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Q8NEZ5

- FBX22_HUMAN

UniProt

Q8NEZ5 - FBX22_HUMAN

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Protein

F-box only protein 22

Gene
FBXO22, FBX22
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. Promotes the proteasome-dependent degradation of key sarcomeric proteins, such as alpha-actinin (ACTN2) and filamin-C (FLNC), essential for maintenance of normal contractile function.1 Publication

GO - Molecular functioni

  1. ubiquitin-protein transferase activity Source: ProtInc

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. cellular response to starvation Source: Ensembl
  3. nucleocytoplasmic transport Source: Ensembl
  4. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  5. positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: Ensembl
  6. protein polyubiquitination Source: Ensembl
  7. regulation of skeletal muscle fiber development Source: Ensembl
  8. ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
F-box only protein 22
Alternative name(s):
F-box protein FBX22p44
Gene namesi
Name:FBXO22
Synonyms:FBX22
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:13593. FBXO22.

Subcellular locationi

CytoplasmmyofibrilsarcomereZ line By similarity

GO - Cellular componenti

  1. nucleus Source: Ensembl
  2. Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28035.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403F-box only protein 22PRO_0000119906Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei194 – 1941N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8NEZ5.
PaxDbiQ8NEZ5.
PRIDEiQ8NEZ5.

PTM databases

PhosphoSiteiQ8NEZ5.

Expressioni

Tissue specificityi

Predominantly expressed in liver, also enriched in cardiac muscle.1 Publication

Gene expression databases

ArrayExpressiQ8NEZ5.
BgeeiQ8NEZ5.
CleanExiHS_FBXO22.
GenevestigatoriQ8NEZ5.

Organism-specific databases

HPAiHPA003165.
HPA050178.

Interactioni

Subunit structurei

Directly interacts with SKP1 and CUL1.1 Publication

Protein-protein interaction databases

BioGridi117649. 7 interactions.
IntActiQ8NEZ5. 2 interactions.
STRINGi9606.ENSP00000307833.

Structurei

3D structure databases

ProteinModelPortaliQ8NEZ5.
SMRiQ8NEZ5. Positions 24-58.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 6747F-boxAdd
BLAST

Sequence similaritiesi

Contains 1 F-box domain.

Phylogenomic databases

eggNOGiNOG26261.
HOGENOMiHOG000285967.
HOVERGENiHBG051570.
InParanoidiQ8NEZ5.
KOiK10302.
OMAiCCKVGAS.
OrthoDBiEOG72G17J.
PhylomeDBiQ8NEZ5.
TreeFamiTF328809.

Family and domain databases

InterProiIPR001810. F-box_dom.
IPR019494. FIST_C_domain.
[Graphical view]
PfamiPF00646. F-box. 1 hit.
PF10442. FIST_C. 1 hit.
[Graphical view]
SMARTiSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMiSSF81383. SSF81383. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8NEZ5-1) [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

MEPVGCCGEC RGSSVDPRST FVLSNLAEVV ERVLTFLPAK ALLRVACVCR    50
LWRECVRRVL RTHRSVTWIS AGLAEAGHLE GHCLVRVVAE ELENVRILPH 100
TVLYMADSET FISLEECRGH KRARKRTSME TALALEKLFP KQCQVLGIVT 150
PGIVVTPMGS GSNRPQEIEI GESGFALLFP QIEGIKIQPF HFIKDPKNLT 200
LERHQLTEVG LLDNPELRVV LVFGYNCCKV GASNYLQQVV STFSDMNIIL 250
AGGQVDNLSS LTSEKNPLDI DASGVVGLSF SGHRIQSATV LLNEDVSDEK 300
TAEAAMQRLK AANIPEHNTI GFMFACVGRG FQYYRAKGNV EADAFRKFFP 350
SVPLFGFFGN GEIGCDRIVT GNFILRKCNE VKDDDLFHSY TTIMALIHLG 400
SSK 403
Length:403
Mass (Da):44,508
Last modified:October 1, 2002 - v1
Checksum:iD96712BAA1149D8D
GO
Isoform 2 (identifier: Q8NEZ5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     47-403: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:46
Mass (Da):4,922
Checksum:i1D49258F07775FA2
GO
Isoform 3 (identifier: Q8NEZ5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     266-276: NPLDIDASGVV → YVLCASDFVCE
     277-403: Missing.

Note: No experimental confirmation available.

Show »
Length:276
Mass (Da):30,589
Checksum:i0E9B0CE3E208358B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei47 – 403357Missing in isoform 2. VSP_041821Add
BLAST
Alternative sequencei266 – 27611NPLDIDASGVV → YVLCASDFVCE in isoform 3. VSP_013058Add
BLAST
Alternative sequencei277 – 403127Missing in isoform 3. VSP_013059Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 118VGCCGECR → AGACGGP in AAF04523. 1 Publication
Sequence conflicti349 – 3491F → L in AAH32540. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY005144 mRNA. Translation: AAF89095.1.
AK024048 mRNA. Translation: BAB14798.1.
AC027104 Genomic DNA. No translation available.
BC032540 mRNA. Translation: AAH32540.1.
BC020204 mRNA. Translation: AAH20204.2.
BC039024 mRNA. Translation: AAH39024.1. Sequence problems.
BC041691 mRNA. Translation: AAH41691.1.
AF174602 Genomic DNA. Translation: AAF04523.1.
CCDSiCCDS10287.1. [Q8NEZ5-1]
CCDS45310.1. [Q8NEZ5-3]
RefSeqiNP_036302.1. NM_012170.3. [Q8NEZ5-3]
NP_671717.1. NM_147188.2. [Q8NEZ5-1]
UniGeneiHs.591115.

Genome annotation databases

EnsembliENST00000308275; ENSP00000307833; ENSG00000167196. [Q8NEZ5-1]
ENST00000453211; ENSP00000396442; ENSG00000167196. [Q8NEZ5-3]
ENST00000540507; ENSP00000439270; ENSG00000167196.
ENST00000569022; ENSP00000457531; ENSG00000167196. [Q8NEZ5-2]
GeneIDi26263.
KEGGihsa:26263.
UCSCiuc002bbj.2. human. [Q8NEZ5-3]
uc002bbk.3. human. [Q8NEZ5-1]

Polymorphism databases

DMDMi30580428.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY005144 mRNA. Translation: AAF89095.1 .
AK024048 mRNA. Translation: BAB14798.1 .
AC027104 Genomic DNA. No translation available.
BC032540 mRNA. Translation: AAH32540.1 .
BC020204 mRNA. Translation: AAH20204.2 .
BC039024 mRNA. Translation: AAH39024.1 . Sequence problems.
BC041691 mRNA. Translation: AAH41691.1 .
AF174602 Genomic DNA. Translation: AAF04523.1 .
CCDSi CCDS10287.1. [Q8NEZ5-1 ]
CCDS45310.1. [Q8NEZ5-3 ]
RefSeqi NP_036302.1. NM_012170.3. [Q8NEZ5-3 ]
NP_671717.1. NM_147188.2. [Q8NEZ5-1 ]
UniGenei Hs.591115.

3D structure databases

ProteinModelPortali Q8NEZ5.
SMRi Q8NEZ5. Positions 24-58.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117649. 7 interactions.
IntActi Q8NEZ5. 2 interactions.
STRINGi 9606.ENSP00000307833.

PTM databases

PhosphoSitei Q8NEZ5.

Polymorphism databases

DMDMi 30580428.

Proteomic databases

MaxQBi Q8NEZ5.
PaxDbi Q8NEZ5.
PRIDEi Q8NEZ5.

Protocols and materials databases

DNASUi 26263.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308275 ; ENSP00000307833 ; ENSG00000167196 . [Q8NEZ5-1 ]
ENST00000453211 ; ENSP00000396442 ; ENSG00000167196 . [Q8NEZ5-3 ]
ENST00000540507 ; ENSP00000439270 ; ENSG00000167196 .
ENST00000569022 ; ENSP00000457531 ; ENSG00000167196 . [Q8NEZ5-2 ]
GeneIDi 26263.
KEGGi hsa:26263.
UCSCi uc002bbj.2. human. [Q8NEZ5-3 ]
uc002bbk.3. human. [Q8NEZ5-1 ]

Organism-specific databases

CTDi 26263.
GeneCardsi GC15P076196.
HGNCi HGNC:13593. FBXO22.
HPAi HPA003165.
HPA050178.
MIMi 609096. gene.
neXtProti NX_Q8NEZ5.
PharmGKBi PA28035.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG26261.
HOGENOMi HOG000285967.
HOVERGENi HBG051570.
InParanoidi Q8NEZ5.
KOi K10302.
OMAi CCKVGAS.
OrthoDBi EOG72G17J.
PhylomeDBi Q8NEZ5.
TreeFami TF328809.

Miscellaneous databases

GenomeRNAii 26263.
NextBioi 48531.
PROi Q8NEZ5.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8NEZ5.
Bgeei Q8NEZ5.
CleanExi HS_FBXO22.
Genevestigatori Q8NEZ5.

Family and domain databases

InterProi IPR001810. F-box_dom.
IPR019494. FIST_C_domain.
[Graphical view ]
Pfami PF00646. F-box. 1 hit.
PF10442. FIST_C. 1 hit.
[Graphical view ]
SMARTi SM00256. FBOX. 1 hit.
[Graphical view ]
SUPFAMi SSF81383. SSF81383. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "FBX22p44: a novel human F-box protein predominantly expressed in the liver."
    Tan P., Pan Z.-Q.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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 3).
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORMS 1 AND 2).
    Tissue: Brain, Colon and Lung.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
  6. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "F-box and leucine-rich repeat protein 22 is a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo."
    Spaich S., Will R.D., Just S., Spaich S., Kuhn C., Frank D., Berger I.M., Wiemann S., Korn B., Koegl M., Backs J., Katus H.A., Rottbauer W., Frey N.
    Circ. Res. 111:1504-1516(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH SKP1 AND CUL1.
  10. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFBX22_HUMAN
AccessioniPrimary (citable) accession number: Q8NEZ5
Secondary accession number(s): Q0D2P8
, Q6PIL5, Q8IXW3, Q9H824, Q9UKC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 9, 2003
Last sequence update: October 1, 2002
Last modified: September 3, 2014
This is version 100 of the entry and version 1 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 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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