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AINX_HUMAN
ID   AINX_HUMAN              Reviewed;         499 AA.
AC   Q16352; B1AQK0; Q9BRC5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   03-AUG-2022, entry version 192.
DE   RecName: Full=Alpha-internexin;
DE            Short=Alpha-Inx;
DE   AltName: Full=66 kDa neurofilament protein;
DE            Short=NF-66;
DE            Short=Neurofilament-66;
DE   AltName: Full=Neurofilament 5;
GN   Name=INA; Synonyms=NEF5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-92.
RC   TISSUE=Fetal brain;
RX   PubMed=7769995; DOI=10.1016/0169-328x(94)00268-j;
RA   Chan S.-O., Chiu F.-C.;
RT   "Cloning and developmental expression of human 66 kd neurofilament
RT   protein.";
RL   Brain Res. Mol. Brain Res. 29:177-184(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 46-83; 105-111; 121-130; 139-145; 216-228; 279-288;
RP   323-330; 339-367; 378-397 AND 407-430, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-290, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [8]
RP   VARIANT [LARGE SCALE ANALYSIS] GLN-110.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Class-IV neuronal intermediate filament that is able to self-
CC       assemble. It is involved in the morphogenesis of neurons. It may form
CC       an independent structural network without the involvement of other
CC       neurofilaments or it may cooperate with NEFL to form the filamentous
CC       backbone to which NEFM and NEFH attach to form the cross-bridges. May
CC       also cooperate with the neuronal intermediate filament protein PRPH to
CC       form filamentous networks (By similarity).
CC       {ECO:0000250|UniProtKB:P46660}.
CC   -!- SUBUNIT: Forms homodimers (in vitro) (By similarity). Forms
CC       heterodimers with NEFL, NEFM or NEFH (in vitro) (By similarity).
CC       {ECO:0000250|UniProtKB:P23565}.
CC   -!- INTERACTION:
CC       Q16352; P05067: APP; NbExp=3; IntAct=EBI-366258, EBI-77613;
CC       Q16352; P37840: SNCA; NbExp=3; IntAct=EBI-366258, EBI-985879;
CC   -!- TISSUE SPECIFICITY: Found predominantly in adult CNS.
CC   -!- DEVELOPMENTAL STAGE: Expressed in brain as early as the 16th week of
CC       gestation, and increased rapidly and reached a steady state level by
CC       the 18th week of gestation.
CC   -!- PTM: O-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; S78296; AAB34482.1; -; mRNA.
DR   EMBL; AL591408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471066; EAW49653.1; -; Genomic_DNA.
DR   EMBL; BC006359; AAH06359.1; -; mRNA.
DR   CCDS; CCDS7545.1; -.
DR   PIR; I52658; I52658.
DR   RefSeq; NP_116116.1; NM_032727.3.
DR   AlphaFoldDB; Q16352; -.
DR   SMR; Q16352; -.
DR   BioGRID; 114566; 106.
DR   IntAct; Q16352; 54.
DR   MINT; Q16352; -.
DR   STRING; 9606.ENSP00000358865; -.
DR   GlyGen; Q16352; 6 sites, 1 O-linked glycan (6 sites).
DR   iPTMnet; Q16352; -.
DR   PhosphoSitePlus; Q16352; -.
DR   SwissPalm; Q16352; -.
DR   BioMuta; INA; -.
DR   DMDM; 20141266; -.
DR   EPD; Q16352; -.
DR   jPOST; Q16352; -.
DR   MassIVE; Q16352; -.
DR   MaxQB; Q16352; -.
DR   PaxDb; Q16352; -.
DR   PeptideAtlas; Q16352; -.
DR   PRIDE; Q16352; -.
DR   ProteomicsDB; 60861; -.
DR   Antibodypedia; 1538; 498 antibodies from 41 providers.
DR   DNASU; 9118; -.
DR   Ensembl; ENST00000369849.9; ENSP00000358865.4; ENSG00000148798.11.
DR   GeneID; 9118; -.
DR   KEGG; hsa:9118; -.
DR   MANE-Select; ENST00000369849.9; ENSP00000358865.4; NM_032727.4; NP_116116.1.
DR   UCSC; uc001kws.3; human.
DR   CTD; 9118; -.
DR   DisGeNET; 9118; -.
DR   GeneCards; INA; -.
DR   HGNC; HGNC:6057; INA.
DR   HPA; ENSG00000148798; Group enriched (brain, retina).
DR   MIM; 605338; gene.
DR   neXtProt; NX_Q16352; -.
DR   OpenTargets; ENSG00000148798; -.
DR   PharmGKB; PA29867; -.
DR   VEuPathDB; HostDB:ENSG00000148798; -.
DR   eggNOG; ENOG502RAU0; Eukaryota.
DR   GeneTree; ENSGT00940000154418; -.
DR   HOGENOM; CLU_012560_7_3_1; -.
DR   InParanoid; Q16352; -.
DR   OMA; EHYLCSA; -.
DR   OrthoDB; 888678at2759; -.
DR   PhylomeDB; Q16352; -.
DR   TreeFam; TF330122; -.
DR   PathwayCommons; Q16352; -.
DR   SignaLink; Q16352; -.
DR   BioGRID-ORCS; 9118; 6 hits in 1066 CRISPR screens.
DR   ChiTaRS; INA; human.
DR   GenomeRNAi; 9118; -.
DR   Pharos; Q16352; Tbio.
DR   PRO; PR:Q16352; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q16352; protein.
DR   Bgee; ENSG00000148798; Expressed in cortical plate and 126 other tissues.
DR   Genevisible; Q16352; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0005882; C:intermediate filament; IBA:GO_Central.
DR   GO; GO:0005883; C:neurofilament; TAS:ProtInc.
DR   GO; GO:0099160; C:postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR   GO; GO:0098973; F:structural constituent of postsynaptic actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0099184; F:structural constituent of postsynaptic intermediate filament cytoskeleton; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IEA:Ensembl.
DR   GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR   InterPro; IPR027703; Alpha-Inx.
DR   InterPro; IPR018039; IF_conserved.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR006821; Intermed_filament_DNA-bd.
DR   PANTHER; PTHR45652:SF18; PTHR45652:SF18; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF04732; Filament_head; 1.
DR   SMART; SM01391; Filament; 1.
DR   PROSITE; PS00226; IF_ROD_1; 1.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Developmental protein; Differentiation;
KW   Direct protein sequencing; Glycoprotein; Intermediate filament;
KW   Neurogenesis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..499
FT                   /note="Alpha-internexin"
FT                   /id="PRO_0000063783"
FT   DOMAIN          94..407
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..87
FT                   /note="Head"
FT   REGION          88..129
FT                   /note="Coil 1A"
FT   REGION          130..142
FT                   /note="Linker 1"
FT   REGION          143..238
FT                   /note="Coil 1B"
FT   REGION          239..262
FT                   /note="Linker 2"
FT   REGION          263..408
FT                   /note="Coil 2"
FT   REGION          409..499
FT                   /note="Tail"
FT   REGION          441..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46660"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46660"
FT   MOD_RES         290
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P46660"
FT   MOD_RES         469
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P23565"
FT   MOD_RES         496
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   VARIANT         92
FT                   /note="T -> S (in dbSNP:rs1063455)"
FT                   /evidence="ECO:0000269|PubMed:7769995"
FT                   /id="VAR_049808"
FT   VARIANT         110
FT                   /note="E -> Q (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036369"
FT   VARIANT         149
FT                   /note="D -> H (in dbSNP:rs1063456)"
FT                   /id="VAR_033497"
FT   CONFLICT        37..41
FT                   /note="GFRSQ -> ASVE (in Ref. 1; AAB34482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        67
FT                   /note="R -> A (in Ref. 1; AAB34482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128..132
FT                   /note="ALRQR -> RCDT (in Ref. 1; AAB34482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="E -> Q (in Ref. 1; AAB34482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        147..152
FT                   /note="LRDLRA -> PRHLP (in Ref. 1; AAB34482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        191..198
FT                   /note="GAERALKA -> RRARLKR (in Ref. 1; AAB34482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        244
FT                   /note="A -> R (in Ref. 1; AAB34482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        263
FT                   /note="S -> A (in Ref. 1; AAB34482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        301
FT                   /note="S -> T (in Ref. 1; AAB34482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        310..311
FT                   /note="EE -> DQ (in Ref. 1; AAB34482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        318
FT                   /note="Missing (in Ref. 1; AAB34482)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   499 AA;  55391 MW;  4C972764E9E68D3E CRC64;
     MSFGSEHYLC SSSSYRKVFG DGSRLSARLS GAGGAGGFRS QSLSRSNVAS SAACSSASSL
     GLGLAYRRPP ASDGLDLSQA AARTNEYKII RTNEKEQLQG LNDRFAVFIE KVHQLETQNR
     ALEAELAALR QRHAEPSRVG ELFQRELRDL RAQLEEASSA RSQALLERDG LAEEVQRLRA
     RCEEESRGRE GAERALKAQQ RDVDGATLAR LDLEKKVESL LDELAFVRQV HDEEVAELLA
     TLQASSQAAA EVDVTVAKPD LTSALREIRA QYESLAAKNL QSAEEWYKSK FANLNEQAAR
     STEAIRASRE EIHEYRRQLQ ARTIEIEGLR GANESLERQI LELEERHSAE VAGYQDSIGQ
     LENDLRNTKS EMARHLREYQ DLLNVKMALD IEIAAYRKLL EGEETRFSTS GLSISGLNPL
     PNPSYLLPPR ILSATTSKVS STGLSLKKEE EEEEASKVAS KKTSQIGESF EEILEETVIS
     TKKTEKSNIE ETTISSQKI
 
 
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