Q8VDU0 (GPSM2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
G-protein-signaling modulator 2

Alternative name(s):
Pins homolog

Gene names

Name:	Gpsm2
Synonyms:	Lgn, Pins

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	679 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays an important role in spindle pole orientation By similarity. Interacts and contributes to the functional activity of G(i) alpha proteins. Acts to stabilize the apical complex during neuroblast divisions.
Subunit structure	Interacts with LLGL2 By similarity. Interacts with INSC/inscuteable and F2RL2. Ref.4
Subcellular location	Cytoplasm By similarity. Cytoplasm › cell cortex By similarity. Note: Localizes in the cytoplasm in the interphase and at cell periphery in the metaphase By similarity.
Tissue specificity	Expressed in many tissues, but its expression is enriched in the ventricular zone of the developing central nervous systems.
Sequence similarities	Belongs to the GPSM family. Contains 4 GoLoco domains. Contains 8 TPR repeats.
Caution	It is uncertain whether Met-1 or Met-8 is the initiator.
Sequence caution	The sequence AAH21308.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence AAL87447.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Repeat TPR repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	establishment of mitotic spindle orientation Inferred from mutant phenotype PubMed 21385765. Source: MGI lung epithelial cell differentiation Inferred from mutant phenotype PubMed 21385765. Source: MGI regulation of G-protein coupled receptor protein signaling pathway Inferred from electronic annotation. Source: InterPro signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	apical part of cell Inferred from direct assay PubMed 21385765. Source: MGI cell cortex Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: Compara
Molecular_function	GDP-dissociation inhibitor 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

Chain

1 – 679

679

G-protein-signaling modulator 2

PRO_0000106359

Regions

Repeat

24 – 57

34

TPR 1

Repeat

62 – 95

34

TPR 2

Repeat

102 – 135

34

TPR 3

Repeat

142 – 184

43

TPR 4

Repeat

202 – 235

34

TPR 5

Repeat

242 – 275

34

TPR 6

Repeat

282 – 315

34

TPR 7

Repeat

322 – 355

34

TPR 8

Domain

490 – 512

23

GoLoco 1

Domain

543 – 565

23

GoLoco 2

Domain

594 – 616

23

GoLoco 3

Domain

628 – 650

23

GoLoco 4

Amino acid modifications

Modified residue

408

1

Phosphoserine Ref.5 Ref.6

Modified residue

484

1

Phosphoserine By similarity

Modified residue

487

1

Phosphothreonine By similarity

Modified residue

540

1

Phosphoserine By similarity

Modified residue

564

1

Phosphoserine Ref.6

Secondary structure

1

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679

Helix Strand Turn

Details...

Helix

22 – 36

15

Helix

40 – 53

14

Helix

58 – 74

17

Helix

78 – 95

18

Helix

98 – 114

17

Helix

118 – 134

17

Helix

138 – 157

20

Beta strand

159 – 163

5

Helix

172 – 195

24

Helix

198 – 214

17

Helix

218 – 235

18

Helix

238 – 254

17

Helix

258 – 274

17

Helix

278 – 294

17

Helix

298 – 314

17

Helix

318 – 335

18

Helix

338 – 352

15

Helix

631 – 640

10

Helix

644 – 646

3

Sequences

	Sequence		Length	Mass (Da)
	Q8VDU0 [UniParc]. Last modified April 20, 2010. Version 2. Checksum: 8005F2A52FE66D77	FASTA	679	75,591
	10 20 30 40 50 60 MEGNLISMRE DHSFHVRYRM EASCLELALE GERLCKSGDC RAGVSFFEAA VQVGTEDLKT 70 80 90 100 110 120 LSAIYSQLGN AYFYLHDYAK ALEYHHHDLT LARTIGDQLG EAKASGNLGN TLKVLGNFDE 130 140 150 160 170 180 AIVCCQRHLD ISRELNDKVG EARALYNLGN VYHAKGKSFG CPGPQDTGEF PEDVRNALQA 190 200 210 220 230 240 AVDLYEENLS LVTALGDRAA QGRAFGNLGN THYLLGNFRD AVIAHEQRLL IAKEFGDKAA 250 260 270 280 290 300 ERRAYSNLGN AYIFLGEFET ASEYYKKTLL LARQLKDRAV EAQSCYSLGN TYTLLQDYEK 310 320 330 340 350 360 AIDYHLKHLA IAQELKDRIG EGRACWSLGN AYTALGNHDQ AMHFAEKHLE ISREVGDKSG 370 380 390 400 410 420 ELTARLNLSD LQMVLGLSYS TNNSMMSENI EIDGSLHGAG AKLGRRHSME NLELMKLTPE 430 440 450 460 470 480 KVPNWNSEIL AKQKPLIAKP SAKLLFVNRL KGKKYKSGSA CTKVLQDASN SVDHRAPRSQ 490 500 510 520 530 540 KKISSDTIGD EGFFDLLRRF QSNRMDDQRC HLQGNCRTTS TAAASATPKL MKAPSVSVVS 550 560 570 580 590 600 PNTDEFLDLL ASSQSRRLDD QRASFSNLPG LRLTKGNSPS VLERLMTNDK KEPDEDFFDI 610 620 630 640 650 660 LVKCQGSRLD DQRCAPPSAA TKGPTVPDED FFSLILRSQA KRMDEQRVLL QRDPNRDSEF 670 GLKELLQNNA LLEFKHSGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A mouse homologue of Drosophila pins can asymmetrically localize and substitute for pins function in Drosophila neuroblasts." Yu F., Morin X., Kaushik R., Bahri S., Yang X., Chia W. J. Cell Sci. 116:887-896(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J.
[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]. Strain: FVB/N-3. Tissue: Mammary tumor.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-640. Strain: C57BL/6J. Tissue: Aorta and Vein.
[4]	"Asymmetric cell divisions promote stratification and differentiation of mammalian skin." Lechler T., Fuchs E. Nature 437:275-280(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INSC AND F2RL2. Strain: CD-1. Tissue: Epidermis.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, MASS SPECTROMETRY. Tissue: Melanoma.
[6]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408 AND SER-564, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY081187 mRNA. Translation: AAL87447.1. Different initiation.
BC021308 mRNA. Translation: AAH21308.1. Different initiation.
AK040996 mRNA. Translation: BAC30775.1.

IPI

IPI00165828.

RefSeq

NP_083798.2. NM_029522.2.

UniGene

Mm.226941.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3RO2	X-ray	2.30	A	22-357	[»]
3RO3	X-ray	1.10	A	198-357	[»]
4G2V	X-ray	2.40	A	22-357	[»]
4G5O	X-ray	2.90	E/F/G/H	628-653	[»]
4G5Q	X-ray	2.90	E/F/G/H	628-652	[»]
4G5R	X-ray	3.48	E/F/G/Z	628-652	[»]
4G5S	X-ray	3.62	E/F/G/Z	594-618	[»]

ProteinModelPortal

Q8VDU0.

SMR

Q8VDU0. Positions 20-381.

ModBase

Search...

PTM databases

PhosphoSite

Q8VDU0.

Proteomic databases

PaxDb

Q8VDU0.

PRIDE

Q8VDU0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000029482; ENSMUSP00000029482; ENSMUSG00000027883.

GeneID

76123.

KEGG

mmu:76123.

Organism-specific databases

CTD

29899.

MGI

MGI:1923373. Gpsm2.

Phylogenomic databases

eggNOG

COG0457.

GeneTree

ENSGT00530000063126.

HOGENOM

HOG000231543.

HOVERGEN

HBG051823.

InParanoid

Q8VDU0.

KO

K15837.

OMA

EYYEANL.

OrthoDB

EOG4SXNC5.

Gene expression databases

ArrayExpress

Q8VDU0.

Bgee

Q8VDU0.

Genevestigator

Q8VDU0.

GermOnline

ENSMUSG00000027883. Mus musculus.

Family and domain databases

Gene3D

1.25.40.10. 2 hits.

InterPro

IPR024807. G_prot_signal_mod_2.
IPR003109. GoLoco_motif.
IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

PANTHER

PTHR10098:SF39. PTHR10098:SF39. 1 hit.

Pfam

PF02188. GoLoco. 4 hits.
PF00515. TPR_1. 2 hits.
PF13176. TPR_7. 1 hit.
[Graphical view]

SMART

SM00390. GoLoco. 4 hits.
SM00028. TPR. 6 hits.
[Graphical view]

PROSITE

PS50877. GOLOCO. 4 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

344635.

SOURCE

Search...

Entry information

Entry name

GPSM2_MOUSE

Accession

Primary (citable) accession number: Q8VDU0
Secondary accession number(s): Q8BLX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	April 20, 2010
Last modified:	April 3, 2013
This is version 93 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program