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Protein

Protein FAM76B

Gene

FAM76B

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

Functioni

GO - Molecular functioni

  1. NEDD8-specific protease activity Source: GO_Central

GO - Biological processi

  1. protein deneddylation Source: GO_Central
  2. proteolysis Source: GOC
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Protein FAM76B
Gene namesi
Name:FAM76B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:28492. FAM76B.

Subcellular locationi

  1. Nucleus speckle 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
  2. nuclear membrane Source: HPA
  3. nuclear speck Source: UniProtKB-SubCell
  4. nucleoplasm Source: HPA
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671838.

Polymorphism and mutation databases

BioMutaiFAM76B.
DMDMi296439347.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 339338Protein FAM76BPRO_0000245763Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei22 – 221Phosphoserine1 Publication
Modified residuei148 – 1481Phosphoserine1 Publication
Modified residuei193 – 1931Phosphoserine5 Publications
Cross-linki225 – 225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Post-translational modificationi

Isoform 2 is ubiquitinated at Lys-225.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ5HYJ3.
PaxDbiQ5HYJ3.
PRIDEiQ5HYJ3.

PTM databases

PhosphoSiteiQ5HYJ3.

Expressioni

Gene expression databases

BgeeiQ5HYJ3.
CleanExiHS_FAM76B.
ExpressionAtlasiQ5HYJ3. baseline and differential.
GenevestigatoriQ5HYJ3.

Organism-specific databases

HPAiHPA036608.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KRTAP10-11P604123EBI-751192,EBI-10217483
KRTAP10-5P603705EBI-751192,EBI-10172150
KRTAP10-7P604093EBI-751192,EBI-10172290
KRTAP10-8P604103EBI-751192,EBI-10171774
KRTAP10-9P604113EBI-751192,EBI-10172052
KRTAP4-7Q9BYR03EBI-751192,EBI-10302547
KRTAP5-9P263713EBI-751192,EBI-3958099
KRTAP9-2Q9BYQ43EBI-751192,EBI-1044640

Protein-protein interaction databases

BioGridi126816. 21 interactions.
IntActiQ5HYJ3. 12 interactions.
MINTiMINT-1472951.
STRINGi9606.ENSP00000351631.

Structurei

3D structure databases

ProteinModelPortaliQ5HYJ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili248 – 32881Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi151 – 16010Poly-Ser
Compositional biasi167 – 18721His-richAdd
BLAST
Compositional biasi171 – 18010Poly-His

Domaini

The polyhistidine repeat acts as a targeting signal to nuclear speckles.1 Publication

Sequence similaritiesi

Belongs to the FAM76 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG330390.
GeneTreeiENSGT00390000014462.
HOGENOMiHOG000231316.
HOVERGENiHBG080224.
InParanoidiQ5HYJ3.
OMAiNQRYPFE.
OrthoDBiEOG7TXKGS.
PhylomeDBiQ5HYJ3.
TreeFamiTF313644.

Family and domain databases

InterProiIPR029661. FAM76B.
[Graphical view]
PANTHERiPTHR22875:SF9. PTHR22875:SF9. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5HYJ3-1) [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
MAASALYACT KCTQRYPFEE LSQGQQLCKE CRIAHPIVKC TYCRSEFQQE
60 70 80 90 100
SKTNTICKKC AQNVKQFGTP KPCQYCNIIA AFIGTKCQRC TNSEKKYGPP
110 120 130 140 150
QTCEQCKQQC AFDRKEEGRR KVDGKLLCWL CTLSYKRVLQ KTKEQRKSLG
160 170 180 190 200
SSHSNSSSSS LTEKDQHHPK HHHHHHHHHH RHSSSHHKIS NLSPEEEQGL
210 220 230 240 250
WKQSHKSSAT IQNETPKKKP KLESKPSNGD SSSINQSADS GGTDNFVLIS
260 270 280 290 300
QLKEEVMSLK RLLQQRDQTI LEKDKKLTEL KADFQYQESN LRTKMNSMEK
310 320 330
AHKETVEQLQ AKNRELLKQV AALSKGKKFD KSGSILTSP
Length:339
Mass (Da):38,708
Last modified:May 18, 2010 - v3
Checksum:i4ED7FEE05F23790C
GO
Isoform 2 (identifier: Q5HYJ3-2) [UniParc]FASTAAdd to basket

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

Note: Ubiquitinated at position 225.Curated

Show »
Length:233
Mass (Da):26,771
Checksum:i3080A28B11A7C341
GO
Isoform 3 (identifier: Q5HYJ3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     231-339: SSSINQSADS...DKSGSILTSP → RCM

Note: No experimental confirmation available.

Show »
Length:233
Mass (Da):26,787
Checksum:i309BA28B11A7C341
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2281N → K in CAI46088 (PubMed:17974005).Curated
Sequence conflicti328 – 3281K → E in CAI46088 (PubMed:17974005).Curated
Sequence conflicti333 – 3331G → R in CAI46088 (PubMed:17974005).Curated
Isoform 2 (identifier: Q5HYJ3-2)
Sequence conflicti232 – 2321S → C in AAH26013 (PubMed:16554811).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei231 – 339109SSSIN…ILTSP → RCM in isoform 3. 1 PublicationVSP_057354Add
BLAST
Alternative sequencei231 – 2333SSS → RSM in isoform 2. 1 PublicationVSP_022679
Alternative sequencei234 – 339106Missing in isoform 2. 1 PublicationVSP_022680Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK313727 mRNA. Translation: BAG36469.1.
BX647586 mRNA. Translation: CAI46088.1.
AP001877 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW66962.1.
CH471065 Genomic DNA. Translation: EAW66963.1.
BC026013 mRNA. Translation: AAH26013.1.
BC028727 mRNA. Translation: AAH28727.1.
CCDSiCCDS41700.1. [Q5HYJ3-1]
RefSeqiNP_653265.3. NM_144664.4. [Q5HYJ3-1]
XP_005273834.1. XM_005273777.3. [Q5HYJ3-3]
UniGeneiHs.288304.

Genome annotation databases

EnsembliENST00000358780; ENSP00000351631; ENSG00000077458. [Q5HYJ3-1]
ENST00000398187; ENSP00000381248; ENSG00000077458. [Q5HYJ3-3]
ENST00000543641; ENSP00000444087; ENSG00000077458. [Q5HYJ3-3]
GeneIDi143684.
KEGGihsa:143684.
UCSCiuc001pfn.2. human. [Q5HYJ3-1]

Polymorphism and mutation databases

BioMutaiFAM76B.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK313727 mRNA. Translation: BAG36469.1.
BX647586 mRNA. Translation: CAI46088.1.
AP001877 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW66962.1.
CH471065 Genomic DNA. Translation: EAW66963.1.
BC026013 mRNA. Translation: AAH26013.1.
BC028727 mRNA. Translation: AAH28727.1.
CCDSiCCDS41700.1. [Q5HYJ3-1]
RefSeqiNP_653265.3. NM_144664.4. [Q5HYJ3-1]
XP_005273834.1. XM_005273777.3. [Q5HYJ3-3]
UniGeneiHs.288304.

3D structure databases

ProteinModelPortaliQ5HYJ3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126816. 21 interactions.
IntActiQ5HYJ3. 12 interactions.
MINTiMINT-1472951.
STRINGi9606.ENSP00000351631.

PTM databases

PhosphoSiteiQ5HYJ3.

Polymorphism and mutation databases

BioMutaiFAM76B.
DMDMi296439347.

Proteomic databases

MaxQBiQ5HYJ3.
PaxDbiQ5HYJ3.
PRIDEiQ5HYJ3.

Protocols and materials databases

DNASUi143684.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358780; ENSP00000351631; ENSG00000077458. [Q5HYJ3-1]
ENST00000398187; ENSP00000381248; ENSG00000077458. [Q5HYJ3-3]
ENST00000543641; ENSP00000444087; ENSG00000077458. [Q5HYJ3-3]
GeneIDi143684.
KEGGihsa:143684.
UCSCiuc001pfn.2. human. [Q5HYJ3-1]

Organism-specific databases

CTDi143684.
GeneCardsiGC11M095502.
H-InvDBHIX0010043.
HGNCiHGNC:28492. FAM76B.
HPAiHPA036608.
neXtProtiNX_Q5HYJ3.
PharmGKBiPA142671838.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG330390.
GeneTreeiENSGT00390000014462.
HOGENOMiHOG000231316.
HOVERGENiHBG080224.
InParanoidiQ5HYJ3.
OMAiNQRYPFE.
OrthoDBiEOG7TXKGS.
PhylomeDBiQ5HYJ3.
TreeFamiTF313644.

Miscellaneous databases

GeneWikiiFAM76B.
GenomeRNAii143684.
NextBioi35467867.
PROiQ5HYJ3.

Gene expression databases

BgeeiQ5HYJ3.
CleanExiHS_FAM76B.
ExpressionAtlasiQ5HYJ3. baseline and differential.
GenevestigatoriQ5HYJ3.

Family and domain databases

InterProiIPR029661. FAM76B.
[Graphical view]
PANTHERiPTHR22875:SF9. PTHR22875:SF9. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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).
    Tissue: Brain.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Fetal skin.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "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.
  7. "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.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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.
  12. "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.
  13. "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.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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].
  16. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFA76B_HUMAN
AccessioniPrimary (citable) accession number: Q5HYJ3
Secondary accession number(s): B2R9C2, Q6PIU3, Q8TC53
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: May 18, 2010
Last modified: April 29, 2015
This is version 83 of the entry and version 3 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 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.