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Protein

Transmembrane glycoprotein NMB

Gene

Gpnmb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Could be a melanogenic enzyme.By similarity

GO - Molecular functioni

  • heparin binding Source: MGI
  • integrin binding Source: MGI

GO - Biological processi

  • bone mineralization Source: Ensembl
  • cell adhesion Source: MGI
  • negative regulation of tumor necrosis factor production Source: CACAO
  • osteoblast differentiation Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Transmembrane glycoprotein NMB
Alternative name(s):
DC-HIL
Dendritic cell-associated transmembrane protein
Osteoactivin
Gene namesi
Name:Gpnmb
Synonyms:Dchil, Hgfin, Nmb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1934765. Gpnmb.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 502480ExtracellularSequence AnalysisAdd
BLAST
Transmembranei503 – 52321HelicalSequence AnalysisAdd
BLAST
Topological domaini524 – 57451CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasmic membrane-bounded vesicle Source: MGI
  • cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  • endomembrane system Source: UniProtKB-SubCell
  • integral component of plasma membrane Source: MGI
  • melanosome Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Involvement in diseasei

May promote bone metastatic phenotype when overexpressed in breast cancer cells.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 574552Transmembrane glycoprotein NMBPRO_0000024710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi93 – 931N-linked (GlcNAc...)Sequence Analysis
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi296 – 2961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi306 – 3061N-linked (GlcNAc...)Sequence Analysis
Glycosylationi312 – 3121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence Analysis
Modified residuei546 – 5461Phosphoserine1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ99P91.
PRIDEiQ99P91.

PTM databases

PhosphoSiteiQ99P91.

Expressioni

Tissue specificityi

In early development, mRNA is detected at high levels in the outer layer of the retina. Later in development expression gets restricted to the retinal pigment epithelium and iris. Overexpressed in mammary cancer cells possessing a strong bone metastatic phenotype.1 Publication

Gene expression databases

BgeeiQ99P91.
CleanExiMM_GPNMB.
MM_NMB.
ExpressionAtlasiQ99P91. baseline and differential.
GenevisibleiQ99P91. MM.

Interactioni

Protein-protein interaction databases

IntActiQ99P91. 1 interaction.
STRINGi10090.ENSMUSP00000031840.

Structurei

3D structure databases

ProteinModelPortaliQ99P91.
SMRiQ99P91. Positions 258-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini250 – 33889PKDPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi558 – 5603Cell attachment siteSequence Analysis

Sequence similaritiesi

Belongs to the PMEL/NMB family.Curated
Contains 1 PKD domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG40272.
GeneTreeiENSGT00530000063573.
HOGENOMiHOG000252941.
HOVERGENiHBG051797.
InParanoidiQ99P91.
OMAiFPGNQEK.
OrthoDBiEOG7GXPB9.
TreeFamiTF334865.

Family and domain databases

Gene3Di2.60.40.670. 1 hit.
InterProiIPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
[Graphical view]
PfamiPF00801. PKD. 1 hit.
[Graphical view]
SMARTiSM00089. PKD. 1 hit.
[Graphical view]
SUPFAMiSSF49299. SSF49299. 1 hit.
PROSITEiPS50093. PKD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q99P91-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESLCGVLGF LLLAAGLPLQ AAKRFRDVLG HEQYPDHMRE HNQLRGWSSD
60 70 80 90 100
ENEWDEHLYP VWRRGDGRWK DSWEGGRVQA VLTSDSPALV GSNITFVVNL
110 120 130 140 150
VFPRCQKEDA NGNIVYEKNC RNDLGLTSDL HVYNWTAGAD DGDWEDGTSR
160 170 180 190 200
SQHLRFPDRR PFPRPHGWKK WSFVYVFHTL GQYFQKLGRC SARVSINTVN
210 220 230 240 250
LTAGPQVMEV TVFRRYGRAY IPISKVKDVY VITDQIPVFV TMSQKNDRNL
260 270 280 290 300
SDEIFLRDLP IVFDVLIHDP SHFLNDSAIS YKWNFGDNTG LFVSNNHTLN
310 320 330 340 350
HTYVLNGTFN LNLTVQTAVP GPCPPPSPST PPPPSTPPSP PPSPLPTLST
360 370 380 390 400
PSPSLMPTGY KSMELSDISN ENCRINRYGY FRATITIVEG ILEVSIMQIA
410 420 430 440 450
DVPMPTPQPA NSLMDFTVTC KGATPMEACT IISDPTCQIA QNRVCSPVAV
460 470 480 490 500
DGLCLLSVRR AFNGSGTYCV NFTLGDDASL ALTSTLISIP GKDPDSPLRA
510 520 530 540 550
VNGVLISIGC LAVLVTMVTI LLYKKHKAYK PIGNCPRNTV KGKGLSVLLS
560 570
HAKAPFFRGD QEKDPLLQDK PRTL
Length:574
Mass (Da):63,676
Last modified:July 27, 2011 - v2
Checksum:iB6AE99DD5DB7C6D0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361D → N in AAK14240 (PubMed:11114299).Curated
Sequence conflicti36 – 361D → N in BAC32074 (PubMed:16141072).Curated
Sequence conflicti36 – 361D → N in AAH26375 (PubMed:15489334).Curated
Sequence conflicti333 – 3331P → S in CAB65272 (PubMed:12638126).Curated
Sequence conflicti339 – 3413SPP → LPS in CAB65272 (PubMed:12638126).Curated
Sequence conflicti498 – 4981L → M in BAC32074 (PubMed:16141072).Curated
Sequence conflicti541 – 5411K → E in BAC32074 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF322054 mRNA. Translation: AAK14240.1.
AJ251685 mRNA. Translation: CAB65272.1.
AK044764 mRNA. Translation: BAC32074.1.
AK076347 mRNA. Translation: BAC36306.1.
AK150739 mRNA. Translation: BAE29813.1.
AK154617 mRNA. Translation: BAE32716.1.
AK170506 mRNA. Translation: BAE41844.1.
AK171441 mRNA. Translation: BAE42454.1.
AK171465 mRNA. Translation: BAE42471.1.
AK171474 mRNA. Translation: BAE42479.1.
AK171517 mRNA. Translation: BAE42501.1.
BC026375 mRNA. Translation: AAH26375.1.
CCDSiCCDS20122.1.
RefSeqiNP_444340.3. NM_053110.4.
UniGeneiMm.302602.

Genome annotation databases

EnsembliENSMUST00000031840; ENSMUSP00000031840; ENSMUSG00000029816.
GeneIDi93695.
KEGGimmu:93695.
UCSCiuc012elo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF322054 mRNA. Translation: AAK14240.1.
AJ251685 mRNA. Translation: CAB65272.1.
AK044764 mRNA. Translation: BAC32074.1.
AK076347 mRNA. Translation: BAC36306.1.
AK150739 mRNA. Translation: BAE29813.1.
AK154617 mRNA. Translation: BAE32716.1.
AK170506 mRNA. Translation: BAE41844.1.
AK171441 mRNA. Translation: BAE42454.1.
AK171465 mRNA. Translation: BAE42471.1.
AK171474 mRNA. Translation: BAE42479.1.
AK171517 mRNA. Translation: BAE42501.1.
BC026375 mRNA. Translation: AAH26375.1.
CCDSiCCDS20122.1.
RefSeqiNP_444340.3. NM_053110.4.
UniGeneiMm.302602.

3D structure databases

ProteinModelPortaliQ99P91.
SMRiQ99P91. Positions 258-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99P91. 1 interaction.
STRINGi10090.ENSMUSP00000031840.

PTM databases

PhosphoSiteiQ99P91.

Proteomic databases

MaxQBiQ99P91.
PRIDEiQ99P91.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031840; ENSMUSP00000031840; ENSMUSG00000029816.
GeneIDi93695.
KEGGimmu:93695.
UCSCiuc012elo.1. mouse.

Organism-specific databases

CTDi10457.
MGIiMGI:1934765. Gpnmb.

Phylogenomic databases

eggNOGiNOG40272.
GeneTreeiENSGT00530000063573.
HOGENOMiHOG000252941.
HOVERGENiHBG051797.
InParanoidiQ99P91.
OMAiFPGNQEK.
OrthoDBiEOG7GXPB9.
TreeFamiTF334865.

Miscellaneous databases

ChiTaRSiGpnmb. mouse.
NextBioi351449.
PROiQ99P91.
SOURCEiSearch...

Gene expression databases

BgeeiQ99P91.
CleanExiMM_GPNMB.
MM_NMB.
ExpressionAtlasiQ99P91. baseline and differential.
GenevisibleiQ99P91. MM.

Family and domain databases

Gene3Di2.60.40.670. 1 hit.
InterProiIPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
[Graphical view]
PfamiPF00801. PKD. 1 hit.
[Graphical view]
SMARTiSM00089. PKD. 1 hit.
[Graphical view]
SUPFAMiSSF49299. SSF49299. 1 hit.
PROSITEiPS50093. PKD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of a dendritic cell-associated transmembrane protein, DC-HIL, that promotes RGD-dependent adhesion of endothelial cells through recognition of heparan sulfate proteoglycans."
    Shikano S., Bonkobara M., Zukas P.K., Ariizumi K.
    J. Biol. Chem. 276:8125-8134(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "mRNA expression of the murine glycoprotein (transmembrane) nmb (Gpnmb) gene is linked to the developing retinal pigment epithelium and iris."
    Bachner D., Schroder D., Gross G.
    Gene Expr. Patterns 1:159-165(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  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].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Retina and Skin.
  4. "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.
    Tissue: Salivary gland.
  5. Cited for: DISEASE.
  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-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGPNMB_MOUSE
AccessioniPrimary (citable) accession number: Q99P91
Secondary accession number(s): Q3U3R9
, Q8BVV9, Q8BXL4, Q9QXA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.