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Protein

FH1/FH2 domain-containing protein 3

Gene

FHOD3

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

Functioni

Actin-organizing protein that may cause stress fiber formation together with cell elongation (By similarity). Isoform 4 may play a role in actin filament polymerization in cardiomyocytes.By similarity1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

SIGNORiQ2V2M9.

Names & Taxonomyi

Protein namesi
Recommended name:
FH1/FH2 domain-containing protein 3
Alternative name(s):
Formactin-2
Formin homolog overexpressed in spleen 2
Short name:
hFHOS2
Gene namesi
Name:FHOD3
Synonyms:FHOS2, KIAA1695
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:26178. FHOD3.

Subcellular locationi

  • Cytoplasmcytoskeleton 1 Publication

  • Note: Main part of the protein localizes to actin fibers and the remaining part displays filamentous staining.By similarity
Isoform 4 :
  • CytoplasmmyofibrilsarcomereZ line

  • Note: Threonine phosphorylation in isoform 4-specific sequence TDTDEEEEVE is required for targeting to myofibrils in cardiomyocytes.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134929910.

Polymorphism and mutation databases

DMDMi300669639.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14221422FH1/FH2 domain-containing protein 3PRO_0000283791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei345 – 3451PhosphoserineBy similarity
Modified residuei375 – 3751PhosphoserineBy similarity
Modified residuei763 – 7631PhosphoserineBy similarity
Modified residuei775 – 7751PhosphothreonineBy similarity
Isoform 4 (identifier: Q2V2M9-4)
Modified residuei1474 – 14741Phosphothreonine1 Publication
Modified residuei1476 – 14761Phosphothreonine1 Publication

Post-translational modificationi

Isoform 4: Phosphorylated on Thr-1474 and Thr-1476 by CK2.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ2V2M9.
MaxQBiQ2V2M9.
PaxDbiQ2V2M9.
PRIDEiQ2V2M9.

PTM databases

iPTMnetiQ2V2M9.
PhosphoSiteiQ2V2M9.

Expressioni

Tissue specificityi

Expressed in the heart, kidney and brain. May be down-regulated in various types of heart diseases, including idiopathic dilated, ventricular dilated, familial dilated and perinatal dilated cardiomyopathies, as well as ischemic heart disease (at protein level).2 Publications

Gene expression databases

BgeeiQ2V2M9.
CleanExiHS_FHOD3.
ExpressionAtlasiQ2V2M9. baseline and differential.
GenevisibleiQ2V2M9. HS.

Organism-specific databases

HPAiHPA021827.
HPA024696.

Interactioni

Subunit structurei

Interacts with nestin/NES-based interfilament (IF) (By similarity). Interacts with SQSTM1; isoform 4 threonine phosphorylation disrupts SQSTM1-binding.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SQSTM1Q135016EBI-6395541,EBI-307104

Protein-protein interaction databases

BioGridi123175. 2 interactions.
IntActiQ2V2M9. 3 interactions.
STRINGi9606.ENSP00000257209.

Structurei

3D structure databases

ProteinModelPortaliQ2V2M9.
SMRiQ2V2M9. Positions 2-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 411394GBD/FH3PROSITE-ProRule annotationAdd
BLAST
Domaini827 – 85832FH1Add
BLAST
Domaini883 – 1279397FH2PROSITE-ProRule annotationAdd
BLAST
Domaini1359 – 139133DADPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili448 – 48033Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi626 – 63510Poly-Ser
Compositional biasi827 – 87246Pro-richAdd
BLAST
Compositional biasi889 – 8924Poly-Lys

Domaini

The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments (By similarity).By similarity

Sequence similaritiesi

Belongs to the formin homology family.Curated
Contains 1 DAD (diaphanous autoregulatory) domain.PROSITE-ProRule annotation
Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1925. Eukaryota.
ENOG410XRBZ. LUCA.
GeneTreeiENSGT00810000125396.
HOVERGENiHBG051615.
InParanoidiQ2V2M9.
OMAiDKLPYVP.
OrthoDBiEOG71G9T2.
PhylomeDBiQ2V2M9.
TreeFamiTF316268.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. DAD_dom.
IPR015425. FH2_Formin.
IPR027651. FHOD3.
IPR014768. GBD/FH3_dom.
[Graphical view]
PANTHERiPTHR23213:SF213. PTHR23213:SF213. 3 hits.
PfamiPF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q2V2M9-1) [UniParc]FASTAAdd to basket

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
MATLACRVQF LDDTDPFNST NFPEPSRPPL FTFREDLALG TQLAGVHRLL
60 70 80 90 100
QAPHKLDDCT LQLSHNGAYL DLEATLAEQR DELEGFQDDA GRGKKHSIIL
110 120 130 140 150
RTQLSVRVHA CIEKLYNSSG RDLRRALFSL KQIFQDDKDL VHEFVVAEGL
160 170 180 190 200
TCLIKVGAEA DQNYQNYILR ALGQIMLYVD GMNGVINRNE TIQWLYTLIG
210 220 230 240 250
SKFRLVVKTA LKLLLVFVEY SESNAPLLIQ AVTAVDTKRG VKPWSNIMEI
260 270 280 290 300
LEEKDGVDTE LLVYAMTLVN KTLSGLPDQD TFYDVVDCLE ELGIAAVSQR
310 320 330 340 350
HLNKKGTDLD LVEQLNIYEV ALRHEDGDET TEPPPSGCRD RRRASVCSSG
360 370 380 390 400
GGEHRGLDRR RSRRHSVQSI KSTLSAPTSP CSQSAPSFKP NQVRDLREKY
410 420 430 440 450
SNFGNNSYHS SRPSSGSSVP TTPTSSVSPP QEARLERSSP SGLLTSSFRQ
460 470 480 490 500
HQESLAAERE RRRQEREERL QRIEREERNK FRYKYLEQLA AEEHEKELRS
510 520 530 540 550
RSVSRGRADL SLDLTSPAAP ACLAPLSHSP SSSDSQEALT VSASSPGTPH
560 570 580 590 600
HPQASAGDPE PESEAEPEAE AGAGQVADEA GQDIASAHEG AETEVEQALE
610 620 630 640 650
QEPEERASLS EKERQNEGVN ERDNCSASSV SSSSSTLERE EKEDKLSRDR
660 670 680 690 700
TTGLWPAGVQ DAGVNGQCGD ILTNKRFMLD MLYAHNRKSP DDEEKGDGEA
710 720 730 740 750
GRTQQEAEAV ASLATRISTL QANSQTQDES VRRVDVGCLD NRGSVKAFAE
760 770 780 790 800
KFNSGDLGRG SISPDAEPND KVPETAPVQP KTESDYIWDQ LMANPRELRI
810 820 830 840 850
QDMDFTDLGE EDDIDVLDVD LGHREAPGPP PPPPPTFLGL PPPPPPPLLD
860 870 880 890 900
SIPPPPVPGN LLVPPPPVFN APQGLGWSQV PRGQPTFTKK KKTIRLFWNE
910 920 930 940 950
VRPFDWPCKN NRRCREFLWS KLEPIKVDTS RLEHLFESKS KELSVSKKTA
960 970 980 990 1000
ADGKRQEIIV LDSKRSNAIN IGLTVLPPPR TIKIAILNFD EYALNKEGIE
1010 1020 1030 1040 1050
KILTMIPTDE EKQKIQEAQL ANPEIPLGSA EQFLLTLSSI SELSARLHLW
1060 1070 1080 1090 1100
AFKMDYETTE KEVAEPLLDL KEGIDQLENN KTLGFILSTL LAIGNFLNGT
1110 1120 1130 1140 1150
NAKAFELSYL EKVPEVKDTV HKQSLLHHVC TMVVENFPDS SDLYSEIGAI
1160 1170 1180 1190 1200
TRSAKVDFDQ LQDNLCQMER RCKASWDHLK AIAKHEMKPV LKQRMSEFLK
1210 1220 1230 1240 1250
DCAERIIILK IVHRRIINRF HSFLLFMGHP PYAIREVNIN KFCRIISEFA
1260 1270 1280 1290 1300
LEYRTTRERV LQQKQKRANH RERNKTRGKM ITDSGKFSGS SPAPPSQPQG
1310 1320 1330 1340 1350
LSYAEDAAEH ENMKAVLKTS SPSVEDATPA LGVRTRSRAS RGSTSSWTMG
1360 1370 1380 1390 1400
TDDSPNVTDD AADEIMDRIV KSATQVPSQR VVPRERKRSR ANRKSLRRTL
1410 1420
KSGLTPEEAR ALGLVGTSEL QL
Length:1,422
Mass (Da):158,613
Last modified:July 13, 2010 - v2
Checksum:i7CE7A8C0054856BE
GO
Isoform 2 (identifier: Q2V2M9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     400-437: Missing.
     481-481: F → FSRDYLDKREEQRQAREE

Show »
Length:1,401
Mass (Da):156,752
Checksum:iF2B9F0473D7D3BC6
GO
Isoform 3 (identifier: Q2V2M9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     481-481: F → FSRDYLDKREEQRQAREE

Note: Prediction based on ESTs. No experimental confirmation available.
Show »
Length:1,439
Mass (Da):160,804
Checksum:i72C7122A8348E1A9
GO
Isoform 4 (identifier: Q2V2M9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     399-399: K → KEEEEEEEQP...YHFRSFSSNR
     481-481: F → FSRDYLDKREEQRQAREE
     1282-1283: TD → TDTDEEEEVE

Show »
Length:1,622
Mass (Da):180,080
Checksum:iEFCFEA5D7FF75299
GO

Sequence cautioni

The sequence BAB15292.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB15463.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711D → G in BAC67014 (PubMed:15966898).Curated
Sequence conflicti202 – 2021K → E in ADL62709 (PubMed:21149568).Curated
Sequence conflicti432 – 4321E → G in ADL62709 (PubMed:21149568).Curated
Sequence conflicti435 – 4351L → W in BAC67014 (PubMed:15966898).Curated
Sequence conflicti527 – 5271S → G in ADL62709 (PubMed:21149568).Curated
Sequence conflicti581 – 5811G → A in ADL62709 (PubMed:21149568).Curated
Sequence conflicti647 – 6471S → P in ADL62709 (PubMed:21149568).Curated
Sequence conflicti654 – 6541L → K in BAC87252 (PubMed:14702039).Curated
Sequence conflicti1134 – 11341V → I in AAH81563 (PubMed:15489334).Curated
Sequence conflicti1417 – 14171T → A in BAB15463 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti475 – 4751R → W.
Corresponds to variant rs9964535 [ dbSNP | Ensembl ].
VAR_055804

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei399 – 3991K → KEEEEEEEQPITEPSSEEER EDDASCQGKDSKVGAASGQS PTGRDAAPKSSALPAVSNAS SQGKPLLVGTAGGTTWHSGS SGSEATPSALLSPPASAARP SSATPGSLKVSPTIDKLPYV PHSPFHLFSYDFEDSSLSTK EKEAESQKENSSSDSFSLST YSASEPYHFRSFSSNR in isoform 4. 1 PublicationVSP_044682
Alternative sequencei400 – 43738Missing in isoform 2. 1 PublicationVSP_024397Add
BLAST
Alternative sequencei481 – 4811F → FSRDYLDKREEQRQAREE in isoform 2, isoform 3 and isoform 4. 2 PublicationsVSP_024398
Alternative sequencei1282 – 12832TD → TDTDEEEEVE in isoform 4. 1 PublicationVSP_044683

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB084087 mRNA. Translation: BAC67014.1.
HM191478 mRNA. Translation: ADL62709.1.
AC023043 Genomic DNA. No translation available.
AC055840 Genomic DNA. No translation available.
AC090333 Genomic DNA. No translation available.
AC131053 Genomic DNA. No translation available.
AK025950 mRNA. Translation: BAB15292.1. Different initiation.
AK026370 mRNA. Translation: BAB15463.1. Different initiation.
AK128053 mRNA. Translation: BAC87252.1.
AB051482 mRNA. Translation: BAB21786.1.
BC050670 mRNA. Translation: AAH50670.1.
BC081563 mRNA. Translation: AAH81563.1.
AL834480 mRNA. Translation: CAD39139.1.
CCDSiCCDS32816.1. [Q2V2M9-3]
CCDS62418.1. [Q2V2M9-4]
CCDS62419.1. [Q2V2M9-1]
RefSeqiNP_001268668.1. NM_001281739.2. [Q2V2M9-1]
NP_001268669.1. NM_001281740.2. [Q2V2M9-4]
NP_079411.2. NM_025135.4. [Q2V2M9-3]
XP_005258412.1. XM_005258355.1. [Q2V2M9-2]
UniGeneiHs.436636.
Hs.630884.

Genome annotation databases

EnsembliENST00000257209; ENSP00000257209; ENSG00000134775. [Q2V2M9-3]
ENST00000359247; ENSP00000352186; ENSG00000134775. [Q2V2M9-1]
ENST00000590592; ENSP00000466937; ENSG00000134775. [Q2V2M9-4]
GeneIDi80206.
KEGGihsa:80206.
UCSCiuc002kzs.3. human. [Q2V2M9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB084087 mRNA. Translation: BAC67014.1.
HM191478 mRNA. Translation: ADL62709.1.
AC023043 Genomic DNA. No translation available.
AC055840 Genomic DNA. No translation available.
AC090333 Genomic DNA. No translation available.
AC131053 Genomic DNA. No translation available.
AK025950 mRNA. Translation: BAB15292.1. Different initiation.
AK026370 mRNA. Translation: BAB15463.1. Different initiation.
AK128053 mRNA. Translation: BAC87252.1.
AB051482 mRNA. Translation: BAB21786.1.
BC050670 mRNA. Translation: AAH50670.1.
BC081563 mRNA. Translation: AAH81563.1.
AL834480 mRNA. Translation: CAD39139.1.
CCDSiCCDS32816.1. [Q2V2M9-3]
CCDS62418.1. [Q2V2M9-4]
CCDS62419.1. [Q2V2M9-1]
RefSeqiNP_001268668.1. NM_001281739.2. [Q2V2M9-1]
NP_001268669.1. NM_001281740.2. [Q2V2M9-4]
NP_079411.2. NM_025135.4. [Q2V2M9-3]
XP_005258412.1. XM_005258355.1. [Q2V2M9-2]
UniGeneiHs.436636.
Hs.630884.

3D structure databases

ProteinModelPortaliQ2V2M9.
SMRiQ2V2M9. Positions 2-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123175. 2 interactions.
IntActiQ2V2M9. 3 interactions.
STRINGi9606.ENSP00000257209.

PTM databases

iPTMnetiQ2V2M9.
PhosphoSiteiQ2V2M9.

Polymorphism and mutation databases

DMDMi300669639.

Proteomic databases

EPDiQ2V2M9.
MaxQBiQ2V2M9.
PaxDbiQ2V2M9.
PRIDEiQ2V2M9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000257209; ENSP00000257209; ENSG00000134775. [Q2V2M9-3]
ENST00000359247; ENSP00000352186; ENSG00000134775. [Q2V2M9-1]
ENST00000590592; ENSP00000466937; ENSG00000134775. [Q2V2M9-4]
GeneIDi80206.
KEGGihsa:80206.
UCSCiuc002kzs.3. human. [Q2V2M9-1]

Organism-specific databases

CTDi80206.
GeneCardsiFHOD3.
H-InvDBHIX0014410.
HIX0174208.
HGNCiHGNC:26178. FHOD3.
HPAiHPA021827.
HPA024696.
MIMi609691. gene.
neXtProtiNX_Q2V2M9.
PharmGKBiPA134929910.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1925. Eukaryota.
ENOG410XRBZ. LUCA.
GeneTreeiENSGT00810000125396.
HOVERGENiHBG051615.
InParanoidiQ2V2M9.
OMAiDKLPYVP.
OrthoDBiEOG71G9T2.
PhylomeDBiQ2V2M9.
TreeFamiTF316268.

Enzyme and pathway databases

SIGNORiQ2V2M9.

Miscellaneous databases

ChiTaRSiFHOD3. human.
GenomeRNAii80206.
PROiQ2V2M9.
SOURCEiSearch...

Gene expression databases

BgeeiQ2V2M9.
CleanExiHS_FHOD3.
ExpressionAtlasiQ2V2M9. baseline and differential.
GenevisibleiQ2V2M9. HS.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR014767. DAD_dom.
IPR015425. FH2_Formin.
IPR027651. FHOD3.
IPR014768. GBD/FH3_dom.
[Graphical view]
PANTHERiPTHR23213:SF213. PTHR23213:SF213. 3 hits.
PfamiPF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51231. DAD. 1 hit.
PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Fhos2, a novel formin-related actin-organizing protein, probably associates with the nestin intermediate filament."
    Kanaya H., Takeya R., Takeuchi K., Watanabe N., Jing N., Sumimoto H.
    Genes Cells 10:665-678(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. "Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance."
    Iskratsch T., Lange S., Dwyer J., Kho A.L., dos Remedios C., Ehler E.
    J. Cell Biol. 191:1159-1172(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-1474 AND THR-1476 (ISOFORM 4), TISSUE SPECIFICITY.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] OF 1-654 AND 906-1422 (ISOFORM 1).
    Tissue: Small intestine and Testis.
  5. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 203-1422 (ISOFORM 2).
    Tissue: Brain.
  6. "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] OF 895-1422.
    Tissue: Brain and PNS.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1009-1422.
    Tissue: Melanoma.
  8. "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].

Entry informationi

Entry nameiFHOD3_HUMAN
AccessioniPrimary (citable) accession number: Q2V2M9
Secondary accession number(s): A8MQT4
, E5F5Q0, Q642I2, Q6ZRQ7, Q86TF9, Q8N3A5, Q9C0G8, Q9H604, Q9H6G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: July 13, 2010
Last modified: June 8, 2016
This is version 96 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, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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

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 one 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.