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Q9Y2H6

- FND3A_HUMAN

UniProt

Q9Y2H6 - FND3A_HUMAN

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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

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
Complete GO annotation...

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

Topology

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

GO - Cellular componenti

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

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

BgeeiQ9Y2H6.
CleanExiHS_FNDC3A.
ExpressionAtlasiQ9Y2H6. baseline and differential.
GenevestigatoriQ9Y2H6.

Organism-specific databases

HPAiHPA008927.
HPA012825.

Interactioni

Protein-protein interaction databases

BioGridi116530. 6 interactions.
IntActiQ9Y2H6. 5 interactions.
MINTiMINT-3084391.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00770000120549.
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

        10         20         30         40         50
MAEHPPLLDT TQILSSDISL LSAPIVSADG TQQVILVQVN PGEAFTIRRE
60 70 80 90 100
DGQFQCITGP AQVPMMSPNG SVPPIYVPPG YAPQVIEDNG VRRVVVVPQA
110 120 130 140 150
PEFHPGSHTV LHRSPHPPLP GFIPVPTMMP PPPRHMYSPV TGAGDMTTQY
160 170 180 190 200
MPQYQSSQVY GDVDAHSTHG RSNFRDERSS KTYERLQKKL KDRQGTQKDK
210 220 230 240 250
MSSPPSSPQK CPSPINEHNG LIKGQIAGGI NTGSAKIKSG KGKGGTQVDT
260 270 280 290 300
EIEEKDEETK AFEALLSNIV KPVASDIQAR TVVLTWSPPS SLINGETDES
310 320 330 340 350
SVPELYGYEV LISSTGKDGK YKSVYVGEET NITLNDLKPA MDYHAKVQAE
360 370 380 390 400
YNSIKGTPSE AEIFTTLSCE PDIPNPPRIA NRTKNSLTLQ WKAPSDNGSK
410 420 430 440 450
IQNFVLEWDE GKGNGEFCQC YMGSQKQFKI TKLSPAMGCK FRLSARNDYG
460 470 480 490 500
TSGFSEEVLY YTSGCAPSMP ASPVLTKAGI TWLSLQWSKP SGTPSDEGIS
510 520 530 540 550
YILEMEEETS GYGFKPKYDG EDLAYTVKNL RRSTKYKFKV IAYNSEGKSN
560 570 580 590 600
PSEVVEFTTC PDKPGIPVKP SVKGKIHSHS FKITWDPPKD NGGATINKYV
610 620 630 640 650
VEMAEGSNGN KWEMIYSGAT REHLCDRLNP GCFYRLRVYC ISDGGQSAVS
660 670 680 690 700
ESLLVQTPAV PPGPCLPPRL QGRPKAKEIQ LRWGPPLVDG GSPISCYSVE
710 720 730 740 750
MSPIEKDEPR EVYQGSEVEC TVSSLLPGKT YSFRLRAANK MGFGPFSEKC
760 770 780 790 800
DITTAPGPPD QCKPPQVTCR SATCAQVNWE VPLSNGTDVT EYRLEWGGVE
810 820 830 840 850
GSMQICYCGP GLSYEIKGLS PATTYYCRVQ ALSVVGAGPF SEVVACVTPP
860 870 880 890 900
SVPGIVTCLQ EISDDEIENP HYSPSTCLAI SWEKPCDHGS EILAYSIDFG
910 920 930 940 950
DKQSLTVGKV TSYIINNLQP DTTYRIRIQA LNSLGAGPFS HMIKLKTKPL
960 970 980 990 1000
PPDPPRLECV AFSHQNLKLK WGEGTPKTLS TDSIQYHLQM EDKNGRFVSL
1010 1020 1030 1040 1050
YRGPCHTYKV QRLNESTSYK FCIQACNEAG EGPLSQEYIF TTPKSVPAAL
1060 1070 1080 1090 1100
KAPKIEKVND HICEITWECL QPMKGDPVIY SLQVMLGKDS EFKQIYKGPD
1110 1120 1130 1140 1150
SSFRYSSLQL NCEYRFRVCA IRQCQDSLGH QDLVGPYSTT VLFISQRTEP
1160 1170 1180 1190
PASTNRDTVE STRTRRALSD EQCAAVILVL FAFFSILIAF IIQYFVIK
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. Curated
The sequence BAD18784.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 6 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.
GeneTreei ENSGT00770000120549.
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

Bgeei Q9Y2H6.
CleanExi HS_FNDC3A.
ExpressionAtlasi Q9Y2H6. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 124 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