O75628 (REM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GTP-binding protein REM 1

Alternative name(s):
GTPase-regulating endothelial cell sprouting
Rad and Gem-like GTP-binding protein 1

Gene names

Name:	REM1
Synonyms:	GES, REM

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	298 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Promotes endothelial cell sprouting and actin cytoskeletal reorganization. May be involved in angiogenesis. May function in Ca2+ signaling.
Subunit structure	In vitro, interacts with calmodulin in a calcium-dependent manner.
Tissue specificity	Most highly expressed in the endothelial lining of the blood vessels in uterus and heart. Lower levels found in spleen, lymph node, kidney and testis. Also found in cells with secretory function such as the islets of Langerhans, lobule/duct epithelium in the breast, bile duct epithelium in the liver, surface epithelium in the endometrial glands of the uterus, colon mucosa and acinar cells in the pancreas and the prostate.
Sequence similarities	Belongs to the small GTPase superfamily. RGK family.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Calmodulin-binding GTP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase 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 – 298

298

GTP-binding protein REM 1

PRO_0000122481

Regions

Nucleotide binding

87 – 94

8

GTP By similarity

Nucleotide binding

195 – 198

4

GTP By similarity

Region

268 – 287

20

Calmodulin-binding By similarity

Compositional bias

241 – 288

48

Arg-rich

Amino acid modifications

Modified residue

18

1

Phosphoserine By similarity

Natural variations

Natural variant

28

1

H → R. Ref.3 Ref.4
Corresponds to variant rs1006459 [ dbSNP | Ensembl ].

VAR_049498

Natural variant

45

1

R → W.
Corresponds to variant rs59730832 [ dbSNP | Ensembl ].

VAR_061232

Natural variant

59

1

P → A.
Corresponds to variant rs2233829 [ dbSNP | Ensembl ].

VAR_049499

Experimental info

Mutagenesis

94

1

T → N: No endothelial cell sprouting. Ref.2

Sequence conflict

209

1

E → V in AAC33132. Ref.1

Secondary structure

1

.

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298

Helix Strand Turn

Details...

Beta strand

80 – 86

7

Helix

93 – 101

9

Beta strand

112 – 123

12

Beta strand

126 – 133

8

Helix

145 – 149

5

Turn

150 – 152

3

Beta strand

155 – 162

8

Helix

166 – 181

16

Beta strand

190 – 195

6

Turn

200 – 202

3

Helix

207 – 217

11

Beta strand

219 – 223

5

Turn

226 – 229

4

Helix

232 – 247

16

Sequences

	Sequence		Length	Mass (Da)
	O75628 [UniParc]. Last modified November 7, 2003. Version 2. Checksum: E7CCE776FFD42CD7	FASTA	298	32,947
	10 20 30 40 50 60 MTLNTEQEAK TPLHRRASTP LPLSPRGHQP GRLSTVPSTQ SQHPRLGQSA SLNPPTQKPS 70 80 90 100 110 120 PAPDDWSSES SDSEGSWEAL YRVVLLGDPG VGKTSLASLF AGKQERDLHE QLGEDVYERT 130 140 150 160 170 180 LTVDGEDTTL VVVDTWEAEK LDKSWSQESC LQGGSAYVIV YSIADRGSFE SASELRIQLR 190 200 210 220 230 240 RTHQADHVPI ILVGNKADLA RCREVSVEEG RACAVVFDCK FIETSATLQH NVAELFEGVV 250 260 270 280 290 RQLRLRRRDS AAKEPPAPRR PASLAQRARR FLARLTARSA RRRALKARSK SCHNLAVL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the human Rem gene." Finlin B.S., Andres D.A. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Ges, a human GTPase of the Rad/Gem/Kir family, promotes endothelial cell sprouting and cytoskeleton reorganization." Pan J.Y., Fieles W.E., White A.M., Egerton M.M., Silberstein D.S. J. Cell Biol. 149:1107-1116(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF THR-94. Tissue: Lymph node.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-28.
[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], VARIANT ARG-28. Tissue: Caudate nucleus.
[5]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF084465 mRNA. Translation: AAC33132.1.
AF152863 mRNA. Translation: AAF74212.1.
BT020078 mRNA. Translation: AAV38881.1.
BT020079 mRNA. Translation: AAV38882.1.
AK313060 mRNA. Translation: BAG35890.1.
AL121751 Genomic DNA. Translation: CAB90274.1.
CH471077 Genomic DNA. Translation: EAW76439.1.
CH471077 Genomic DNA. Translation: EAW76440.1.
CH471077 Genomic DNA. Translation: EAW76442.1.
BC039813 mRNA. Translation: AAH39813.1.

IPI

IPI00289912.

RefSeq

NP_054731.2. NM_014012.4.

UniGene

Hs.247729.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NZJ	X-ray	2.50	A/B/C/D	79-251	[»]

ProteinModelPortal

O75628.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000201979.

PTM databases

PhosphoSite

O75628.

Proteomic databases

PaxDb

O75628.

PRIDE

O75628.

Protocols and materials databases

DNASU

28954.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000201979; ENSP00000201979; ENSG00000088320.

GeneID

28954.

KEGG

hsa:28954.

UCSC

uc002wwa.3. human.

Organism-specific databases

CTD

28954.

GeneCards

GC20P030063.

HGNC

HGNC:15922. REM1.

HPA

HPA049821.

MIM

610388. gene.

neXtProt

NX_O75628.

PharmGKB

PA34324.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000246961.

HOVERGEN

HBG104899.

InParanoid

O75628.

KO

K07847.

OMA

KLDESWS.

OrthoDB

EOG4G7C0D.

PhylomeDB

O75628.

Gene expression databases

Bgee

O75628.

CleanEx

HS_REM1.

Genevestigator

O75628.

GermOnline

ENSG00000088320. Homo sapiens.

Family and domain databases

InterPro

IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR017358. Small_GTPase_GEM/REM/Rad.
IPR020849. Small_GTPase_Ras.
[Graphical view]

PANTHER

PTHR24070. PTHR24070. 1 hit.

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PIRSF

PIRSF038017. GTP-binding_GEM. 1 hit.

PRINTS

PR00449. RASTRNSFRMNG.

SUPFAM

SSF52540. SSF52540. 1 hit.

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51421. RAS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O75628.

GenomeRNAi

28954.

NextBio

51769.

SOURCE

Search...

Entry information

Entry name

REM1_HUMAN

Accession

Primary (citable) accession number: O75628
Secondary accession number(s): E1P5L1 , Q5TZR7, Q5TZR8, Q9NP57

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	November 7, 2003
Last modified:	May 29, 2013
This is version 115 of the entry and version 2 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.