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Q9HCN4

- GPN1_HUMAN

UniProt

Q9HCN4 - GPN1_HUMAN

Protein

GPN-loop GTPase 1

Gene

GPN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Forms an interface between the RNA polymerase II enzyme and chaperone/scaffolding protein, suggesting that it is required to connect RNA polymerase II to regulators of protein complex formation. May be involved in nuclear localization of XPA.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 338GTP (Pootential)

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. nucleoside-triphosphatase activity Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GPN-loop GTPase 1
    Alternative name(s):
    MBD2-interacting protein
    Short name:
    MBDin
    XPA-binding protein 1
    Gene namesi
    Name:GPN1
    Synonyms:MBDIN, XAB1
    ORF Names:HUSSY-23
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:17030. GPN1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    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

    ArrayExpressiQ9HCN4.
    BgeeiQ9HCN4.
    CleanExiHS_GPN1.
    GenevestigatoriQ9HCN4.

    Organism-specific databases

    HPAiHPA036794.

    Interactioni

    Subunit structurei

    Tightly associated with the RNA polymerase II complex. Interacts with XPA.2 Publications

    Protein-protein interaction databases

    BioGridi116452. 57 interactions.
    IntActiQ9HCN4. 5 interactions.
    MINTiMINT-1460192.
    STRINGi9606.ENSP00000264718.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HCN4.
    SMRiQ9HCN4. Positions 18-254.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GPN-loop GTPase family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    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

    MAASAAAAEL QASGGPRHPV CLLVLGMAGS GKTTFVQRLT GHLHAQGTPP    50
    YVINLDPAVH EVPFPANIDI RDTVKYKEVM KQYGLGPNGG IVTSLNLFAT 100
    RFDQVMKFIE KAQNMSKYVL IDTPGQIEVF TWSASGTIIT EALASSFPTV 150
    VIYVMDTSRS TNPVTFMSNM LYACSILYKT KLPFIVVMNK TDIIDHSFAV 200
    EWMQDFEAFQ DALNQETTYV SNLTRSMSLV LDEFYSSLRV VGVSAVLGTG 250
    LDELFVQVTS AAEEYEREYR PEYERLKKSL ANAESQQQRE QLERLRKDMG 300
    SVALDAGTAK DSLSPVLHPS DLILTRGTLD EEDEEADSDT DDIDHRVTEE 350
    SHEEPAFQNF MQESMAQYWK RNNK 374
    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:
    EMBL
    GenBank
    DDBJ
    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]
    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:
    EMBL
    GenBank
    DDBJ
    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 18-254.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116452. 57 interactions.
    IntActi Q9HCN4. 5 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 ]
    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.
    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

    ArrayExpressi Q9HCN4.
    Bgeei Q9HCN4.
    CleanExi HS_GPN1.
    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

    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.
      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. "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.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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].
    15. "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].
    16. 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: October 1, 2014
    This is version 117 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