O43566 (RGS14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Regulator of G-protein signaling 14
Short name=RGS14

Gene names

Name:

RGS14

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	566 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a regulator of G protein signaling (RGS). Modulates G protein alpha subunits nucleotide exchange and hydrolysis activities by functioning either as a GTPase-activating protein (GAP), thereby driving G protein alpha subunits into their inactive GDP-bound form, or as a GDP-dissociation inhibitor (GDI). Confers GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not G(o) alpha subunit GNAO1 and G(i) alpha subunit GNAI2. Confers GAP activity on G(o) alpha subunit GNAI0 and G(i) alpha subunits GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS1 and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division. Probably required for the nerve growth factor (NGF)-mediated neurite outgrowth. May be involved in visual memory processing capacity and hippocampal-based learning and memory. Ref.7 Ref.8
Subunit structure	Interacts with GNAO1 and GNAI2. Interacts (via RGS and GoLoco domains) GNAI1; the interaction occurs in the centrosomes. Interacts with RABGEF1; the interactions is GTP-dependent. Interacts with RAP2A; the interactions is GTP-dependent and does not alter its function on G(i) alpha subunits either as GAP or as GDI. Associates with microtubules. Found in a complex with at least BRAF, HRAS1, MAP2K1, MAPK3 and RGS14. Interacts with RIC8A (via C-terminus). Interacts (via RBD 1 domain) with HRAS1 (active GTP-bound form preferentially). Interacts (via RBD domains) with BRAF (via N-terminus); the interaction mediates the formation of a ternary complex with RAF1. Interacts (via RBD domains) with RAF1 (via N-terminus); the interaction mediates the formation of a ternary complex with BRAF. Interacts with KRAS (active GTP-bound form preferentially), MRAS (active GTP-bound form preferentially), NRAS (active GTP-bound form preferentially) and RRAS (active GTP-bound form preferentially). Interacts with GNAI1 (via active GTP- or inactive GDP-bound forms); the interaction prevents association of RGS14 with centrosomes or nuclear localization. Interacts with GNAI2. Interacts with GNAI3 (via active GTP- or inactive GDP-bound forms); the interaction prevents association of RGS14 with centrosomes or nuclear localization By similarity. Associates with microtubules.
Subcellular location	Nucleus By similarity. Nucleus › PML body By similarity. Cytoplasm. Membrane By similarity. Cell membrane By similarity. Cytoplasm › cytoskeleton › centrosome By similarity. Cytoplasm › cytoskeleton › spindle. Cytoplasm › cytoskeleton › spindle pole By similarity. Cell projection › dendrite By similarity. Cell projection › dendritic spine By similarity. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density By similarity. Note: Associates with the perinuclear sheaths of microtubules (MTs) surrounding the pronuclei, prior to segregating to the anastral mitotic apparatus and subsequently the barrel-shaped cytoplasmic bridge between the nascent nuclei of the emerging 2-cell embryo. Localizes to a perinuclear compartment near the microtubule-organizing center (MTOC). Expressed in the nucleus during interphase and segregates to the centrosomes and astral MTs during mitosis. Relocalizes to the nucleus in PML nuclear bodies in response to heat stress. Colocalizes with RIC8A in CA2 hippocampal neurons. Localizes to spindle poles during metaphase. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. Recruited from the cytosol to the plasma membrane by the inactive GDP-bound forms of G(i) alpha subunits GNAI1 and GNAI3. Recruited from the cytosol to membranes by the active GTP-bound form of HRAS1. Colocalizes with G(i) alpha subunit GNAI1 and RIC8A at the plasma membrane. Colocalizes with BRAF and RAF1 in both the cytoplasm and membranes By similarity. Ref.7
Domain	The RGS domain is necessary for GTPase-activating protein (GAP) activity for G subunits and localization to the nucleus and centrosomes By similarity. The GoLoco domain is necessary for GDP-dissociation inhibitor (GDI) activity, translocation out of the nucleus and interaction with G(i) alpha subunits GNAI1, GNAI2 and GNAI3 By similarity. The RBD domains are necessary for localization to the nucleus and centrosomes By similarity.
Post-translational modification	Phosphorylated by PKC. Phosphorylation is increased in presence of forskolin and may enhance the GDI activity on G(i) alpha subunit GNAI1 By similarity.
Sequence similarities	Contains 1 GoLoco domain. Contains 2 RBD (Ras-binding) domains. Contains 1 RGS domain.
Sequence caution	The sequence AAB92614.1 differs from that shown. Reason: Frameshift at positions 337, 344, 348, 539 and 544.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Microtubule Nucleus Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	GTPase activation Signal transduction inhibitor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromosome segregation Inferred from sequence or structural similarity. Source: UniProtKB long-term memory Inferred from sequence or structural similarity. Source: UniProtKB long-term synaptic potentiation Inferred from sequence or structural similarity. Source: UniProtKB mitosis Inferred from electronic annotation. Source: Compara negative regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of MAP kinase activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of synaptic plasticity Inferred from sequence or structural similarity. Source: UniProtKB nucleocytoplasmic transport Inferred from sequence or structural similarity. Source: UniProtKB platelet-derived growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of neurogenesis Inferred from sequence or structural similarity. Source: UniProtKB regulation of DNA-dependent transcription in response to stress Inferred from sequence or structural similarity. Source: UniProtKB regulation of G-protein coupled receptor protein signaling pathway Traceable author statement PubMed 9168931. Source: ProtInc response to oxidative stress Inferred from sequence or structural similarity. Source: UniProtKB spindle organization Inferred from mutant phenotype Ref.7. Source: UniProtKB termination of G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: InterPro visual learning Inferred from sequence or structural similarity. Source: UniProtKB zygote asymmetric cell division Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell cell junction Inferred from electronic annotation. Source: UniProtKB-KW centrosome Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB intermediate filament cytoskeleton Inferred from direct assay. Source: HPA microtubule Inferred from electronic annotation. Source: UniProtKB-KW nuclear body Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB postsynaptic density Inferred from sequence or structural similarity. Source: UniProtKB postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW spindle pole Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	GDP-dissociation inhibitor activity Inferred from direct assay Ref.7. Source: UniProtKB GTPase activator activity Inferred from direct assay Ref.7. Source: UniProtKB microtubule binding Inferred from direct assay Ref.7. Source: UniProtKB receptor signaling complex scaffold activity Inferred from sequence or structural similarity. Source: UniProtKB receptor signaling protein activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O43566-7)

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.

Note: No experimental confirmation available.

Isoform 2 (identifier: O43566-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.
     352-354: ALV → VGT
     355-566: Missing.

Isoform 3 (identifier: O43566-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.
     351-351: Q → QK

Isoform 4 (identifier: O43566-6)

The sequence of this isoform differs from the canonical sequence as follows:
     54-273: Missing.
     351-351: Q → QK

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 566

566

Regulator of G-protein signaling 14

PRO_0000204217

Regions

Domain

67 – 184

118

RGS

Domain

302 – 373

72

RBD 1

Domain

375 – 445

71

RBD 2

Domain

498 – 521

24

GoLoco

Region

299 – 425

127

Necessary for interaction with RABGEF1 By similarity

Amino acid modifications

Modified residue

20

1

Phosphoserine Ref.9

Modified residue

42

1

Phosphoserine Ref.9

Modified residue

45

1

Phosphoserine Ref.9

Modified residue

288

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 153

153

Missing in isoform 2 and isoform 3.

VSP_027577

Alternative sequence

54 – 273

220

Missing in isoform 4.

VSP_029426

Alternative sequence

351

1

Q → QK in isoform 3 and isoform 4.

VSP_037959

Alternative sequence

352 – 354

3

ALV → VGT in isoform 2.

VSP_027578

Alternative sequence

355 – 566

212

Missing in isoform 2.

VSP_027579

Experimental info

Sequence conflict

407

1

H → R in BAC85600. Ref.4

Sequence conflict

415

1

V → A in AAY26402. Ref.1

Sequence conflict

502

1

Missing in AAB92614. Ref.2

Secondary structure

1

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566

Helix Strand Turn

Details...

Helix

61 – 65

5

Helix

68 – 73

6

Helix

75 – 84

10

Beta strand

87 – 89

3

Helix

92 – 105

14

Helix

111 – 125

15

Helix

144 – 148

5

Turn

152 – 155

4

Helix

156 – 167

12

Helix

170 – 174

5

Helix

180 – 184

5

Helix

499 – 509

11

Beta strand

517 – 519

3

Turn

522 – 525

4

Helix

529 – 531

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 1, 2009. Version 4. Checksum: 811296228B479C3D	FASTA	566	61,447
	10 20 30 40 50 60 MPGKPKHLGV PNGRMVLAVS DGELSSTTGP QGQGEGRGSS LSIHSLPSGP SSPFPTEEQP 70 80 90 100 110 120 VASWALSFER LLQDPLGLAY FTEFLKKEFS AENVTFWKAC ERFQQIPASD TQQLAQEARN 130 140 150 160 170 180 IYQEFLSSQA LSPVNIDRQA WLGEEVLAEP RPDMFRAQQL QIFNLMKFDS YARFVKSPLY 190 200 210 220 230 240 RECLLAEAEG RPLREPGSSR LGSPDATRKK PKLKPGKSLP LGVEELGQLP PVEGPGGRPL 250 260 270 280 290 300 RKSFRRELGG TANAALRRES QGSLNSSASL DLGFLAFVSS KSESHRKSLG STEGESESRP 310 320 330 340 350 360 GKYCCVYLPD GTASLALARP GLTIRDMLAG ICEKRGLSLP DIKVYLVGNE QALVLDQDCT 370 380 390 400 410 420 VLADQEVRLE NRITFELELT ALERVVRISA KPTKRLQEAL QPILEKHGLS PLEVVLHRPG 430 440 450 460 470 480 EKQPLDLGKL VSSVAAQRLV LDTLPGVKIS KARDKSPCRS QGCPPRTQDK ATHPPPASPS 490 500 510 520 530 540 SLVKVPSSAT GKRQTCDIEG LVELLNRVQS SGAHDQRGLL RKEDLVLPEF LQLPAQGPSS 550 560 EETPPQTKSA AQPIGGSLNS TTDSAL
	Isoform 2 [UniParc]. Checksum: 3CBC0E128BC8346E	FASTA	201	21,781
	10 20 30 40 50 60 MFRAQQLQIF NLMKFDSYAR FVKSPLYREC LLAEAEGRPL REPGSSRLGS PDATRKKPKL 70 80 90 100 110 120 KPGKSLPLGV EELGQLPPVE GPGGRPLRKS FRRELGGTAN AALRRESQGS LNSSASLDLG 130 140 150 160 170 180 FLAFVSSKSE SHRKSLGSTE GESESRPGKY CCVYLPDGTA SLALARPGLT IRDMLAGICE 190 200 KRGLSLPDIK VYLVGNEQVG T
	Isoform 3 [UniParc]. Checksum: 9B2548AD3346AA00	FASTA	414	44,820
	10 20 30 40 50 60 MFRAQQLQIF NLMKFDSYAR FVKSPLYREC LLAEAEGRPL REPGSSRLGS PDATRKKPKL 70 80 90 100 110 120 KPGKSLPLGV EELGQLPPVE GPGGRPLRKS FRRELGGTAN AALRRESQGS LNSSASLDLG 130 140 150 160 170 180 FLAFVSSKSE SHRKSLGSTE GESESRPGKY CCVYLPDGTA SLALARPGLT IRDMLAGICE 190 200 210 220 230 240 KRGLSLPDIK VYLVGNEQKA LVLDQDCTVL ADQEVRLENR ITFELELTAL ERVVRISAKP 250 260 270 280 290 300 TKRLQEALQP ILEKHGLSPL EVVLHRPGEK QPLDLGKLVS SVAAQRLVLD TLPGVKISKA 310 320 330 340 350 360 RDKSPCRSQG CPPRTQDKAT HPPPASPSSL VKVPSSATGK RQTCDIEGLV ELLNRVQSSG 370 380 390 400 410 AHDQRGLLRK EDLVLPEFLQ LPAQGPSSEE TPPQTKSAAQ PIGGSLNSTT DSAL
	Isoform 4 [UniParc]. Checksum: FBB19202385063E6	FASTA	347	36,922
	10 20 30 40 50 60 MPGKPKHLGV PNGRMVLAVS DGELSSTTGP QGQGEGRGSS LSIHSLPSGP SSPFLAFVSS 70 80 90 100 110 120 KSESHRKSLG STEGESESRP GKYCCVYLPD GTASLALARP GLTIRDMLAG ICEKRGLSLP 130 140 150 160 170 180 DIKVYLVGNE QKALVLDQDC TVLADQEVRL ENRITFELEL TALERVVRIS AKPTKRLQEA 190 200 210 220 230 240 LQPILEKHGL SPLEVVLHRP GEKQPLDLGK LVSSVAAQRL VLDTLPGVKI SKARDKSPCR 250 260 270 280 290 300 SQGCPPRTQD KATHPPPASP SSLVKVPSSA TGKRQTCDIE GLVELLNRVQ SSGAHDQRGL 310 320 330 340 LRKEDLVLPE FLQLPAQGPS SEETPPQTKS AAQPIGGSLN STTDSAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Localization of the GoLoco motif carrier regulator of G-protein signalling 12 and 14 proteins in monkey and rat brain." Lopez-Aranda M.F., Acevedo M.J., Carballo F.J., Gutierrez A., Khan Z.U. Eur. J. Neurosci. 23:2971-2982(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Brain.
[2]	Chatterjee T.K., Fisher R.A. Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
[3]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[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] (ISOFORM 4). Tissue: Caudate nucleus.
[5]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Colon.
[7]	"RGS14 is a microtubule-associated protein." Martin-McCaffrey L., Willard F.S., Pajak A., Dagnino L., Siderovski D.P., D'Souza S.J. Cell Cycle 4:953-960(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION.
[8]	"Localization of Gi alpha proteins in the centrosomes and at the midbody: implication for their role in cell division." Cho H., Kehrl J.H. J. Cell Biol. 178:245-255(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-42 AND SER-45, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Structure-based protocol for identifying mutations that enhance protein-protein binding affinities." Sammond D.W., Eletr Z.M., Purbeck C., Kimple R.J., Siderovski D.P., Kuhlman B. J. Mol. Biol. 371:1392-1404(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 497-532.
[11]	"Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits." Soundararajan M., Willard F.S., Kimple A.J., Turnbull A.P., Ball L.J., Schoch G.A., Gileadi C., Fedorov O.Y., Dowler E.F., Higman V.A., Hutsell S.Q., Sundstroem M., Doyle D.A., Siderovski D.P. Proc. Natl. Acad. Sci. U.S.A. 105:6457-6462(2008) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 56-207.
[12]	"Structural determinants of affinity enhancement between GoLoco motifs and G-protein alpha subunit mutants." Bosch D.E., Kimple A.J., Sammond D.W., Muller R.E., Miley M.J., Machius M., Kuhlman B., Willard F.S., Siderovski D.P. J. Biol. Chem. 286:3351-3358(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 497-532 IN COMPLEX WITH GNAI1 AND GDP.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

A balanced mind - Issue 132 of October 2011

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY987041 mRNA. Translation: AAY26402.1.
AF037194 mRNA. Translation: AAB92613.1.
AF037195 mRNA. Translation: AAB92614.1. Frameshift.
AF493936 mRNA. Translation: AAM12650.1.
AK123382 mRNA. Translation: BAC85600.1.
AC146507 Genomic DNA. No translation available.
BC014094 mRNA. Translation: AAH14094.1.

IPI

IPI00219126.
IPI00873546.
IPI00914936.
IPI00943204.

RefSeq

NP_006471.2. NM_006480.4.

UniGene

Hs.9347.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JNU	NMR	-	A	56-207	[»]
2OM2	X-ray	2.20	B/D	497-532	[»]
2XNS	X-ray	3.41	C/D	497-520	[»]
3ONW	X-ray	2.38	C/D	497-532	[»]
3QI2	X-ray	2.80	C/D	497-532	[»]

ProteinModelPortal

O43566.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41167N.

IntAct

O43566. 6 interactions.

MINT

MINT-236295.

STRING

9606.ENSP00000386229.

PTM databases

PhosphoSite

O43566.

Proteomic databases

PaxDb

O43566.

PRIDE

O43566.

Protocols and materials databases

DNASU

10636.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000408923; ENSP00000386229; ENSG00000169220.

GeneID

10636.

KEGG

hsa:10636.

UCSC

uc003mgf.3. human.
uc003mgg.1. human.

Organism-specific databases

CTD

10636.

GeneCards

GC05P176784.

HGNC

HGNC:9996. RGS14.

HPA

HPA046847.

MIM

602513. gene.

neXtProt

NX_O43566.

PharmGKB

PA34366.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG253607.

HOGENOM

HOG000049111.

HOVERGEN

HBG061568.

KO

K16449.

OMA

CPPRTQD.

OrthoDB

EOG4RR6HP.

Gene expression databases

Bgee

O43566.

CleanEx

HS_RGS14.

Genevestigator

O43566.

GermOnline

ENSG00000169220. Homo sapiens.

Family and domain databases

Gene3D

1.10.196.10. 1 hit.

InterPro

IPR003109. GoLoco_motif.
IPR003116. Raf-like_ras-bd.
IPR000342. Regulat_G_prot_signal.
IPR024066. Regulat_G_prot_signal_dom1.
IPR016137. Regulat_G_prot_signal_superfam.
[Graphical view]

Pfam

PF02188. GoLoco. 1 hit.
PF02196. RBD. 2 hits.
PF00615. RGS. 1 hit.
[Graphical view]

PRINTS

PR01301. RGSPROTEIN.

SMART

SM00390. GoLoco. 1 hit.
SM00455. RBD. 2 hits.
SM00315. RGS. 1 hit.
[Graphical view]

SUPFAM

SSF48097. Regulat_G_prot_signal_superfam. 1 hit.

PROSITE

PS50877. GOLOCO. 1 hit.
PS50898. RBD. 2 hits.
PS50132. RGS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O43566.

GenomeRNAi

10636.

NextBio

40425.

SOURCE

Search...

Entry information

Entry name

RGS14_HUMAN

Accession

Primary (citable) accession number: O43566
Secondary accession number(s): O43565 , Q506M1, Q6ZWA4, Q8TD62

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	September 1, 2009
Last modified:	May 1, 2013
This is version 124 of the entry and version 4 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.