Q6NW40 (RGMB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RGM domain family member B

Alternative name(s):
DRG11-responsive axonal guidance and outgrowth of neurite
Short name=DRAGON

Gene names

Name:

RGMB

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	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Member of the repulsive guidance molecule (RGM) family that contributes to the patterning of the developing nervous system By similarity. Acts as a bone morphogenetic protein (BMP) coreceptor that potentiates BMP signaling By similarity. Promotes neuronal adhesion By similarity. May inhibit neurite outgrowth. Ref.4
Subunit structure	Homooligomer By similarity. Interacts with DRGX By similarity. Interacts with BMP2 and BMP4 By similarity. Interacts with the BMP type I receptors ACVR1, BMPR1A and BMPR1B and with the BMP type II receptor ACVR2B By similarity.
Subcellular location	Cell membrane; Lipid-anchor › GPI-anchor By similarity. Membrane raft By similarity.
Post-translational modification	GPI-anchored By similarity.
Sequence similarities	Belongs to the repulsive guidance molecule (RGM) family.
Sequence caution	The sequence AAH67736.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence BAC11268.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Signal
PTM	GPI-anchor Glycoprotein Lipoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	BMP signaling pathway Inferred from sequence or structural similarity. Source: HGNC axon guidance Traceable author statement. Source: Reactome cell adhesion Inferred from sequence or structural similarity. Source: HGNC positive regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: HGNC
Cellular component	anchored to plasma membrane Inferred from sequence or structural similarity. Source: HGNC endoplasmic reticulum-Golgi intermediate compartment Inferred from sequence or structural similarity. Source: HGNC membrane raft Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	identical protein binding Inferred from sequence or structural similarity. Source: HGNC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 45	45	Potential
	Chain	46 – 413	368	RGM domain family member B		PRO_0000030394
	Propeptide	414 – 437	24	Removed in mature form Potential		PRO_0000030395
Amino acid modifications
	Lipidation	413	1	GPI-anchor amidated asparagine Potential
	Glycosylation	120	1	N-linked (GlcNAc...) Potential
	Glycosylation	383	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	22	1	S → R in AAH67736. Ref.3
	Sequence conflict	225	1	E → G in AAH67736. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q6NW40 [UniParc]. Last modified April 5, 2011. Version 3. Checksum: 48C26166E68DCE5F	FASTA	437	47,547
	10 20 30 40 50 60 MGLRAAPSSA AAAAAEVEQR RSPGLCPPPL ELLLLLLFSL GLLHAGDCQQ PAQCRIQKCT 70 80 90 100 110 120 TDFVSLTSHL NSAVDGFDSE FCKALRAYAG CTQRTSKACR GNLVYHSAVL GISDLMSQRN 130 140 150 160 170 180 CSKDGPTSST NPEVTHDPCN YHSHAGAREH RRGDQNPPSY LFCGLFGDPH LRTFKDNFQT 190 200 210 220 230 240 CKVEGAWPLI DNNYLSVQVT NVPVVPGSSA TATNKITIIF KAHHECTDQK VYQAVTDDLP 250 260 270 280 290 300 AAFVDGTTSG GDSDAKSLRI VERESGHYVE MHARYIGTTV FVRQVGRYLT LAIRMPEDLA 310 320 330 340 350 360 MSYEESQDLQ LCVNGCPLSE RIDDGQGQVS AILGHSLPRT SLVQAWPGYT LETANTQCHE 370 380 390 400 410 420 KMPVKDIYFQ SCVFDLLTTG DANFTAAAHS ALEDVEALHP RKERWHIFPS SGNGTPRGGS 430 DLSVSLGLTC LILIVFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]	"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: 15372022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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: Placenta.
[4]	"Repulsive guidance molecule b inhibits neurite growth and is increased after spinal cord injury." Liu X., Hashimoto M., Horii H., Yamaguchi A., Naito K., Yamashita T. Biochem. Biophys. Res. Commun. 382:795-800(2009) [PubMed: 19324014] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK074887 mRNA. Translation: BAC11268.1. Sequence problems. AC008522 Genomic DNA. No translation available. BC067736 mRNA. Translation: AAH67736.1. Different initiation.
IPI	IPI00963921.
RefSeq	NP_001012779.2. NM_001012761.2.
UniGene	Hs.526902.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6NW40.
Polymorphism databases
DMDM	51316243.
Proteomic databases
PRIDE	Q6NW40.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000308234; ENSP00000308219; ENSG00000174136. ENST00000513185; ENSP00000423256; ENSG00000174136.
GeneID	285704.
KEGG	hsa:285704.
UCSC	uc003knb.1. human. uc003knc.1. human.
Organism-specific databases
CTD	285704.
GeneCards	GC05P098132.
HGNC	HGNC:26896. RGMB.
HPA	HPA016993.
MIM	612687. gene.
neXtProt	NX_Q6NW40.
PharmGKB	PA134868641.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15941.
GeneTree	ENSGT00390000008488.
HOGENOM	HBG505677.
HOVERGEN	HBG057627.
InParanoid	Q6NW40.
OrthoDB	EOG4GHZNX.
Enzyme and pathway databases
Pathway_Interaction_DB	bmppathway. BMP receptor signaling.
Reactome	REACT_111045. Developmental Biology.
Gene expression databases
ArrayExpress	Q6NW40.
Bgee	Q6NW40.
CleanEx	HS_RGMB.
Genevestigator	Q6NW40.
GermOnline	ENSG00000174136. Homo sapiens.
Family and domain databases
InterPro	IPR009496. RGM_C. IPR010536. RGM_N. [Graphical view]
KO	K06847.
Pfam	PF06534. RGM_C. 1 hit. PF06535. RGM_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	95719.
SOURCE	Search...

Entry information

Entry name

RGMB_HUMAN

Accession

Primary (citable) accession number: Q6NW40
Secondary accession number(s): D6R9A0, Q8NC92

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	April 5, 2011
Last modified:	January 25, 2012
This is version 63 of the entry and version 3 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.