAR_033497

Experimental info

Sequence conflict37 – 415GFRSQ → ASVE in AAB34482. Ref.1
Sequence conflict671R → A in AAB34482. Ref.1
Sequence conflict128 – 1325ALRQR → RCDT in AAB34482. Ref.1
Sequence conflict1411E → Q in AAB34482. Ref.1
Sequence conflict147 – 1526LRDLRA → PRHLP in AAB34482. Ref.1
Sequence conflict191 – 1988GAERALKA → RRARLKR in AAB34482. Ref.1
Sequence conflict2441A → R in AAB34482. Ref.1
Sequence conflict2631S → A in AAB34482. Ref.1
Sequence conflict3011S → T in AAB34482. Ref.1
Sequence conflict310 – 3112EE → DQ in AAB34482. Ref.1
Sequence conflict3181Missing in AAB34482. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q16352 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 4C972764E9E68D3E

FASTA49955,391
        10         20         30         40         50         60 
MSFGSEHYLC SSSSYRKVFG DGSRLSARLS GAGGAGGFRS QSLSRSNVAS SAACSSASSL 

        70         80         90        100        110        120 
GLGLAYRRPP ASDGLDLSQA AARTNEYKII RTNEKEQLQG LNDRFAVFIE KVHQLETQNR 

       130        140        150        160        170        180 
ALEAELAALR QRHAEPSRVG ELFQRELRDL RAQLEEASSA RSQALLERDG LAEEVQRLRA 

       190        200        210        220        230        240 
RCEEESRGRE GAERALKAQQ RDVDGATLAR LDLEKKVESL LDELAFVRQV HDEEVAELLA 

       250        260        270        280        290        300 
TLQASSQAAA EVDVTVAKPD LTSALREIRA QYESLAAKNL QSAEEWYKSK FANLNEQAAR 

       310        320        330        340        350        360 
STEAIRASRE EIHEYRRQLQ ARTIEIEGLR GANESLERQI LELEERHSAE VAGYQDSIGQ 

       370        380        390        400        410        420 
LENDLRNTKS EMARHLREYQ DLLNVKMALD IEIAAYRKLL EGEETRFSTS GLSISGLNPL 

       430        440        450        460        470        480 
PNPSYLLPPR ILSATTSKVS STGLSLKKEE EEEEASKVAS KKTSQIGESF EEILEETVIS 

       490 
TKKTEKSNIE ETTISSQKI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-110.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S78296 mRNA. Translation: AAB34482.1.
AL591408 Genomic DNA. Translation: CAI16744.1.
CH471066 Genomic DNA. Translation: EAW49653.1.
BC006359 mRNA. Translation: AAH06359.1.
CCDSCCDS7545.1.
PIRI52658.
RefSeqNP_116116.1. NM_032727.3.
UniGeneHs.500916.

3D structure databases

ProteinModelPortalQ16352.
SMRQ16352. Positions 91-231, 259-329, 333-402.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114566. 9 interactions.
IntActQ16352. 3 interactions.
STRING9606.ENSP00000358865.

PTM databases

PhosphoSiteQ16352.

Polymorphism databases

DMDM20141266.

Proteomic databases

MaxQBQ16352.
PaxDbQ16352.
PeptideAtlasQ16352.
PRIDEQ16352.

Protocols and materials databases

DNASU9118.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369849; ENSP00000358865; ENSG00000148798.
GeneID9118.
KEGGhsa:9118.
UCSCuc001kws.3. human.

Organism-specific databases

CTD9118.
GeneCardsGC10P105026.
HGNCHGNC:6057. INA.
HPACAB002059.
HPA008057.
MIM605338. gene.
neXtProtNX_Q16352.
PharmGKBPA29867.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG149366.
HOGENOMHOG000230977.
HOVERGENHBG013015.
InParanoidQ16352.
KOK07608.
OMARCNVASS.
OrthoDBEOG7FV3Q8.
PhylomeDBQ16352.
TreeFamTF330122.

Gene expression databases

ArrayExpressQ16352.
BgeeQ16352.
CleanExHS_INA.
GenevestigatorQ16352.

Family and domain databases

InterProIPR027703. Alpha-Inx.
IPR001664. IF.
IPR006821. Intermed_filament_DNA-bd.
IPR018039. Intermediate_filament_CS.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PTHR23239:SF132. PTHR23239:SF132. 1 hit.
PfamPF00038. Filament. 1 hit.
PF04732. Filament_head. 1 hit.
[Graphical view]
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSINA. human.
GenomeRNAi9118.
NextBio34171.
PROQ16352.
SOURCESearch...

Entry information

Entry nameAINX_HUMAN
AccessionPrimary (citable) accession number: Q16352
Secondary accession number(s): B1AQK0, Q9BRC5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 137 of the entry and version 2 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 10

Human chromosome 10: entries, gene names and cross-references to MIM