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Q5HYJ3 (FA76B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein FAM76B
Gene names
Name:FAM76B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Nucleus speckle Ref.9.

Domain

The polyhistidine repeat acts as a targeting signal to nuclear speckles (Ref.9).

Post-translational modification

Isoform 2 is ubiquitinated at Lys-225.

Sequence similarities

Belongs to the FAM76 family.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentnuclear membrane

Inferred from direct assay. Source: HPA

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: HPA

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5HYJ3-1)

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.
Isoform 2 (identifier: Q5HYJ3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     231-233: SSS → RSM
     234-339: Missing.
Note: Ubiquitinated at position 225.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 339338Protein FAM76B
PRO_0000245763

Regions

Coiled coil248 – 32881 Potential
Compositional bias151 – 16010Poly-Ser
Compositional bias167 – 18721His-rich
Compositional bias171 – 18010Poly-His

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.14 Ref.15
Modified residue221Phosphoserine Ref.6
Modified residue1481Phosphoserine Ref.11
Modified residue1931Phosphoserine Ref.4 Ref.7 Ref.10 Ref.11 Ref.13
Cross-link225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.5

Natural variations

Alternative sequence231 – 2333SSS → RSM in isoform 2.
VSP_022679
Alternative sequence234 – 339106Missing in isoform 2.
VSP_022680

Experimental info

Sequence conflict2281N → K in CAI46088. Ref.1
Sequence conflict3281K → E in CAI46088. Ref.1
Sequence conflict3331G → R in CAI46088. Ref.1
Isoform 2:
Sequence conflict2321S → C in AAH26013. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 4ED7FEE05F23790C

FASTA33938,708
        10         20         30         40         50         60 
MAASALYACT KCTQRYPFEE LSQGQQLCKE CRIAHPIVKC TYCRSEFQQE SKTNTICKKC 

        70         80         90        100        110        120 
AQNVKQFGTP KPCQYCNIIA AFIGTKCQRC TNSEKKYGPP QTCEQCKQQC AFDRKEEGRR 

       130        140        150        160        170        180 
KVDGKLLCWL CTLSYKRVLQ KTKEQRKSLG SSHSNSSSSS LTEKDQHHPK HHHHHHHHHH 

       190        200        210        220        230        240 
RHSSSHHKIS NLSPEEEQGL WKQSHKSSAT IQNETPKKKP KLESKPSNGD SSSINQSADS 

       250        260        270        280        290        300 
GGTDNFVLIS QLKEEVMSLK RLLQQRDQTI LEKDKKLTEL KADFQYQESN LRTKMNSMEK 

       310        320        330 
AHKETVEQLQ AKNRELLKQV AALSKGKKFD KSGSILTSP 

« Hide

Isoform 2 [UniParc].

Checksum: 3080A28B11A7C341
Show »

FASTA23326,771

References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Fetal skin.
[2]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 2).
Tissue: Testis.
[4]"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-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-225 (ISOFORM 2).
Tissue: Lung adenocarcinoma.
[6]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[9]"Genome-wide analysis of histidine repeats reveals their role in the localization of human proteins to the nuclear speckles compartment."
Salichs E., Ledda A., Mularoni L., Alba M.M., de la Luna S.
PLoS Genet. 5:E1000397-E1000397(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX647586 mRNA. Translation: CAI46088.1.
AP001877 Genomic DNA. No translation available.
BC026013 mRNA. Translation: AAH26013.1.
BC028727 mRNA. Translation: AAH28727.1.
RefSeqNP_653265.3. NM_144664.4.
XP_005273834.1. XM_005273777.2.
UniGeneHs.288304.

3D structure databases

ProteinModelPortalQ5HYJ3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126816. 5 interactions.
IntActQ5HYJ3. 4 interactions.
MINTMINT-1472951.
STRING9606.ENSP00000351631.

PTM databases

PhosphoSiteQ5HYJ3.

Polymorphism databases

DMDM296439347.

Proteomic databases

PaxDbQ5HYJ3.
PRIDEQ5HYJ3.

Protocols and materials databases

DNASU143684.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358780; ENSP00000351631; ENSG00000077458. [Q5HYJ3-1]
GeneID143684.
KEGGhsa:143684.
UCSCuc001pfn.2. human. [Q5HYJ3-1]

Organism-specific databases

CTD143684.
GeneCardsGC11M095502.
H-InvDBHIX0010043.
HGNCHGNC:28492. FAM76B.
HPAHPA036608.
neXtProtNX_Q5HYJ3.
PharmGKBPA142671838.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG330390.
HOGENOMHOG000231316.
HOVERGENHBG080224.
InParanoidQ5HYJ3.
OMANQRYPFE.
OrthoDBEOG7TXKGS.
PhylomeDBQ5HYJ3.
TreeFamTF313644.

Gene expression databases

ArrayExpressQ5HYJ3.
BgeeQ5HYJ3.
CleanExHS_FAM76B.
GenevestigatorQ5HYJ3.

Family and domain databases

ProtoNetSearch...

Other

GeneWikiFAM76B.
GenomeRNAi143684.
NextBio84772.
PROQ5HYJ3.

Entry information

Entry nameFA76B_HUMAN
AccessionPrimary (citable) accession number: Q5HYJ3
Secondary accession number(s): Q6PIU3, Q8TC53
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 73 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM