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Protein

Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1

Gene

GBF1

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

Functioni

Promotes guanine-nucleotide exchange on ARF5. Promotes the activation of ARF5 through replacement of GDP with GTP (By similarity).By similarity

Enzyme regulationi

Inhibited by brefeldin A.By similarity

GO - Molecular functioni

  1. ARF guanyl-nucleotide exchange factor activity Source: GO_Central

GO - Biological processi

  1. COPI coating of Golgi vesicle Source: Reactome
  2. membrane organization Source: Reactome
  3. positive regulation of GTPase activity Source: GOC
  4. post-Golgi vesicle-mediated transport Source: Reactome
  5. regulation of ARF protein signal transduction Source: InterPro
  6. retrograde vesicle-mediated transport, Golgi to ER Source: Reactome
  7. vesicle-mediated transport Source: GO_Central
  8. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_11096. COPI Mediated Transport.
REACT_19187. Clathrin derived vesicle budding.

Names & Taxonomyi

Protein namesi
Recommended name:
Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1
Short name:
BFA-resistant GEF 1
Gene namesi
Name:GBF1
Synonyms:KIAA0248
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:4181. GBF1.

Subcellular locationi

GO - Cellular componenti

  1. cis-Golgi network Source: Ensembl
  2. endoplasmic reticulum lumen Source: Ensembl
  3. Golgi apparatus Source: HPA
  4. Golgi membrane Source: Reactome
  5. Golgi stack Source: Ensembl
  6. membrane Source: UniProtKB
  7. mitochondrion Source: Ensembl
  8. peroxisome Source: Ensembl
  9. trans-Golgi network Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28595.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18591859Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1PRO_0000120210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei507 – 5071Phosphothreonine1 Publication
Modified residuei662 – 6621Phosphoserine1 Publication
Modified residuei1298 – 12981Phosphoserine3 Publications
Modified residuei1316 – 13161Phosphotyrosine1 Publication
Modified residuei1320 – 13201Phosphoserine1 Publication
Modified residuei1335 – 13351Phosphoserine1 Publication
Modified residuei1475 – 14751Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ92538.
PaxDbiQ92538.
PeptideAtlasiQ92538.
PRIDEiQ92538.

PTM databases

PhosphoSiteiQ92538.

Miscellaneous databases

PMAP-CutDBQ92538.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ92538.
CleanExiHS_GBF1.
ExpressionAtlasiQ92538. baseline and differential.
GenevestigatoriQ92538.

Organism-specific databases

HPAiHPA037759.
HPA037760.

Interactioni

Subunit structurei

Interacts with poliovirus protein 3A.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
COPG1P536202EBI-359050,EBI-8511600From a different organism.
COPG1Q9Y6782EBI-359050,EBI-1049127

Protein-protein interaction databases

BioGridi114268. 23 interactions.
IntActiQ92538. 8 interactions.
MINTiMINT-5006508.
STRINGi9606.ENSP00000359000.

Structurei

3D structure databases

ProteinModelPortaliQ92538.
SMRiQ92538. Positions 706-889.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini692 – 882191SEC7PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1751 – 1854104Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 SEC7 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5307.
GeneTreeiENSGT00770000120644.
HOGENOMiHOG000230678.
HOVERGENiHBG005810.
InParanoidiQ92538.
KOiK18443.
OMAiAFTERWM.
OrthoDBiEOG7Z3F3M.
PhylomeDBiQ92538.
TreeFamiTF105934.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR023394. Sec7_alpha_orthog.
IPR000904. Sec7_dom.
[Graphical view]
PfamiPF01369. Sec7. 1 hit.
[Graphical view]
SMARTiSM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF48425. SSF48425. 1 hit.
PROSITEiPS50190. SEC7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q92538-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVDKNIYIIQ GEINIVVGAI KRNARWSTHT PLDEERDPLL HSFGHLKEVL
60 70 80 90 100
NSITELSEIE PNVFLRPFLE VIRSEDTTGP ITGLALTSVN KFLSYALIDP
110 120 130 140 150
THEGTAEGME NMADAVTHAR FVGTDPASDE VVLMKILQVL RTLLLTPVGA
160 170 180 190 200
HLTNESVCEI MQSCFRICFE MRLSELLRKS AEHTLVDMVQ LLFTRLPQFK
210 220 230 240 250
EEPKNYVGTN MKKLKMRAGG MSDSSKWKKQ KRSPRPPRHM TKVTPGSELP
260 270 280 290 300
TPNGTTLSSN LTGGMPFIDV PTPISSASSE AASAVVSPST DSGLEFSSQT
310 320 330 340 350
TSKEDLTDLE QPGSPGYSTA TEPGSSELGV PEQPDLQEGT HVEKSQSASV
360 370 380 390 400
ESIPEVLEEC TSPADHSDSA SVHDMDYVNP RGVRFTQSSQ KEGTALVPYG
410 420 430 440 450
LPCIRELFRF LISLTNPHDR HNSEVMIHMG LHLLTVALES APVAQCQTLL
460 470 480 490 500
GLIKDEMCRH LFQLLSIERL NLYAASLRVC FLLFESMREH LKFQMEMYIK
510 520 530 540 550
KLMEIITVEN PKMPYEMKEM ALEAIVQLWR IPSFVTELYI NYDCDYYCSN
560 570 580 590 600
LFEELTKLLS KNAFPVSGQL YTTHLLSLDA LLTVIDSTEA HCQAKVLNSL
610 620 630 640 650
TQQEKKETAR PSCEIVDGTR EASNTERTAS DGKAVGMASD IPGLHLPGGG
660 670 680 690 700
RLPPEHGKSG CSDLEEAVDS GADKKFARKP PRFSCLLPDP RELIEIKNKK
710 720 730 740 750
KLLITGTEQF NQKPKKGIQF LQEKGLLTIP MDNTEVAQWL RENPRLDKKM
760 770 780 790 800
IGEFVSDRKN IDLLESFVST FSFQGLRLDE ALRLYLEAFR LPGEAPVIQR
810 820 830 840 850
LLEAFTERWM NCNGSPFANS DACFSLAYAV IMLNTDQHNH NVRKQNAPMT
860 870 880 890 900
LEEFRKNLKG VNGGKDFEQD ILEDMYHAIK NEEIVMPEEQ TGLVRENYVW
910 920 930 940 950
NVLLHRGATP EGIFLRVPTA SYDLDLFTMT WGPTIAALSY VFDKSLEETI
960 970 980 990 1000
IQKAISGFRK CAMISAHYGL SDVFDNLIIS LCKFTALSSE SIENLPSVFG
1010 1020 1030 1040 1050
SNPKAHIAAK TVFHLAHRHG DILREGWKNI MEAMLQLFRA QLLPKAMIEV
1060 1070 1080 1090 1100
EDFVDPNGKI SLQREETPSN RGESTVLSFV SWLTLSGPEQ SSVRGPSTEN
1110 1120 1130 1140 1150
QEAKRVALEC IKQCDPEKMI TESKFLQLES LQELMKALVS VTPDEETYDE
1160 1170 1180 1190 1200
EDAAFCLEML LRIVLENRDR VGCVWQTVRD HLYHLCVQAQ DFCFLVERAV
1210 1220 1230 1240 1250
VGLLRLAIRL LRREEISAQV LLSLRILLLM KPSVLSRVSH QVAYGLHELL
1260 1270 1280 1290 1300
KTNAANIHSG DDWATLFTLL ECIGSGVKPP AALQATARAD APDAGAQSDS
1310 1320 1330 1340 1350
ELPSYHQNDV SLDRGYTSDS EVYTDHGRPG KIHRSATDAD VVNSGWLVVG
1360 1370 1380 1390 1400
KDDVDNSKPG PSRPGPSPLI NQYSLTVGLD LGPHDTKSLL KCVESLSFIV
1410 1420 1430 1440 1450
RDAAHITPDN FELCVKTLRI FVEASLNGGC KSQEKRGKSH KYDSKGNRFK
1460 1470 1480 1490 1500
KKSKEGSMLR RPRTSSQHAS RGGQSDDDED EGVPASYHTV SLQVSQDLLD
1510 1520 1530 1540 1550
LMHTLHTRAA SIYSSWAEEQ RHLETGGQKI EADSRTLWAH CWCPLLQGIA
1560 1570 1580 1590 1600
CLCCDARRQV RMQALTYLQR ALLVHDLQKL DALEWESCFN KVLFPLLTKL
1610 1620 1630 1640 1650
LENISPADVG GMEETRMRAS TLLSKVFLQH LSPLLSLSTF AALWLTILDF
1660 1670 1680 1690 1700
MDKYMHAGSS DLLSEAIPES LKNMLLVMDT AEIFHSADAR GGGPSALWEI
1710 1720 1730 1740 1750
TWERIDCFLP HLRDELFKQT VIQDPMPMEP QGQKPLASAH LTSAAGDTRT
1760 1770 1780 1790 1800
PGHPPPPEIP SELGACDFEK PESPRAASSS SPGSPVASSP SRLSPTPDGP
1810 1820 1830 1840 1850
PPLAQPPLIL QPLASPLQVG VPPMTLPIIL NPALIEATSP VPLLATPRPT

DPIPTSEVN
Length:1,859
Mass (Da):206,446
Last modified:August 1, 1999 - v2
Checksum:i5015D2BD70009CFA
GO

Sequence cautioni

The sequence BAA13379.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241A → S in BAA13379. (PubMed:9039502)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1693 – 16931G → S.
Corresponds to variant rs11191274 [ dbSNP | Ensembl ].
VAR_051926

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068755 mRNA. Translation: AAD15903.1.
D87435 mRNA. Translation: BAA13379.2. Different initiation.
AL356420, AL121928, AL160011 Genomic DNA. Translation: CAH72761.1.
AL121928, AL160011, AL356420 Genomic DNA. Translation: CAI12515.1.
AL160011, AL121928, AL356420 Genomic DNA. Translation: CAH71625.1.
BC007941 mRNA. Translation: AAH07941.2.
BC014171 mRNA. Translation: AAH14171.2.
CCDSiCCDS7533.1.
RefSeqiNP_001186307.1. NM_001199378.1.
NP_001186308.1. NM_001199379.1.
NP_004184.1. NM_004193.2.
UniGeneiHs.290243.

Genome annotation databases

EnsembliENST00000369983; ENSP00000359000; ENSG00000107862.
GeneIDi8729.
KEGGihsa:8729.
UCSCiuc001kux.2. human.

Polymorphism databases

DMDMi13124260.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF068755 mRNA. Translation: AAD15903.1.
D87435 mRNA. Translation: BAA13379.2. Different initiation.
AL356420, AL121928, AL160011 Genomic DNA. Translation: CAH72761.1.
AL121928, AL160011, AL356420 Genomic DNA. Translation: CAI12515.1.
AL160011, AL121928, AL356420 Genomic DNA. Translation: CAH71625.1.
BC007941 mRNA. Translation: AAH07941.2.
BC014171 mRNA. Translation: AAH14171.2.
CCDSiCCDS7533.1.
RefSeqiNP_001186307.1. NM_001199378.1.
NP_001186308.1. NM_001199379.1.
NP_004184.1. NM_004193.2.
UniGeneiHs.290243.

3D structure databases

ProteinModelPortaliQ92538.
SMRiQ92538. Positions 706-889.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114268. 23 interactions.
IntActiQ92538. 8 interactions.
MINTiMINT-5006508.
STRINGi9606.ENSP00000359000.

PTM databases

PhosphoSiteiQ92538.

Polymorphism databases

DMDMi13124260.

Proteomic databases

MaxQBiQ92538.
PaxDbiQ92538.
PeptideAtlasiQ92538.
PRIDEiQ92538.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369983; ENSP00000359000; ENSG00000107862.
GeneIDi8729.
KEGGihsa:8729.
UCSCiuc001kux.2. human.

Organism-specific databases

CTDi8729.
GeneCardsiGC10P103995.
HGNCiHGNC:4181. GBF1.
HPAiHPA037759.
HPA037760.
MIMi603698. gene.
neXtProtiNX_Q92538.
PharmGKBiPA28595.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5307.
GeneTreeiENSGT00770000120644.
HOGENOMiHOG000230678.
HOVERGENiHBG005810.
InParanoidiQ92538.
KOiK18443.
OMAiAFTERWM.
OrthoDBiEOG7Z3F3M.
PhylomeDBiQ92538.
TreeFamiTF105934.

Enzyme and pathway databases

ReactomeiREACT_11096. COPI Mediated Transport.
REACT_19187. Clathrin derived vesicle budding.

Miscellaneous databases

ChiTaRSiGBF1. human.
GeneWikiiGBF1.
GenomeRNAii8729.
NextBioi32749.
PMAP-CutDBQ92538.
PROiQ92538.
SOURCEiSearch...

Gene expression databases

BgeeiQ92538.
CleanExiHS_GBF1.
ExpressionAtlasiQ92538. baseline and differential.
GenevestigatoriQ92538.

Family and domain databases

Gene3Di1.10.1000.11. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR023394. Sec7_alpha_orthog.
IPR000904. Sec7_dom.
[Graphical view]
PfamiPF01369. Sec7. 1 hit.
[Graphical view]
SMARTiSM00222. Sec7. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 6 hits.
SSF48425. SSF48425. 1 hit.
PROSITEiPS50190. SEC7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human GBF1 is a ubiquitously expressed gene of the sec7 domain family mapping to 10q24."
    Mansour S.J., Herbrick J.-A., Scherer S.W., Melancon P.
    Genomics 54:323-327(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
    Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
    DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    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] OF 1312-1859.
    Tissue: Kidney and Muscle.
  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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Effects of picornavirus 3A Proteins on Protein Transport and GBF1-dependent COP-I recruitment."
    Wessels E., Duijsings D., Lanke K.H., van Dooren S.H., Jackson C.L., Melchers W.J., van Kuppeveld F.J.
    J. Virol. 80:11852-11860(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLIOVIRUS PROTEIN 3A.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-507, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662 AND SER-1298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-1298; TYR-1316; SER-1335 AND SER-1475, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-1320, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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-1298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGBF1_HUMAN
AccessioniPrimary (citable) accession number: Q92538
Secondary accession number(s): Q5VXX3
, Q96CK6, Q96HZ3, Q9H473
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 1, 1999
Last modified: February 4, 2015
This is version 140 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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
  5. 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.