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Q9HCN4

- GPN1_HUMAN

UniProt

Q9HCN4 - GPN1_HUMAN

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Protein

GPN-loop GTPase 1

Gene

GPN1

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

Functioni

Small GTPase required for proper nuclear import of RNA polymerase II (RNAPII) (PubMed:20855544, PubMed:21768307). May act at an RNAP assembly step prior to nuclear import (PubMed:21768307). Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding proteins, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation (PubMed:17643375). May be involved in nuclear localization of XPA (PubMed:11058119).3 Publications1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei88 – 881Stabilizes the phosphate intermediate; shared with dimeric partnerBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi29 – 346GTPBy similarity
Nucleotide bindingi189 – 1924GTPBy similarity

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
GPN-loop GTPase 11 Publication (EC:3.6.5.-2 Publications)
Alternative name(s):
MBD2-interacting protein
Short name:
MBDin
RNAPII-associated protein 41 Publication
XPA-binding protein 11 Publication
Gene namesi
Name:GPN1Imported1 Publication
Synonyms:MBDIN, RPAP41 Publication, XAB11 Publication
ORF Names:HUSSY-23
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:17030. GPN1.

Subcellular locationi

Cytoplasm 2 Publications. Nucleus 1 Publication
Note: Shuttles between the nucleus and the cytoplasm.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 324GSGK → AAAA: Abolishes GTPase activity and decreases association with GPN3. 1 Publication

Organism-specific databases

PharmGKBiPA162390148.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 374373GPN-loop GTPase 1PRO_0000066001Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei312 – 3121Phosphoserine1 Publication
Modified residuei314 – 3141Phosphoserine3 Publications
Modified residuei338 – 3381Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9HCN4.
PaxDbiQ9HCN4.
PeptideAtlasiQ9HCN4.
PRIDEiQ9HCN4.

PTM databases

PhosphoSiteiQ9HCN4.

Expressioni

Tissue specificityi

Expressed ubiquitously.

Gene expression databases

BgeeiQ9HCN4.
CleanExiHS_GPN1.
ExpressionAtlasiQ9HCN4. baseline and differential.
GenevestigatoriQ9HCN4.

Organism-specific databases

HPAiHPA036794.

Interactioni

Subunit structurei

Heterodimer with GPN3 (PubMed:21768307). Binds to RNA polymerase II (RNAPII) (PubMed:17643375, PubMed:20864038, PubMed:21844196). Interacts directly with RNAPII subunits RPB4 and RPB7 and the CTD of RPB1 (PubMed:21768307). Interacts with XPA (PubMed:11058119).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GPN3Q9UHW53EBI-745137,EBI-395491

Protein-protein interaction databases

BioGridi116452. 60 interactions.
IntActiQ9HCN4. 6 interactions.
MINTiMINT-1460192.
STRINGi9606.ENSP00000264718.

Structurei

3D structure databases

ProteinModelPortaliQ9HCN4.
SMRiQ9HCN4. Positions 22-254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi86 – 883Gly-Pro-Asn (GPN)-loop; involved in dimer interfaceBy similarity

Sequence similaritiesi

Belongs to the GPN-loop GTPase family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00550000074926.
HOGENOMiHOG000191633.
HOVERGENiHBG047768.
InParanoidiQ9HCN4.
KOiK06883.
OrthoDBiEOG7SN8D0.
PhylomeDBiQ9HCN4.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR004130. Uncharacterised_ATP-bd.
[Graphical view]
PfamiPF03029. ATP_bind_1. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9HCN4-1) [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
MAASAAAAEL QASGGPRHPV CLLVLGMAGS GKTTFVQRLT GHLHAQGTPP
60 70 80 90 100
YVINLDPAVH EVPFPANIDI RDTVKYKEVM KQYGLGPNGG IVTSLNLFAT
110 120 130 140 150
RFDQVMKFIE KAQNMSKYVL IDTPGQIEVF TWSASGTIIT EALASSFPTV
160 170 180 190 200
VIYVMDTSRS TNPVTFMSNM LYACSILYKT KLPFIVVMNK TDIIDHSFAV
210 220 230 240 250
EWMQDFEAFQ DALNQETTYV SNLTRSMSLV LDEFYSSLRV VGVSAVLGTG
260 270 280 290 300
LDELFVQVTS AAEEYEREYR PEYERLKKSL ANAESQQQRE QLERLRKDMG
310 320 330 340 350
SVALDAGTAK DSLSPVLHPS DLILTRGTLD EEDEEADSDT DDIDHRVTEE
360 370
SHEEPAFQNF MQESMAQYWK RNNK
Length:374
Mass (Da):41,740
Last modified:March 1, 2001 - v1
Checksum:i9B96F452FAFE955C
GO
Isoform 2 (identifier: Q9HCN4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.

Note: No experimental confirmation available.

Show »
Length:295
Mass (Da):33,455
Checksum:i2C342A039956B031
GO
Isoform 3 (identifier: Q9HCN4-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: MAASAAAAEL...LNLFATRFDQ → MKFPFLPIL

Note: No experimental confirmation available.

Show »
Length:279
Mass (Da):31,832
Checksum:i80B128D78E155418
GO
Isoform 4 (identifier: Q9HCN4-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MAASAAAAELQASGGPRHPVCLLVLGMAGSGKTTFVQ → MTGHTRSSLPRCTGIVLLIKLRFSE

Note: No experimental confirmation available.

Show »
Length:362
Mass (Da):40,957
Checksum:iA4E9E4D5AF771F5A
GO
Isoform 5 (identifier: Q9HCN4-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRCLYGRVGGARRKM

Note: No experimental confirmation available.

Show »
Length:388
Mass (Da):43,345
Checksum:i1CC8DDB0DD6AEF92
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 104104MAASA…TRFDQ → MKFPFLPIL in isoform 3. 1 PublicationVSP_042749Add
BLAST
Alternative sequencei1 – 7979Missing in isoform 2. 1 PublicationVSP_042750Add
BLAST
Alternative sequencei1 – 3737MAASA…TTFVQ → MTGHTRSSLPRCTGIVLLIK LRFSE in isoform 4. 1 PublicationVSP_046176Add
BLAST
Alternative sequencei1 – 11M → MRCLYGRVGGARRKM in isoform 5. 1 PublicationVSP_054366

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044661 mRNA. Translation: BAB17612.1.
AK298827 mRNA. Translation: BAG60957.1.
AK298866 mRNA. Translation: BAG60986.1.
AK302131 mRNA. Translation: BAG63506.1.
AK310340 mRNA. No translation available.
AK316404 mRNA. Translation: BAH14775.1.
AC074091 Genomic DNA. No translation available.
BC007451 mRNA. Translation: AAH07451.1.
AJ010842 mRNA. Translation: CAA09376.1.
CCDSiCCDS1760.2. [Q9HCN4-5]
CCDS46248.1. [Q9HCN4-4]
CCDS46249.1. [Q9HCN4-3]
CCDS46250.1. [Q9HCN4-2]
RefSeqiNP_001138519.1. NM_001145047.1. [Q9HCN4-4]
NP_001138520.1. NM_001145048.1. [Q9HCN4-2]
NP_001138521.1. NM_001145049.1. [Q9HCN4-3]
NP_009197.2. NM_007266.3. [Q9HCN4-5]
UniGeneiHs.18259.

Genome annotation databases

EnsembliENST00000264718; ENSP00000264718; ENSG00000198522. [Q9HCN4-5]
ENST00000407583; ENSP00000384255; ENSG00000198522. [Q9HCN4-4]
ENST00000424214; ENSP00000398115; ENSG00000198522. [Q9HCN4-2]
ENST00000458167; ENSP00000412170; ENSG00000198522. [Q9HCN4-3]
ENST00000503738; ENSP00000427269; ENSG00000198522. [Q9HCN4-3]
ENST00000515877; ENSP00000424678; ENSG00000198522. [Q9HCN4-2]
ENST00000610189; ENSP00000476446; ENSG00000198522. [Q9HCN4-1]
ENST00000616939; ENSP00000484680; ENSG00000198522. [Q9HCN4-5]
GeneIDi11321.
KEGGihsa:11321.
UCSCiuc010ezg.1. human. [Q9HCN4-1]
uc010ymb.2. human. [Q9HCN4-3]

Polymorphism databases

DMDMi34925430.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB044661 mRNA. Translation: BAB17612.1 .
AK298827 mRNA. Translation: BAG60957.1 .
AK298866 mRNA. Translation: BAG60986.1 .
AK302131 mRNA. Translation: BAG63506.1 .
AK310340 mRNA. No translation available.
AK316404 mRNA. Translation: BAH14775.1 .
AC074091 Genomic DNA. No translation available.
BC007451 mRNA. Translation: AAH07451.1 .
AJ010842 mRNA. Translation: CAA09376.1 .
CCDSi CCDS1760.2. [Q9HCN4-5 ]
CCDS46248.1. [Q9HCN4-4 ]
CCDS46249.1. [Q9HCN4-3 ]
CCDS46250.1. [Q9HCN4-2 ]
RefSeqi NP_001138519.1. NM_001145047.1. [Q9HCN4-4 ]
NP_001138520.1. NM_001145048.1. [Q9HCN4-2 ]
NP_001138521.1. NM_001145049.1. [Q9HCN4-3 ]
NP_009197.2. NM_007266.3. [Q9HCN4-5 ]
UniGenei Hs.18259.

3D structure databases

ProteinModelPortali Q9HCN4.
SMRi Q9HCN4. Positions 22-254.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116452. 60 interactions.
IntActi Q9HCN4. 6 interactions.
MINTi MINT-1460192.
STRINGi 9606.ENSP00000264718.

PTM databases

PhosphoSitei Q9HCN4.

Polymorphism databases

DMDMi 34925430.

Proteomic databases

MaxQBi Q9HCN4.
PaxDbi Q9HCN4.
PeptideAtlasi Q9HCN4.
PRIDEi Q9HCN4.

Protocols and materials databases

DNASUi 11321.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264718 ; ENSP00000264718 ; ENSG00000198522 . [Q9HCN4-5 ]
ENST00000407583 ; ENSP00000384255 ; ENSG00000198522 . [Q9HCN4-4 ]
ENST00000424214 ; ENSP00000398115 ; ENSG00000198522 . [Q9HCN4-2 ]
ENST00000458167 ; ENSP00000412170 ; ENSG00000198522 . [Q9HCN4-3 ]
ENST00000503738 ; ENSP00000427269 ; ENSG00000198522 . [Q9HCN4-3 ]
ENST00000515877 ; ENSP00000424678 ; ENSG00000198522 . [Q9HCN4-2 ]
ENST00000610189 ; ENSP00000476446 ; ENSG00000198522 . [Q9HCN4-1 ]
ENST00000616939 ; ENSP00000484680 ; ENSG00000198522 . [Q9HCN4-5 ]
GeneIDi 11321.
KEGGi hsa:11321.
UCSCi uc010ezg.1. human. [Q9HCN4-1 ]
uc010ymb.2. human. [Q9HCN4-3 ]

Organism-specific databases

CTDi 11321.
GeneCardsi GC02P027821.
H-InvDB HIX0001929.
HGNCi HGNC:17030. GPN1.
HPAi HPA036794.
MIMi 611479. gene.
neXtProti NX_Q9HCN4.
PharmGKBi PA162390148.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00550000074926.
HOGENOMi HOG000191633.
HOVERGENi HBG047768.
InParanoidi Q9HCN4.
KOi K06883.
OrthoDBi EOG7SN8D0.
PhylomeDBi Q9HCN4.

Miscellaneous databases

ChiTaRSi GPN1. human.
GenomeRNAii 11321.
NextBioi 43011.
PROi Q9HCN4.
SOURCEi Search...

Gene expression databases

Bgeei Q9HCN4.
CleanExi HS_GPN1.
ExpressionAtlasi Q9HCN4. baseline and differential.
Genevestigatori Q9HCN4.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR004130. Uncharacterised_ATP-bd.
[Graphical view ]
Pfami PF03029. ATP_bind_1. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A novel cytoplasmic GTPase XAB1 interacts with DNA repair protein XPA."
    Nitta M., Saijo M., Kodo N., Matsuda T., Nakastu Y., Tamai H., Tanaka K.
    Nucleic Acids Res. 28:4212-4218(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH XPA, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
    Tissue: Cervix carcinoma.
  2. "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 2; 3; 4 AND 5).
    Tissue: Testis.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Muscle.
  5. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17; 182-190 AND 226-267, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  6. "Characterization of 16 novel human genes showing high similarity to yeast sequences."
    Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G.
    Yeast 18:69-80(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-374 (ISOFORM 1).
    Tissue: Liver and Spleen.
  7. "Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme."
    Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C., Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B., Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.
    Mol. Cell 27:262-274(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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-312; SER-314 AND SER-338, 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. "The protein interaction network of the human transcription machinery reveals a role for the conserved GTPase RPAP4/GPN1 and microtubule assembly in nuclear import and biogenesis of RNA polymerase II."
    Forget D., Lacombe A.A., Cloutier P., Al-Khoury R., Bouchard A., Lavallee-Adam M., Faubert D., Jeronimo C., Blanchette M., Coulombe B.
    Mol. Cell. Proteomics 9:2827-2839(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, BINDING TO RNA POYMERASE II.
  13. "HSP90 and its R2TP/Prefoldin-like cochaperone are involved in the cytoplasmic assembly of RNA polymerase II."
    Boulon S., Pradet-Balade B., Verheggen C., Molle D., Boireau S., Georgieva M., Azzag K., Robert M.C., Ahmad Y., Neel H., Lamond A.I., Bertrand E.
    Mol. Cell 39:912-924(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING TO RNA POYMERASE II.
  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-314 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "GTP-dependent binding and nuclear transport of RNA polymerase II by Npa3 protein."
    Staresincic L., Walker J., Dirac-Svejstrup A.B., Mitter R., Svejstrup J.Q.
    J. Biol. Chem. 286:35553-35561(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING TO RNA POYMERASE II.
  17. "Human GTPases associate with RNA polymerase II to mediate its nuclear import."
    Carre C., Shiekhattar R.
    Mol. Cell. Biol. 31:3953-3962(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BINDING TO RNA POYMERASE II, INTERACTION WITH GPN3; RPB1; RPB4 AND RPB7, CATALYTIC ACTIVITY, MUTAGENESIS OF 29-GLY--LYS-32.
  18. "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-314 AND SER-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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].
  20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGPN1_HUMAN
AccessioniPrimary (citable) accession number: Q9HCN4
Secondary accession number(s): B4DQJ5
, B4DQM4, B4DXU4, B5MBZ5, O76004
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 119 of the entry and version 1 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3