Q9HCN4 (GPN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.6
Subunit structure	Tightly associated with the RNA polymerase II complex. Interacts with XPA. Ref.1
Subcellular location	Cytoplasm Ref.1.
Tissue specificity	Expressed ubiquitously.
Sequence similarities	Belongs to the GPN-loop GTPase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell intracellular membrane-bounded organelle Inferred from direct assay. Source: HPA
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 374	373	GPN-loop GTPase 1		PRO_0000066001
Regions
	Nucleotide binding	26 – 33	8	GTP (Pootential)
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.3
	Modified residue	312	1	Phosphoserine Ref.7 Ref.8 Ref.9
	Modified residue	314	1	Phosphoserine Ref.5 Ref.7 Ref.9
	Modified residue	338	1	Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12
	Modified residue	340	1	Phosphothreonine Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Q9HCN4 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 9B96F452FAFE955C	FASTA	374	41,740
	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

References

	« Hide 'large scale' referencesShow '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: 11058119] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH XPA, SUBCELLULAR LOCATION. Tissue: Cervix carcinoma.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[3]	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, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[4]	"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: 11124703] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-374. Tissue: Liver and Spleen.
[5]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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: 17643375] [Abstract] Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX.
[7]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND SER-314, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312 AND THR-340, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312; SER-314 AND SER-338, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, MASS SPECTROMETRY.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB044661 mRNA. Translation: BAB17612.1. BC007451 mRNA. Translation: AAH07451.1. AJ010842 mRNA. Translation: CAA09376.1.
IPI	IPI00027035.
RefSeq	NP_001138519.1. NM_001145047.1. NP_001138520.1. NM_001145048.1. NP_001138521.1. NM_001145049.1. NP_009197.2. NM_007266.3.
UniGene	Hs.18259.
3D structure databases
ProteinModelPortal	Q9HCN4.
SMR	Q9HCN4. Positions 14-261.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9HCN4. 4 interactions.
MINT	MINT-1460192.
STRING	Q9HCN4.
PTM databases
PhosphoSite	Q9HCN4.
Polymorphism databases
DMDM	34925430.
Proteomic databases
PeptideAtlas	Q9HCN4.
PRIDE	Q9HCN4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264718; ENSP00000264718; ENSG00000198522. ENST00000449402; ENSP00000390051; ENSG00000198522.
GeneID	11321.
KEGG	hsa:11321.
UCSC	uc002rlf.1. human.
Organism-specific databases
CTD	11321.
GeneCards	GC02P027821.
H-InvDB	HIX0001929.
HGNC	HGNC:17030. GPN1.
HPA	HPA036794.
MIM	611479. gene.
neXtProt	NX_Q9HCN4.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00550000074926.
HOVERGEN	HBG047768.
InParanoid	Q9HCN4.
PhylomeDB	Q9HCN4.
Gene expression databases
ArrayExpress	Q9HCN4.
Bgee	Q9HCN4.
CleanEx	HS_GPN1.
Genevestigator	Q9HCN4.
Family and domain databases
InterPro	IPR003593. ATPase_AAA+_core. IPR004130. Uncharacterised_ATP-bd. [Graphical view]
KO	K06883.
Pfam	PF03029. ATP_bind_1. 1 hit. [Graphical view]
SMART	SM00382. AAA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	43011.
SOURCE	Search...

Entry information

Entry name

GPN1_HUMAN

Accession

Primary (citable) accession number: Q9HCN4
Secondary accession number(s): O76004

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	March 1, 2001
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.