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Q9Y2H6

- FND3A_HUMAN

UniProt

Q9Y2H6 - FND3A_HUMAN

Protein

Fibronectin type-III domain-containing protein 3A

Gene

FNDC3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 4 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    Mediates spermatid-Sertoli adhesion during spermatogenesis.By similarity

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. fertilization Source: Ensembl
    2. Sertoli cell development Source: Ensembl
    3. single organismal cell-cell adhesion Source: Ensembl
    4. spermatid development Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibronectin type-III domain-containing protein 3A
    Alternative name(s):
    Human gene expressed in odontoblasts
    Gene namesi
    Name:FNDC3A
    Synonyms:FNDC3, HUGO, KIAA0970
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:20296. FNDC3A.

    Subcellular locationi

    GO - Cellular componenti

    1. acrosomal vesicle Source: Ensembl
    2. cytosol Source: Ensembl
    3. Golgi apparatus Source: UniProtKB
    4. Golgi membrane Source: UniProtKB-SubCell
    5. integral component of membrane Source: UniProtKB-KW
    6. membrane Source: UniProtKB
    7. vesicle membrane Source: Ensembl

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA128394588.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11981198Fibronectin type-III domain-containing protein 3APRO_0000087321Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei207 – 2071PhosphoserineBy similarity
    Modified residuei213 – 2131Phosphoserine2 Publications
    Modified residuei384 – 3841N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y2H6.
    PaxDbiQ9Y2H6.
    PRIDEiQ9Y2H6.

    PTM databases

    PhosphoSiteiQ9Y2H6.

    Expressioni

    Tissue specificityi

    Expressed in the odontoblast and nerves in the dental pulp. Also expressed in trachea and to a lesser extent in the brain, liver, lung and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y2H6.
    BgeeiQ9Y2H6.
    CleanExiHS_FNDC3A.
    GenevestigatoriQ9Y2H6.

    Organism-specific databases

    HPAiHPA008927.
    HPA012825.

    Interactioni

    Protein-protein interaction databases

    BioGridi116530. 2 interactions.
    IntActiQ9Y2H6. 5 interactions.
    MINTiMINT-3084391.

    Structurei

    Secondary structure

    1
    1198
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi256 – 26510
    Beta strandi273 – 2764
    Beta strandi282 – 2854
    Beta strandi307 – 3126
    Beta strandi322 – 3287
    Beta strandi330 – 3345
    Beta strandi345 – 3517
    Beta strandi369 – 3713
    Beta strandi378 – 3836
    Beta strandi386 – 3905
    Beta strandi401 – 4088
    Turni410 – 4123
    Beta strandi413 – 4153
    Beta strandi418 – 4247
    Beta strandi426 – 4327
    Beta strandi438 – 4425
    Beta strandi445 – 4495
    Beta strandi458 – 4614
    Beta strandi474 – 4785
    Beta strandi480 – 4867
    Beta strandi495 – 4984
    Beta strandi500 – 5056
    Beta strandi508 – 5114
    Beta strandi515 – 5217
    Beta strandi523 – 5297
    Beta strandi535 – 5439
    Beta strandi548 – 5514
    Beta strandi555 – 5584
    Beta strandi571 – 5777
    Beta strandi580 – 5845
    Beta strandi598 – 60912
    Beta strandi613 – 6164
    Beta strandi621 – 6255
    Beta strandi634 – 6429
    Beta strandi676 – 6827
    Beta strandi696 – 7027
    Beta strandi710 – 7167
    Beta strandi718 – 7247
    Beta strandi730 – 7334
    Beta strandi736 – 7383
    Beta strandi750 – 7534
    Beta strandi768 – 7714
    Beta strandi774 – 7785
    Beta strandi785 – 7873
    Beta strandi791 – 7999
    Beta strandi805 – 8106
    Beta strandi812 – 8187
    Beta strandi824 – 8329
    Beta strandi844 – 8474

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WK0NMR-A256-379[»]
    1X3DNMR-A361-465[»]
    1X4XNMR-A759-851[»]
    1X5XNMR-A467-562[»]
    2CRMNMR-A554-660[»]
    2CRZNMR-A661-757[»]
    ProteinModelPortaliQ9Y2H6.
    SMRiQ9Y2H6. Positions 256-969.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y2H6.

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1177 – 119721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini268 – 369102Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini373 – 46593Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini469 – 56294Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini566 – 66095Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini664 – 75794Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini761 – 85191Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini861 – 95090Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini951 – 104595Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1046 – 1151106Fibronectin type-III 9PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi68 – 13366Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the FNDC3 family.Curated
    Contains 9 fibronectin type-III domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG100680.
    InParanoidiQ9Y2H6.
    OMAiNFRDERS.
    OrthoDBiEOG7F7W8B.
    PhylomeDBiQ9Y2H6.
    TreeFamiTF316401.

    Family and domain databases

    Gene3Di2.60.40.10. 9 hits.
    InterProiIPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PfamiPF00041. fn3. 8 hits.
    [Graphical view]
    SMARTiSM00060. FN3. 9 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 6 hits.
    PROSITEiPS50853. FN3. 9 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative promoter usage. Align

    Isoform 1 (identifier: Q9Y2H6-1) [UniParc]FASTAAdd to Basket

    Also known as: HUGO1

    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.

    « Hide

    MAEHPPLLDT TQILSSDISL LSAPIVSADG TQQVILVQVN PGEAFTIRRE     50
    DGQFQCITGP AQVPMMSPNG SVPPIYVPPG YAPQVIEDNG VRRVVVVPQA 100
    PEFHPGSHTV LHRSPHPPLP GFIPVPTMMP PPPRHMYSPV TGAGDMTTQY 150
    MPQYQSSQVY GDVDAHSTHG RSNFRDERSS KTYERLQKKL KDRQGTQKDK 200
    MSSPPSSPQK CPSPINEHNG LIKGQIAGGI NTGSAKIKSG KGKGGTQVDT 250
    EIEEKDEETK AFEALLSNIV KPVASDIQAR TVVLTWSPPS SLINGETDES 300
    SVPELYGYEV LISSTGKDGK YKSVYVGEET NITLNDLKPA MDYHAKVQAE 350
    YNSIKGTPSE AEIFTTLSCE PDIPNPPRIA NRTKNSLTLQ WKAPSDNGSK 400
    IQNFVLEWDE GKGNGEFCQC YMGSQKQFKI TKLSPAMGCK FRLSARNDYG 450
    TSGFSEEVLY YTSGCAPSMP ASPVLTKAGI TWLSLQWSKP SGTPSDEGIS 500
    YILEMEEETS GYGFKPKYDG EDLAYTVKNL RRSTKYKFKV IAYNSEGKSN 550
    PSEVVEFTTC PDKPGIPVKP SVKGKIHSHS FKITWDPPKD NGGATINKYV 600
    VEMAEGSNGN KWEMIYSGAT REHLCDRLNP GCFYRLRVYC ISDGGQSAVS 650
    ESLLVQTPAV PPGPCLPPRL QGRPKAKEIQ LRWGPPLVDG GSPISCYSVE 700
    MSPIEKDEPR EVYQGSEVEC TVSSLLPGKT YSFRLRAANK MGFGPFSEKC 750
    DITTAPGPPD QCKPPQVTCR SATCAQVNWE VPLSNGTDVT EYRLEWGGVE 800
    GSMQICYCGP GLSYEIKGLS PATTYYCRVQ ALSVVGAGPF SEVVACVTPP 850
    SVPGIVTCLQ EISDDEIENP HYSPSTCLAI SWEKPCDHGS EILAYSIDFG 900
    DKQSLTVGKV TSYIINNLQP DTTYRIRIQA LNSLGAGPFS HMIKLKTKPL 950
    PPDPPRLECV AFSHQNLKLK WGEGTPKTLS TDSIQYHLQM EDKNGRFVSL 1000
    YRGPCHTYKV QRLNESTSYK FCIQACNEAG EGPLSQEYIF TTPKSVPAAL 1050
    KAPKIEKVND HICEITWECL QPMKGDPVIY SLQVMLGKDS EFKQIYKGPD 1100
    SSFRYSSLQL NCEYRFRVCA IRQCQDSLGH QDLVGPYSTT VLFISQRTEP 1150
    PASTNRDTVE STRTRRALSD EQCAAVILVL FAFFSILIAF IIQYFVIK 1198
    Length:1,198
    Mass (Da):131,852
    Last modified:July 28, 2009 - v4
    Checksum:i2809E41E89BDD095
    GO
    Isoform 2 (identifier: Q9Y2H6-2) [UniParc]FASTAAdd to Basket

    Also known as: HUGO2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: Missing.
         57-58: IT → MS

    Show »
    Length:1,142
    Mass (Da):125,822
    Checksum:i2136F2F51012A73F
    GO

    Sequence cautioni

    The sequence BAA76814.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAD18784.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531Q → R in CAI45989. (PubMed:17974005)Curated
    Sequence conflicti350 – 3501E → G in CAE45852. (PubMed:17974005)Curated
    Sequence conflicti501 – 5011Y → H in CAE45852. (PubMed:17974005)Curated
    Sequence conflicti839 – 8391P → R in AAH60816. (PubMed:15489334)Curated
    Sequence conflicti839 – 8391P → R in AAH70072. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071S → G.
    Corresponds to variant rs34539036 [ dbSNP | Ensembl ].
    VAR_059655

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5656Missing in isoform 2. 4 PublicationsVSP_037723Add
    BLAST
    Alternative sequencei57 – 582IT → MS in isoform 2. 4 PublicationsVSP_037724

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ749706 mRNA. Translation: CAG44602.1.
    AJ749707 mRNA. Translation: CAG44603.1.
    AB023187 mRNA. Translation: BAA76814.2. Different initiation.
    AK172814 mRNA. Translation: BAD18784.1. Different initiation.
    AK302415 mRNA. Translation: BAG63723.1.
    BX640739 mRNA. Translation: CAE45852.1.
    BX648141 mRNA. Translation: CAI45989.1.
    AL161421, AL137000, AL359184 Genomic DNA. Translation: CAH70653.1.
    AL359184, AL137000, AL161421 Genomic DNA. Translation: CAH73933.1.
    AL137000, AL161421, AL359184 Genomic DNA. Translation: CAI39727.1.
    AL137000 Genomic DNA. Translation: CAI39726.2.
    CH471075 Genomic DNA. Translation: EAX08804.1.
    CH471075 Genomic DNA. Translation: EAX08806.1.
    BC060816 mRNA. Translation: AAH60816.1.
    BC070072 mRNA. Translation: AAH70072.1.
    BC132812 mRNA. Translation: AAI32813.1.
    BC136617 mRNA. Translation: AAI36618.1.
    BC144301 mRNA. Translation: AAI44302.1.
    CCDSiCCDS41886.1. [Q9Y2H6-1]
    CCDS9413.2. [Q9Y2H6-2]
    RefSeqiNP_001073141.1. NM_001079673.1. [Q9Y2H6-1]
    NP_001265367.1. NM_001278438.1. [Q9Y2H6-1]
    NP_055738.3. NM_014923.4. [Q9Y2H6-2]
    UniGeneiHs.508010.

    Genome annotation databases

    EnsembliENST00000398316; ENSP00000381362; ENSG00000102531. [Q9Y2H6-2]
    ENST00000492622; ENSP00000417257; ENSG00000102531. [Q9Y2H6-1]
    ENST00000541916; ENSP00000441831; ENSG00000102531. [Q9Y2H6-1]
    GeneIDi22862.
    KEGGihsa:22862.
    UCSCiuc001vcm.3. human. [Q9Y2H6-1]
    uc001vcp.1. human. [Q9Y2H6-2]

    Polymorphism databases

    DMDMi254763442.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ749706 mRNA. Translation: CAG44602.1 .
    AJ749707 mRNA. Translation: CAG44603.1 .
    AB023187 mRNA. Translation: BAA76814.2 . Different initiation.
    AK172814 mRNA. Translation: BAD18784.1 . Different initiation.
    AK302415 mRNA. Translation: BAG63723.1 .
    BX640739 mRNA. Translation: CAE45852.1 .
    BX648141 mRNA. Translation: CAI45989.1 .
    AL161421 , AL137000 , AL359184 Genomic DNA. Translation: CAH70653.1 .
    AL359184 , AL137000 , AL161421 Genomic DNA. Translation: CAH73933.1 .
    AL137000 , AL161421 , AL359184 Genomic DNA. Translation: CAI39727.1 .
    AL137000 Genomic DNA. Translation: CAI39726.2 .
    CH471075 Genomic DNA. Translation: EAX08804.1 .
    CH471075 Genomic DNA. Translation: EAX08806.1 .
    BC060816 mRNA. Translation: AAH60816.1 .
    BC070072 mRNA. Translation: AAH70072.1 .
    BC132812 mRNA. Translation: AAI32813.1 .
    BC136617 mRNA. Translation: AAI36618.1 .
    BC144301 mRNA. Translation: AAI44302.1 .
    CCDSi CCDS41886.1. [Q9Y2H6-1 ]
    CCDS9413.2. [Q9Y2H6-2 ]
    RefSeqi NP_001073141.1. NM_001079673.1. [Q9Y2H6-1 ]
    NP_001265367.1. NM_001278438.1. [Q9Y2H6-1 ]
    NP_055738.3. NM_014923.4. [Q9Y2H6-2 ]
    UniGenei Hs.508010.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WK0 NMR - A 256-379 [» ]
    1X3D NMR - A 361-465 [» ]
    1X4X NMR - A 759-851 [» ]
    1X5X NMR - A 467-562 [» ]
    2CRM NMR - A 554-660 [» ]
    2CRZ NMR - A 661-757 [» ]
    ProteinModelPortali Q9Y2H6.
    SMRi Q9Y2H6. Positions 256-969.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116530. 2 interactions.
    IntActi Q9Y2H6. 5 interactions.
    MINTi MINT-3084391.

    PTM databases

    PhosphoSitei Q9Y2H6.

    Polymorphism databases

    DMDMi 254763442.

    Proteomic databases

    MaxQBi Q9Y2H6.
    PaxDbi Q9Y2H6.
    PRIDEi Q9Y2H6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398316 ; ENSP00000381362 ; ENSG00000102531 . [Q9Y2H6-2 ]
    ENST00000492622 ; ENSP00000417257 ; ENSG00000102531 . [Q9Y2H6-1 ]
    ENST00000541916 ; ENSP00000441831 ; ENSG00000102531 . [Q9Y2H6-1 ]
    GeneIDi 22862.
    KEGGi hsa:22862.
    UCSCi uc001vcm.3. human. [Q9Y2H6-1 ]
    uc001vcp.1. human. [Q9Y2H6-2 ]

    Organism-specific databases

    CTDi 22862.
    GeneCardsi GC13P049550.
    H-InvDB HIX0011312.
    HGNCi HGNC:20296. FNDC3A.
    HPAi HPA008927.
    HPA012825.
    MIMi 615794. gene.
    neXtProti NX_Q9Y2H6.
    PharmGKBi PA128394588.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG100680.
    InParanoidi Q9Y2H6.
    OMAi NFRDERS.
    OrthoDBi EOG7F7W8B.
    PhylomeDBi Q9Y2H6.
    TreeFami TF316401.

    Miscellaneous databases

    ChiTaRSi FNDC3A. human.
    EvolutionaryTracei Q9Y2H6.
    GeneWikii FNDC3A.
    GenomeRNAii 22862.
    NextBioi 43369.
    PROi Q9Y2H6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2H6.
    Bgeei Q9Y2H6.
    CleanExi HS_FNDC3A.
    Genevestigatori Q9Y2H6.

    Family and domain databases

    Gene3Di 2.60.40.10. 9 hits.
    InterProi IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    Pfami PF00041. fn3. 8 hits.
    [Graphical view ]
    SMARTi SM00060. FN3. 9 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 6 hits.
    PROSITEi PS50853. FN3. 9 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "HUGO (FNDC3A): a new gene overexpressed in human odontoblasts."
      Carrouel F., Couble M.-L., Vanbelle C., Staquet M.-J., Magloire H., Bleicher F.
      J. Dent. Res. 87:131-136(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE PROMOTER USAGE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Dental pulp and Odontoblast.
    2. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "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.
      , 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 2).
      Tissue: Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Cervix and Fetal kidney.
    6. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 1).
      Tissue: Brain, Placenta and Testis.
    9. "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-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Solution structure of fibronectin type III domains derived from human KIAA0970 protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JAN-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 256-851.

    Entry informationi

    Entry nameiFND3A_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2H6
    Secondary accession number(s): B4DYG1
    , Q5HYC9, Q5JVF8, Q5JVF9, Q6EVH3, Q6EVH4, Q6N020, Q6P9D5, Q6ZME4, Q9H1W1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 122 of the entry and version 4 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3