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Q9HCN4 (GPN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GPN-loop GTPase 1
Alternative name(s):
MBD2-interacting protein
Short name=MBDin
XPA-binding protein 1
Gene names
Name:GPN1
Synonyms:MBDIN, XAB1
ORF Names:HUSSY-23
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

Tightly associated with the RNA polymerase II complex. Interacts with XPA. Ref.1 Ref.7

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Expressed ubiquitously.

Sequence similarities

Belongs to the GPN-loop GTPase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HCN4-1)

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.
Isoform 2 (identifier: Q9HCN4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9HCN4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: MAASAAAAEL...LNLFATRFDQ → MKFPFLPIL
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9HCN4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MAASAAAAELQASGGPRHPVCLLVLGMAGSGKTTFVQ → MTGHTRSSLPRCTGIVLLIKLRFSE
Note: No experimental confirmation available.
Isoform 5 (identifier: Q9HCN4-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRCLYGRVGGARRKM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 374373GPN-loop GTPase 1
PRO_0000066001

Regions

Nucleotide binding26 – 338GTP (Pootential)

Amino acid modifications

Modified residue21N-acetylalanine Ref.5 Ref.15 Ref.16
Modified residue3121Phosphoserine Ref.10
Modified residue3141Phosphoserine Ref.10 Ref.12 Ref.14
Modified residue3381Phosphoserine Ref.10 Ref.12 Ref.14

Natural variations

Alternative sequence1 – 104104MAASA…TRFDQ → MKFPFLPIL in isoform 3.
VSP_042749
Alternative sequence1 – 7979Missing in isoform 2.
VSP_042750
Alternative sequence1 – 3737MAASA…TTFVQ → MTGHTRSSLPRCTGIVLLIK LRFSE in isoform 4.
VSP_046176
Alternative sequence11M → MRCLYGRVGGARRKM in isoform 5.
VSP_054366

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 9B96F452FAFE955C

FASTA37441,740
        10         20         30         40         50         60 
MAASAAAAEL QASGGPRHPV CLLVLGMAGS GKTTFVQRLT GHLHAQGTPP YVINLDPAVH 

        70         80         90        100        110        120 
EVPFPANIDI RDTVKYKEVM KQYGLGPNGG IVTSLNLFAT RFDQVMKFIE KAQNMSKYVL 

       130        140        150        160        170        180 
IDTPGQIEVF TWSASGTIIT EALASSFPTV VIYVMDTSRS TNPVTFMSNM LYACSILYKT 

       190        200        210        220        230        240 
KLPFIVVMNK TDIIDHSFAV EWMQDFEAFQ DALNQETTYV SNLTRSMSLV LDEFYSSLRV 

       250        260        270        280        290        300 
VGVSAVLGTG LDELFVQVTS AAEEYEREYR PEYERLKKSL ANAESQQQRE QLERLRKDMG 

       310        320        330        340        350        360 
SVALDAGTAK DSLSPVLHPS DLILTRGTLD EEDEEADSDT DDIDHRVTEE SHEEPAFQNF 

       370 
MQESMAQYWK RNNK 

« Hide

Isoform 2 [UniParc].

Checksum: 2C342A039956B031
Show »

FASTA29533,455
Isoform 3 [UniParc].

Checksum: 80B128D78E155418
Show »

FASTA27931,832
Isoform 4 [UniParc].

Checksum: A4E9E4D5AF771F5A
Show »

FASTA36240,957
Isoform 5 [UniParc].

Checksum: 1CC8DDB0DD6AEF92
Show »

FASTA38843,345

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS46248.1. [Q9HCN4-4]
CCDS46249.1. [Q9HCN4-3]
CCDS46250.1. [Q9HCN4-2]
RefSeqNP_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]
UniGeneHs.18259.

3D structure databases

ProteinModelPortalQ9HCN4.
SMRQ9HCN4. Positions 18-254.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116452. 57 interactions.
IntActQ9HCN4. 5 interactions.
MINTMINT-1460192.
STRING9606.ENSP00000264718.

PTM databases

PhosphoSiteQ9HCN4.

Polymorphism databases

DMDM34925430.

Proteomic databases

MaxQBQ9HCN4.
PaxDbQ9HCN4.
PeptideAtlasQ9HCN4.
PRIDEQ9HCN4.

Protocols and materials databases

DNASU11321.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264718; ENSP00000264718; ENSG00000198522.
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]
GeneID11321.
KEGGhsa:11321.
UCSCuc010ezg.1. human. [Q9HCN4-1]
uc010ymb.2. human. [Q9HCN4-3]

Organism-specific databases

CTD11321.
GeneCardsGC02P027821.
H-InvDBHIX0001929.
HGNCHGNC:17030. GPN1.
HPAHPA036794.
MIM611479. gene.
neXtProtNX_Q9HCN4.
PharmGKBPA162390148.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000191633.
HOVERGENHBG047768.
InParanoidQ9HCN4.
KOK06883.
OrthoDBEOG7SN8D0.
PhylomeDBQ9HCN4.

Gene expression databases

ArrayExpressQ9HCN4.
BgeeQ9HCN4.
CleanExHS_GPN1.
GenevestigatorQ9HCN4.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR004130. Uncharacterised_ATP-bd.
[Graphical view]
PfamPF03029. ATP_bind_1. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGPN1. human.
GenomeRNAi11321.
NextBio43011.
PROQ9HCN4.
SOURCESearch...

Entry information

Entry nameGPN1_HUMAN
AccessionPrimary (citable) accession number: Q9HCN4
Secondary accession number(s): B4DQJ5 expand/collapse secondary AC list , B4DQM4, B4DXU4, B5MBZ5, O76004
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM