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Protein

Golgin-45

Gene

BLZF1

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

Functioni

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

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: ProtInc
  • Golgi organization Source: MGI
  • Golgi to plasma membrane protein transport Source: MGI
  • mitotic cell cycle Source: Reactome
  • regulation of cell growth Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

Names & Taxonomyi

Protein namesi
Recommended name:
Golgin-45
Alternative name(s):
Basic leucine zipper nuclear factor 1
JEM-1
p45 basic leucine-zipper nuclear factor
Gene namesi
Name:BLZF1
Synonyms:JEM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:1065. BLZF1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • Golgi lumen Source: UniProtKB-SubCell
  • Golgi membrane Source: Reactome
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25375.

Polymorphism and mutation databases

BioMutaiBLZF1.
DMDMi116242501.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400Golgin-45PRO_0000087539Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei49 – 491Phosphoserine1 Publication
Modified residuei348 – 3481Phosphothreonine1 Publication
Modified residuei353 – 3531Phosphoserine1 Publication

Post-translational modificationi

ADP-ribosylated by tankyrase TNKS and TNKS2. Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.1 Publication
Ubiquitinated by RNF146 when poly-ADP-ribosylated, leading to its degradation.1 Publication

Keywords - PTMi

ADP-ribosylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9H2G9.
PaxDbiQ9H2G9.
PRIDEiQ9H2G9.

PTM databases

PhosphoSiteiQ9H2G9.

Expressioni

Tissue specificityi

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.3 Publications

Inductioni

Up-regulated by retinoids.2 Publications

Gene expression databases

BgeeiQ9H2G9.
CleanExiHS_BLZF1.
ExpressionAtlasiQ9H2G9. baseline and differential.
GenevisibleiQ9H2G9. HS.

Organism-specific databases

HPAiHPA025703.
HPA027331.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AKAP9Q99996-23EBI-2548012,EBI-9641546
AMOTL2Q9Y2J4-43EBI-2548012,EBI-10187270
BCL6P411823EBI-2548012,EBI-765407
BEX2Q9BXY83EBI-2548012,EBI-745073
CARD9Q9H2573EBI-2548012,EBI-751319
CHCHD3Q9NX633EBI-2548012,EBI-743375
CINPQ9BW663EBI-2548012,EBI-739784
FBF1Q8TES7-63EBI-2548012,EBI-10244131
FHL2Q141923EBI-2548012,EBI-701903
FRMD6Q96NE93EBI-2548012,EBI-741729
GEMP550403EBI-2548012,EBI-744104
HOXA1P496393EBI-2548012,EBI-740785
IQUBQ8NA543EBI-2548012,EBI-10220600
KLHL38Q2WGJ63EBI-2548012,EBI-6426443
LMO1P258003EBI-2548012,EBI-8639312
LMO2P257913EBI-2548012,EBI-739696
OAZ3Q9UMX23EBI-2548012,EBI-10281601
PRKAB2O437414EBI-2548012,EBI-1053424
PSMA1P257863EBI-2548012,EBI-359352
RAB2AP610193EBI-2548012,EBI-752037
RAB2BQ8WUD13EBI-2548012,EBI-5542466
RAB39AQ149643EBI-2548012,EBI-3048577
RHOJQ9H4E53EBI-2548012,EBI-6285694
SCNM1Q9BWG63EBI-2548012,EBI-748391
SMAD3P840223EBI-2548012,EBI-347161
SSX2BQ163853EBI-2548012,EBI-2210673
TBC1D7Q9P0N93EBI-2548012,EBI-3258000
TRAPPC2LQ9UL333EBI-2548012,EBI-747601
TSC22D4Q8IV543EBI-2548012,EBI-10261521
TXNDC5Q86UY03EBI-2548012,EBI-2825190
VPS28Q548N13EBI-2548012,EBI-10243107
ZBTB24O431673EBI-2548012,EBI-744471
ZGPATQ8N5A53EBI-2548012,EBI-3439227
ZGPATQ8N5A5-23EBI-2548012,EBI-10183064
ZNF410Q86VK43EBI-2548012,EBI-720304

Protein-protein interaction databases

BioGridi114118. 53 interactions.
IntActiQ9H2G9. 42 interactions.
MINTiMINT-4830863.
STRINGi9606.ENSP00000327541.

Structurei

3D structure databases

ProteinModelPortaliQ9H2G9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni394 – 4007Essential for the interaction with GORASP2

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili120 – 21394Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi18 – 225Tankyrase-binding motif

Domaini

The tankyrase-binding motif (also named TBD) is required for interaction with tankyrase TNKS and TNKS2.1 Publication

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG279660.
GeneTreeiENSGT00390000009400.
HOGENOMiHOG000088649.
HOVERGENiHBG051750.
InParanoidiQ9H2G9.
OMAiQRQNRDA.
OrthoDBiEOG7P5T13.
PhylomeDBiQ9H2G9.
TreeFamiTF317238.

Family and domain databases

InterProiIPR027095. Golgin-45.
IPR013183. Hsk3_like.
[Graphical view]
PANTHERiPTHR13066. PTHR13066. 1 hit.
PfamiPF08227. DASH_Hsk3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H2G9-1) [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
MTTKNLETKV TVTSSPIRGA GDGMETEEPP KSVEVTSGVQ SRKHHSLQSP
60 70 80 90 100
WKKAVPSESP GVLQLGKMLT EKAMEVKAVR ILVPKAAITH DIPNKNTKVK
110 120 130 140 150
SLGHHKGEFL GQSEGVIEPN KELSEVKNVL EKLKNSERRL LQDKEGLSNQ
160 170 180 190 200
LRVQTEVNRE LKKLLVASVG DDLQYHFERL AREKNQLILE NEALGRNTAQ
210 220 230 240 250
LSEQLERMSI QCDVWRSKFL ASRVMADELT NSRAALQRQN RDAHGAIQDL
260 270 280 290 300
LSEREQFRQE MIATQKLLEE LLVSLQWGRE QTYSPSVQPH STAELALTNH
310 320 330 340 350
KLAKAVNSHL LGNVGINNQK KIPSTVEFCS TPAEKMAETV LRILDPVTCK
360 370 380 390 400
ESSPDNPFFE SSPTTLLATK KNIGRFHPYT RYENITFNCC NHCRGELIAL
Length:400
Mass (Da):44,910
Last modified:October 17, 2006 - v2
Checksum:iF3F9DA9B13DF45B5
GO
Isoform 2 (identifier: Q9H2G9-2) [UniParc]FASTAAdd to basket

Also known as: JEM1s

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

Show »
Length:174
Mass (Da):19,362
Checksum:i42524E04C956A3AB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti368 – 3681A → V in AAG37822 (PubMed:11056056).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401Q → R.
Corresponds to variant rs1028180 [ dbSNP | Ensembl ].
VAR_028142
Natural varianti196 – 1961R → Q.
Corresponds to variant rs1064274 [ dbSNP | Ensembl ].
VAR_028143

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei158 – 17417NRELK…GDDLQ → RRALIDKMSTTLYVWTF in isoform 2. 1 PublicationVSP_011186Add
BLAST
Alternative sequencei175 – 400226Missing in isoform 2. 1 PublicationVSP_011187Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U79751 mRNA. Translation: AAB63110.1.
AF288161 mRNA. Translation: AAG37835.1.
AF273875, AF288162 Genomic DNA. Translation: AAG37821.1.
AF272386
, 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.
CCDSiCCDS1278.1. [Q9H2G9-1]
RefSeqiNP_003657.1. NM_003666.2. [Q9H2G9-1]
UniGeneiHs.130746.

Genome annotation databases

EnsembliENST00000329281; ENSP00000327541; ENSG00000117475. [Q9H2G9-1]
ENST00000367807; ENSP00000356781; ENSG00000117475. [Q9H2G9-2]
ENST00000367808; ENSP00000356782; ENSG00000117475. [Q9H2G9-1]
GeneIDi8548.
KEGGihsa:8548.
UCSCiuc001gfw.3. human. [Q9H2G9-2]
uc001gfx.2. human. [Q9H2G9-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U79751 mRNA. Translation: AAB63110.1.
AF288161 mRNA. Translation: AAG37835.1.
AF273875, AF288162 Genomic DNA. Translation: AAG37821.1.
AF272386
, 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.
CCDSiCCDS1278.1. [Q9H2G9-1]
RefSeqiNP_003657.1. NM_003666.2. [Q9H2G9-1]
UniGeneiHs.130746.

3D structure databases

ProteinModelPortaliQ9H2G9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114118. 53 interactions.
IntActiQ9H2G9. 42 interactions.
MINTiMINT-4830863.
STRINGi9606.ENSP00000327541.

PTM databases

PhosphoSiteiQ9H2G9.

Polymorphism and mutation databases

BioMutaiBLZF1.
DMDMi116242501.

Proteomic databases

MaxQBiQ9H2G9.
PaxDbiQ9H2G9.
PRIDEiQ9H2G9.

Protocols and materials databases

DNASUi8548.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000329281; ENSP00000327541; ENSG00000117475. [Q9H2G9-1]
ENST00000367807; ENSP00000356781; ENSG00000117475. [Q9H2G9-2]
ENST00000367808; ENSP00000356782; ENSG00000117475. [Q9H2G9-1]
GeneIDi8548.
KEGGihsa:8548.
UCSCiuc001gfw.3. human. [Q9H2G9-2]
uc001gfx.2. human. [Q9H2G9-1]

Organism-specific databases

CTDi8548.
GeneCardsiGC01P169337.
HGNCiHGNC:1065. BLZF1.
HPAiHPA025703.
HPA027331.
MIMi608692. gene.
neXtProtiNX_Q9H2G9.
PharmGKBiPA25375.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG279660.
GeneTreeiENSGT00390000009400.
HOGENOMiHOG000088649.
HOVERGENiHBG051750.
InParanoidiQ9H2G9.
OMAiQRQNRDA.
OrthoDBiEOG7P5T13.
PhylomeDBiQ9H2G9.
TreeFamiTF317238.

Enzyme and pathway databases

ReactomeiREACT_1100. Golgi Cisternae Pericentriolar Stack Reorganization.

Miscellaneous databases

GeneWikiiBLZF1.
GenomeRNAii8548.
NextBioi32028.
PROiQ9H2G9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H2G9.
CleanExiHS_BLZF1.
ExpressionAtlasiQ9H2G9. baseline and differential.
GenevisibleiQ9H2G9. HS.

Family and domain databases

InterProiIPR027095. Golgin-45.
IPR013183. Hsk3_like.
[Graphical view]
PANTHERiPTHR13066. PTHR13066. 1 hit.
PfamiPF08227. DASH_Hsk3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiGO45_HUMAN
AccessioniPrimary (citable) accession number: Q9H2G9
Secondary accession number(s): O15298
, Q5T531, Q5T533, Q9GZX4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 17, 2006
Last modified: June 24, 2015
This is version 107 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

Caution

Because of the presence of a potential basic motif and leucine-zipper domain, PubMed:9129147 and PubMed:11056056 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.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

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.