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Protein

Nucleolar GTP-binding protein 1

Gene

GTPBP4

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

Functioni

Involved in the biogenesis of the 60S ribosomal subunit.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi175 – 1828GTPPROSITE-ProRule annotation
Nucleotide bindingi221 – 2255GTPPROSITE-ProRule annotation
Nucleotide bindingi289 – 2924GTPPROSITE-ProRule annotation

GO - Molecular functioni

  1. GTPase activity Source: HGNC
  2. GTP binding Source: HGNC
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. negative regulation of cell-cell adhesion Source: HGNC
  3. negative regulation of cell migration Source: HGNC
  4. negative regulation of cell proliferation Source: HGNC
  5. negative regulation of collagen binding Source: HGNC
  6. negative regulation of DNA replication Source: HGNC
  7. negative regulation of protein ubiquitination Source: HGNC
  8. osteoblast differentiation Source: UniProtKB
  9. protein stabilization Source: HGNC
  10. regulation of cyclin-dependent protein serine/threonine kinase activity Source: HGNC
  11. ribosome biogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolar GTP-binding protein 1
Alternative name(s):
Chronic renal failure gene protein
GTP-binding protein NGB
Gene namesi
Name:GTPBP4
Synonyms:CRFG, NOG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:21535. GTPBP4.

Subcellular locationi

Nucleusnucleolus 3 Publications

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. Golgi apparatus Source: HPA
  3. membrane Source: UniProtKB
  4. nuclear membrane Source: HPA
  5. nucleolus Source: HPA
  6. nucleus Source: UniProtKB
  7. perinuclear region of cytoplasm Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134922009.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 634633Nucleolar GTP-binding protein 1PRO_0000195023Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei103 – 1031N6-acetyllysine1 Publication
Modified residuei468 – 4681Phosphoserine4 Publications
Modified residuei470 – 4701Phosphoserine4 Publications
Modified residuei472 – 4721Phosphoserine3 Publications
Modified residuei522 – 5221N6-acetyllysine1 Publication
Modified residuei558 – 5581Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BZE4.
PaxDbiQ9BZE4.
PRIDEiQ9BZE4.

2D gel databases

SWISS-2DPAGEQ9BZE4.

PTM databases

PhosphoSiteiQ9BZE4.

Expressioni

Gene expression databases

BgeeiQ9BZE4.
CleanExiHS_GTPBP4.
ExpressionAtlasiQ9BZE4. baseline and differential.
GenevestigatoriQ9BZE4.

Organism-specific databases

HPAiHPA039618.
HPA056468.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NF2P352409EBI-1056249,EBI-1014472

Protein-protein interaction databases

BioGridi117104. 44 interactions.
IntActiQ9BZE4. 11 interactions.
MINTiMINT-4728537.
STRINGi9606.ENSP00000354040.

Structurei

3D structure databases

ProteinModelPortaliQ9BZE4.
SMRiQ9BZE4. Positions 6-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini169 – 340172OBG-type GPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family. NOG subfamily.PROSITE-ProRule annotation
Contains 1 OBG-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG1084.
GeneTreeiENSGT00390000018475.
HOGENOMiHOG000164071.
HOVERGENiHBG052642.
InParanoidiQ9BZE4.
KOiK06943.
OMAiRMETEEP.
OrthoDBiEOG72G175.
PhylomeDBiQ9BZE4.
TreeFamiTF300430.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006073. GTP_binding_domain.
IPR024926. NOG1.
IPR010674. NOG1_Rossman_fold_dom.
IPR012973. NOG_C.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PfamiPF06858. NOG1. 1 hit.
PF08155. NOGCT. 1 hit.
[Graphical view]
PIRSFiPIRSF038919. NOG1. 1 hit.
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51710. G_OBG. 1 hit.
[Graphical view]

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. Align

Isoform 1 (identifier: Q9BZE4-1) [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
MAHYNFKKIT VVPSAKDFID LTLSKTQRKT PTVIHKHYQI HRIRHFYMRK
60 70 80 90 100
VKFTQQNYHD RLSQILTDFP KLDDIHPFYA DLMNILYDKD HYKLALGQIN
110 120 130 140 150
IAKNLVDNVA KDYVRLMKYG DSLYRCKQLK RAALGRMCTV IKRQKQSLEY
160 170 180 190 200
LEQVRQHLSR LPTIDPNTRT LLLCGYPNVG KSSFINKVTR ADVDVQPYAF
210 220 230 240 250
TTKSLFVGHM DYKYLRWQVV DTPGILDHPL EDRNTIEMQA ITALAHLRAA
260 270 280 290 300
VLYVMDLSEQ CGHGLREQLE LFQNIRPLFI NKPLIVVANK CDVKRIAELS
310 320 330 340 350
EDDQKIFTDL QSEGFPVIET STLTEEGVIK VKTEACDRLL AHRVETKMKG
360 370 380 390 400
NKVNEVLNRL HLAIPTRRDD KERPPFIPEG VVARRKRMET EESRKKRERD
410 420 430 440 450
LELEMGDDYI LDLQKYWDLM NLSEKHDKIP EIWEGHNIAD YIDPAIMKKL
460 470 480 490 500
EELEKEEELR TAAGEYDSVS ESEDEEMLEI RQLAKQIREK KKLKILESKE
510 520 530 540 550
KNTQGPRMPR TAKKVQRTVL EKEMRSLGVD MDDKDDAHYA VQARRSRSIT
560 570 580 590 600
RKRKREDSAP PSSVARSGSC SRTPRDVSGL RDVKMVKKAK TMMKNAQKKM
610 620 630
NRLGKKGEAD RHVFDMKPKH LLSGKRKAGK KDRR
Length:634
Mass (Da):73,964
Last modified:January 23, 2007 - v3
Checksum:i0A05E65E65D6DB62
GO
Isoform 2 (identifier: Q9BZE4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Note: No experimental confirmation available.

Show »
Length:587
Mass (Da):68,273
Checksum:i185E3546E24D4BE8
GO
Isoform 3 (identifier: Q9BZE4-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-116: Missing.

Note: No experimental confirmation available.

Show »
Length:518
Mass (Da):60,051
Checksum:i7F5B0AADB755446E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti593 – 5931Missing in AAD09830. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti525 – 5251R → H.1 Publication
Corresponds to variant rs3207775 [ dbSNP | Ensembl ].
VAR_068801

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 116116Missing in isoform 3. CuratedVSP_056146Add
BLAST
Alternative sequencei1 – 4747Missing in isoform 2. 1 PublicationVSP_056147Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120334 mRNA. Translation: AAD09830.1.
AF325353 mRNA. Translation: AAK13444.1.
AK001548 mRNA. Translation: BAG50937.1.
AK001552 mRNA. Translation: BAA91752.1.
AK301721 mRNA. Translation: BAH13539.1.
AK302219 mRNA. Translation: BAG63575.1.
AL359878, AC022536 Genomic DNA. Translation: CAI13664.1.
CH471072 Genomic DNA. Translation: EAW86526.1.
BC038975 mRNA. Translation: AAH38975.1.
CCDSiCCDS31132.1. [Q9BZE4-1]
RefSeqiNP_036473.2. NM_012341.2. [Q9BZE4-1]
UniGeneiHs.215766.

Genome annotation databases

EnsembliENST00000360803; ENSP00000354040; ENSG00000107937. [Q9BZE4-1]
GeneIDi23560.
KEGGihsa:23560.
UCSCiuc001ift.3. human. [Q9BZE4-1]

Polymorphism databases

DMDMi17368711.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120334 mRNA. Translation: AAD09830.1.
AF325353 mRNA. Translation: AAK13444.1.
AK001548 mRNA. Translation: BAG50937.1.
AK001552 mRNA. Translation: BAA91752.1.
AK301721 mRNA. Translation: BAH13539.1.
AK302219 mRNA. Translation: BAG63575.1.
AL359878, AC022536 Genomic DNA. Translation: CAI13664.1.
CH471072 Genomic DNA. Translation: EAW86526.1.
BC038975 mRNA. Translation: AAH38975.1.
CCDSiCCDS31132.1. [Q9BZE4-1]
RefSeqiNP_036473.2. NM_012341.2. [Q9BZE4-1]
UniGeneiHs.215766.

3D structure databases

ProteinModelPortaliQ9BZE4.
SMRiQ9BZE4. Positions 6-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117104. 44 interactions.
IntActiQ9BZE4. 11 interactions.
MINTiMINT-4728537.
STRINGi9606.ENSP00000354040.

PTM databases

PhosphoSiteiQ9BZE4.

Polymorphism databases

DMDMi17368711.

2D gel databases

SWISS-2DPAGEQ9BZE4.

Proteomic databases

MaxQBiQ9BZE4.
PaxDbiQ9BZE4.
PRIDEiQ9BZE4.

Protocols and materials databases

DNASUi23560.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360803; ENSP00000354040; ENSG00000107937. [Q9BZE4-1]
GeneIDi23560.
KEGGihsa:23560.
UCSCiuc001ift.3. human. [Q9BZE4-1]

Organism-specific databases

CTDi23560.
GeneCardsiGC10P001034.
HGNCiHGNC:21535. GTPBP4.
HPAiHPA039618.
HPA056468.
neXtProtiNX_Q9BZE4.
PharmGKBiPA134922009.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1084.
GeneTreeiENSGT00390000018475.
HOGENOMiHOG000164071.
HOVERGENiHBG052642.
InParanoidiQ9BZE4.
KOiK06943.
OMAiRMETEEP.
OrthoDBiEOG72G175.
PhylomeDBiQ9BZE4.
TreeFamiTF300430.

Miscellaneous databases

ChiTaRSiGTPBP4. human.
GeneWikiiGTPBP4.
GenomeRNAii23560.
NextBioi35468847.
PROiQ9BZE4.

Gene expression databases

BgeeiQ9BZE4.
CleanExiHS_GTPBP4.
ExpressionAtlasiQ9BZE4. baseline and differential.
GenevestigatoriQ9BZE4.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006073. GTP_binding_domain.
IPR024926. NOG1.
IPR010674. NOG1_Rossman_fold_dom.
IPR012973. NOG_C.
IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
[Graphical view]
PfamiPF06858. NOG1. 1 hit.
PF08155. NOGCT. 1 hit.
[Graphical view]
PIRSFiPIRSF038919. NOG1. 1 hit.
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51710. G_OBG. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a novel GTP-binding protein, NGB."
    Cheng J.Q., Cao C.H., Testa J.R., Golemis E.A., Jiang C., Yuan W., Nicosia S.V.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Identification of a novel nuclear guanosine triphosphate-binding protein differentially expressed in renal disease."
    Laping N.J., Olson B.A., Zhu Y.
    J. Am. Soc. Nephrol. 12:883-890(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    Tissue: Kidney.
  3. "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] (ISOFORMS 1 AND 2), VARIANT HIS-525.
    Tissue: Testis.
  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. 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: Uterus.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Bienvenut W.V.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-7; 9-25; 37-42; 53-71; 94-111; 119-125; 146-155; 161-169; 191-213; 217-248; 267-276; 296-330; 353-359; 372-384; 398-425; 429-448; 450-460 AND 526-544, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  9. "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.
  10. "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.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468; SER-470; SER-472 AND SER-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-468; SER-470 AND SER-472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-103 AND LYS-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-468; SER-470 AND SER-472, 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-468 AND SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiNOG1_HUMAN
AccessioniPrimary (citable) accession number: Q9BZE4
Secondary accession number(s): B3KMC5
, B4DY13, B7Z7A3, O95446, Q5T3R8, Q9NVJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 134 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, Direct protein sequencing, 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. 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.