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Q9H2G9 (GO45_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Golgin-45
Alternative name(s):
Basic leucine zipper nuclear factor 1
JEM-1
p45 basic leucine-zipper nuclear factor
Gene names
Name:BLZF1
Synonyms:JEM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length400 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for normal Golgi structure and for protein transport from the endoplasmic reticulum (ER) through the Golgi apparatus to the cell surface.

Subunit structure

Interacts with GORASP2 and with the GTP-bound form of RAB2, but not with other Golgi Rab proteins. GORASP2 and BLZF1 form a RAB2 effector complex on medial Golgi. Ref.3

Subcellular location

Golgi apparatus lumen Ref.1 Ref.2 Ref.3.

Isoform 1: Nucleus Ref.1 Ref.2 Ref.3.

Isoform 2: Cytoplasm Ref.1 Ref.2 Ref.3.

Tissue specificity

Ubiquitous. Also found in cell lines derived from several hematopoietic pathologies, such as T-cell leukemia, pro-B, pre-B, myeloma, and plasmacytoma cell lines, but not in Burkitt lymphoma cells. Ref.1 Ref.2 Ref.3

Induction

Up-regulated by retinoids. Ref.1 Ref.2

Domain

The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2. Ref.9

Post-translational modification

ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.

Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation. Ref.9

Caution

Because of the presence of a potential basic motif and leucine-zipper domain, Ref.1 and Ref.2 have thought that BLZF1 is a potential transcription factor. They found it localized in the nucleus, except isoform 2, which was cytoplasmic. However, homology at several typical position for basic or hydrophobic residues is missing.

Ontologies

Keywords
   Biological processER-Golgi transport
Protein transport
Transport
   Cellular componentCytoplasm
Golgi apparatus
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMADP-ribosylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi organization

Inferred from direct assay Ref.3. Source: MGI

Golgi to plasma membrane protein transport

Inferred from direct assay Ref.3. Source: MGI

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

mitotic cell cycle

Traceable author statement. Source: Reactome

regulation of cell growth

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

cytoplasm

Non-traceable author statement Ref.2. Source: UniProtKB

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionDNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.9. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Non-traceable author statement Ref.1. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H2G9-1)

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: Q9H2G9-2)

Also known as: JEM1s;

The sequence of this isoform differs from the canonical sequence as follows:
     158-174: NRELKKLLVASVGDDLQ → RRALIDKMSTTLYVWTF
     175-400: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 400400Golgin-45
PRO_0000087539

Regions

Region394 – 4007Essential for the interaction with GORASP2
Coiled coil120 – 21394 Potential
Motif18 – 225Tankyrase-binding motif

Amino acid modifications

Modified residue491Phosphoserine Ref.8
Modified residue3481Phosphothreonine Ref.7
Modified residue3531Phosphoserine Ref.7

Natural variations

Alternative sequence158 – 17417NRELK…GDDLQ → RRALIDKMSTTLYVWTF in isoform 2.
VSP_011186
Alternative sequence175 – 400226Missing in isoform 2.
VSP_011187
Natural variant401Q → R.
Corresponds to variant rs1028180 [ dbSNP | Ensembl ].
VAR_028142
Natural variant1961R → Q.
Corresponds to variant rs1064274 [ dbSNP | Ensembl ].
VAR_028143

Experimental info

Sequence conflict3681A → V in AAG37822. Ref.2

Sequences

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

Last modified October 17, 2006. Version 2.
Checksum: F3F9DA9B13DF45B5

FASTA40044,910
        10         20         30         40         50         60 
MTTKNLETKV TVTSSPIRGA GDGMETEEPP KSVEVTSGVQ SRKHHSLQSP WKKAVPSESP 

        70         80         90        100        110        120 
GVLQLGKMLT EKAMEVKAVR ILVPKAAITH DIPNKNTKVK SLGHHKGEFL GQSEGVIEPN 

       130        140        150        160        170        180 
KELSEVKNVL EKLKNSERRL LQDKEGLSNQ LRVQTEVNRE LKKLLVASVG DDLQYHFERL 

       190        200        210        220        230        240 
AREKNQLILE NEALGRNTAQ LSEQLERMSI QCDVWRSKFL ASRVMADELT NSRAALQRQN 

       250        260        270        280        290        300 
RDAHGAIQDL LSEREQFRQE MIATQKLLEE LLVSLQWGRE QTYSPSVQPH STAELALTNH 

       310        320        330        340        350        360 
KLAKAVNSHL LGNVGINNQK KIPSTVEFCS TPAEKMAETV LRILDPVTCK ESSPDNPFFE 

       370        380        390        400 
SSPTTLLATK KNIGRFHPYT RYENITFNCC NHCRGELIAL 

« Hide

Isoform 2 (JEM1s) [UniParc].

Checksum: 42524E04C956A3AB
Show »

FASTA17419,362

References

« Hide 'large scale' references
[1]"JEM-1, a novel gene encoding a leucine-zipper nuclear factor upregulated during retinoid-induced maturation of NB4 promyelocytic leukaemia."
Duprez E., Tong J.-H., Derre J., Chen S.-J., Berger R., Chen Z., Lanotte M.
Oncogene 14:1563-1570(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[2]"Genomic organization of the JEM-1 (BLZF1) gene on human chromosome 1q24: molecular cloning and analysis of its promoter region."
Tong J.-H., Fant X., Benoit G., Chen S.-J., Chen Z., Lanotte M.
Genomics 69:380-390(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[3]"A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic."
Short B., Preisinger C., Koerner R., Kopajtich R., Byron O., Barr F.A.
J. Cell Biol. 155:877-883(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GORASP2 AND THE GTP FORM OF RAB2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Testis.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 1).
Tissue: Liver.
[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 THR-348 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-49, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling."
Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A., Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M., Porter J.A., Huang S.M., Cong F.
Nat. Cell Biol. 13:623-629(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ADP-RIBOSYLATION, UBIQUITINATION, DOMAIN TANKYRASE-BINDING MOTIF.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U79751 mRNA. Translation: AAB63110.1.
AF288161 mRNA. Translation: AAG37835.1.
AF273875, AF288162 Genomic DNA. Translation: AAG37821.1.
AF272386 expand/collapse EMBL AC list , AF272387, AF272388, AF273875, AF288162 Genomic DNA. Translation: AAG37822.1.
AL356852 Genomic DNA. Translation: CAI19240.1.
AL356852 Genomic DNA. Translation: CAI19242.1.
CH471067 Genomic DNA. Translation: EAW90837.1.
BC020716 mRNA. Translation: AAH20716.1.
CCDSCCDS1278.1. [Q9H2G9-1]
RefSeqNP_003657.1. NM_003666.2. [Q9H2G9-1]
UniGeneHs.130746.

3D structure databases

ProteinModelPortalQ9H2G9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114118. 12 interactions.
IntActQ9H2G9. 8 interactions.
MINTMINT-4830863.
STRING9606.ENSP00000327541.

PTM databases

PhosphoSiteQ9H2G9.

Polymorphism databases

DMDM116242501.

Proteomic databases

MaxQBQ9H2G9.
PaxDbQ9H2G9.
PRIDEQ9H2G9.

Protocols and materials databases

DNASU8548.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000329281; ENSP00000327541; ENSG00000117475. [Q9H2G9-1]
ENST00000367807; ENSP00000356781; ENSG00000117475. [Q9H2G9-2]
ENST00000367808; ENSP00000356782; ENSG00000117475. [Q9H2G9-1]
GeneID8548.
KEGGhsa:8548.
UCSCuc001gfw.3. human. [Q9H2G9-2]
uc001gfx.2. human. [Q9H2G9-1]

Organism-specific databases

CTD8548.
GeneCardsGC01P169337.
HGNCHGNC:1065. BLZF1.
HPAHPA025703.
HPA027331.
MIM608692. gene.
neXtProtNX_Q9H2G9.
PharmGKBPA25375.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279660.
HOGENOMHOG000088649.
HOVERGENHBG051750.
InParanoidQ9H2G9.
OMAQIDEQNE.
OrthoDBEOG7P5T13.
PhylomeDBQ9H2G9.
TreeFamTF317238.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ9H2G9.
BgeeQ9H2G9.
CleanExHS_BLZF1.
GenevestigatorQ9H2G9.

Family and domain databases

InterProIPR027095. Golgin-45.
IPR013183. Hsk3_like.
[Graphical view]
PANTHERPTHR13066. PTHR13066. 1 hit.
PfamPF08227. DASH_Hsk3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiBLZF1.
GenomeRNAi8548.
NextBio32028.
PROQ9H2G9.
SOURCESearch...

Entry information

Entry nameGO45_HUMAN
AccessionPrimary (citable) accession number: Q9H2G9
Secondary accession number(s): O15298 expand/collapse secondary AC list , Q5T531, Q5T533, Q9GZX4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 100 of the entry and version 2 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM