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Protein

G patch domain-containing protein 1

Gene

GPATCH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

  • mRNA splicing, via spliceosome Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
G patch domain-containing protein 1
Alternative name(s):
Evolutionarily conserved G-patch domain-containing protein
Gene namesi
Name:GPATCH1
Synonyms:ECGP, GPATC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:24658. GPATCH1.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162390063.

Polymorphism and mutation databases

BioMutaiGPATCH1.
DMDMi74732921.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 931930G patch domain-containing protein 1PRO_0000287457Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei6 – 61PhosphoserineCombined sources
Modified residuei8 – 81PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9BRR8.
MaxQBiQ9BRR8.
PaxDbiQ9BRR8.
PRIDEiQ9BRR8.

PTM databases

iPTMnetiQ9BRR8.
PhosphoSiteiQ9BRR8.

Expressioni

Gene expression databases

BgeeiQ9BRR8.
CleanExiHS_GPATCH1.
ExpressionAtlasiQ9BRR8. baseline and differential.
GenevisibleiQ9BRR8. HS.

Organism-specific databases

HPAiHPA043430.
HPA043604.

Interactioni

Protein-protein interaction databases

BioGridi120406. 48 interactions.
IntActiQ9BRR8. 28 interactions.
STRINGi9606.ENSP00000170564.

Structurei

3D structure databases

ProteinModelPortaliQ9BRR8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini152 – 19847G-patchPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the GPATCH1 family.Curated
Contains 1 G-patch domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2138. Eukaryota.
ENOG410Y3I1. LUCA.
GeneTreeiENSGT00390000007074.
HOGENOMiHOG000112797.
HOVERGENiHBG071446.
InParanoidiQ9BRR8.
KOiK13123.
OMAiSPDVGHC.
OrthoDBiEOG7ZD1TV.
PhylomeDBiQ9BRR8.
TreeFamiTF314717.

Family and domain databases

InterProiIPR011666. DUF1604.
IPR000467. G_patch_dom.
[Graphical view]
PfamiPF07713. DUF1604. 1 hit.
PF01585. G-patch. 1 hit.
[Graphical view]
PROSITEiPS50174. G_PATCH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9BRR8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAARDSDSEE DLVSYGTGLE PLEEGERPKK PIPLQDQTVR DEKGRYKRFH
60 70 80 90 100
GAFSGGFSAG YFNTVGSKEG WTPSTFVSSR QNRADKSVLG PEDFMDEEDL
110 120 130 140 150
SEFGIAPKAI VTTDDFASKT KDRIREKARQ LAAATAPIPG ATLLDDLITP
160 170 180 190 200
AKLSVGFELL RKMGWKEGQG VGPRVKRRPR RQKPDPGVKI YGCALPPGSS
210 220 230 240 250
EGSEGEDDDY LPDNVTFAPK DVTPVDFTPK DNVHGLAYKG LDPHQALFGT
260 270 280 290 300
SGEHFNLFSG GSERAGDLGE IGLNKGRKLG ISGQAFGVGA LEEEDDDIYA
310 320 330 340 350
TETLSKYDTV LKDEEPGDGL YGWTAPRQYK NQKESEKDLR YVGKILDGFS
360 370 380 390 400
LASKPLSSKK IYPPPELPRD YRPVHYFRPM VAATSENSHL LQVLSESAGK
410 420 430 440 450
ATPDPGTHSK HQLNASKRAE LLGETPIQGS ATSVLEFLSQ KDKERIKEMK
460 470 480 490 500
QATDLKAAQL KARSLAQNAQ SSRAQLSPAA AAGHCSWNMA LGGGTATLKA
510 520 530 540 550
SNFKPFAKDP EKQKRYDEFL VHMKQGQKDA LERCLDPSMT EWERGRERDE
560 570 580 590 600
FARAALLYAS SHSTLSSRFT HAKEEDDSDQ VEVPRDQEND VGDKQSAVKM
610 620 630 640 650
KMFGKLTRDT FEWHPDKLLC KRFNVPDPYP DSTLVGLPRV KRDKYSVFNF
660 670 680 690 700
LTLPETASLP TTQASSEKVS QHRGPDKSRK PSRWDTSKHE KKEDSISEFL
710 720 730 740 750
SLARSKAEPP KQQSSPLVNK EEEHAPELSA NQTVNKDVDA QAEGEGSRPS
760 770 780 790 800
MDLFRAIFAS SSDEKSSSSE DEQGDSEDDQ AGSGEANFQS SQDTDLGETS
810 820 830 840 850
SVAHALVPAP QEPPPSFPIQ KMQIDEREEF GPRLPPVFCP NARQTLEVPQ
860 870 880 890 900
KEKHKKNKDK HKAKKEHRRK KEKKKKHRKH KHKGKQKNKK PEKSSSSESS
910 920 930
DSSDSQSDEE TADVSPQELL RRLKSLPLRR Q
Length:931
Mass (Da):103,345
Last modified:June 1, 2001 - v1
Checksum:i407082BEC44904F4
GO

Sequence cautioni

The sequence BAA91489.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAD39124.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti484 – 4841H → Y in BAA91489 (PubMed:14702039).Curated
Sequence conflicti748 – 7481R → P in AAN63596 (Ref. 1) Curated
Sequence conflicti800 – 8001S → L in CAD39124 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti476 – 4761L → P.1 Publication
Corresponds to variant rs2287679 [ dbSNP | Ensembl ].
VAR_032303
Natural varianti520 – 5201L → S.
Corresponds to variant rs16967805 [ dbSNP | Ensembl ].
VAR_051014
Natural varianti631 – 6311D → E.
Corresponds to variant rs35389599 [ dbSNP | Ensembl ].
VAR_059657
Natural varianti724 – 7241H → R.1 Publication
Corresponds to variant rs10416265 [ dbSNP | Ensembl ].
VAR_032304
Natural varianti728 – 7281L → S.2 Publications
Corresponds to variant rs10421769 [ dbSNP | Ensembl ].
VAR_032305
Natural varianti909 – 9091E → K.
Corresponds to variant rs16967824 [ dbSNP | Ensembl ].
VAR_032306

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF434677 mRNA. Translation: AAN63596.1.
BC006108 mRNA. Translation: AAH06108.1.
AL834465 mRNA. Translation: CAD39124.1. Different initiation.
AK001068 mRNA. Translation: BAA91489.1. Different initiation.
CCDSiCCDS12428.1.
RefSeqiNP_060495.2. NM_018025.2.
UniGeneiHs.466436.

Genome annotation databases

EnsembliENST00000170564; ENSP00000170564; ENSG00000076650.
GeneIDi55094.
KEGGihsa:55094.
UCSCiuc002nug.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF434677 mRNA. Translation: AAN63596.1.
BC006108 mRNA. Translation: AAH06108.1.
AL834465 mRNA. Translation: CAD39124.1. Different initiation.
AK001068 mRNA. Translation: BAA91489.1. Different initiation.
CCDSiCCDS12428.1.
RefSeqiNP_060495.2. NM_018025.2.
UniGeneiHs.466436.

3D structure databases

ProteinModelPortaliQ9BRR8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120406. 48 interactions.
IntActiQ9BRR8. 28 interactions.
STRINGi9606.ENSP00000170564.

PTM databases

iPTMnetiQ9BRR8.
PhosphoSiteiQ9BRR8.

Polymorphism and mutation databases

BioMutaiGPATCH1.
DMDMi74732921.

Proteomic databases

EPDiQ9BRR8.
MaxQBiQ9BRR8.
PaxDbiQ9BRR8.
PRIDEiQ9BRR8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000170564; ENSP00000170564; ENSG00000076650.
GeneIDi55094.
KEGGihsa:55094.
UCSCiuc002nug.2. human.

Organism-specific databases

CTDi55094.
GeneCardsiGPATCH1.
HGNCiHGNC:24658. GPATCH1.
HPAiHPA043430.
HPA043604.
neXtProtiNX_Q9BRR8.
PharmGKBiPA162390063.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2138. Eukaryota.
ENOG410Y3I1. LUCA.
GeneTreeiENSGT00390000007074.
HOGENOMiHOG000112797.
HOVERGENiHBG071446.
InParanoidiQ9BRR8.
KOiK13123.
OMAiSPDVGHC.
OrthoDBiEOG7ZD1TV.
PhylomeDBiQ9BRR8.
TreeFamiTF314717.

Miscellaneous databases

ChiTaRSiGPATCH1. human.
GenomeRNAii55094.
PROiQ9BRR8.

Gene expression databases

BgeeiQ9BRR8.
CleanExiHS_GPATCH1.
ExpressionAtlasiQ9BRR8. baseline and differential.
GenevisibleiQ9BRR8. HS.

Family and domain databases

InterProiIPR011666. DUF1604.
IPR000467. G_patch_dom.
[Graphical view]
PfamiPF07713. DUF1604. 1 hit.
PF01585. G-patch. 1 hit.
[Graphical view]
PROSITEiPS50174. G_PATCH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of an evolutionarily conserved G-patch domain containing protein."
    Luallen R.J., Sargeant R., Geng Y.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Urinary bladder.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-931, VARIANTS PRO-476; ARG-724 AND SER-728.
    Tissue: Melanoma.
  4. "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] OF 434-931, VARIANT SER-728.
    Tissue: Embryo.
  5. "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.
  6. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-8, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-8, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGPTC1_HUMAN
AccessioniPrimary (citable) accession number: Q9BRR8
Secondary accession number(s): Q8IZV6, Q8N3B7, Q9NW94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 102 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, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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

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 one 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.