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Q6GQT9 (NOMO1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nodal modulator 1
Gene names
Name:Nomo1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1214 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May antagonize Nodal signaling By similarity. UniProtKB Q5JPE7

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Sequence caution

The sequence AAH24503.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAH33923.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC38713.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentMembrane
   DomainCoiled coil
Signal
Transmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 12141191Nodal modulator 1
PRO_0000396822

Regions

Topological domain24 – 11501127Extracellular Potential
Transmembrane1151 – 116717Helical; Potential
Topological domain1168 – 121447Cytoplasmic Potential
Coiled coil692 – 72029 Potential

Amino acid modifications

Modified residue11961Phosphoserine Ref.3
Modified residue11971Phosphoserine Ref.3
Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation2101N-linked (GlcNAc...) Potential
Glycosylation6101N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict61C → G in BAC38508. Ref.1
Sequence conflict62 – 632DC → GW in BAC38508. Ref.1
Sequence conflict751Y → V in BAC38508. Ref.1
Sequence conflict95 – 973TNV → PHG in BAC38508. Ref.1
Sequence conflict1011V → G in BAC38508. Ref.1
Sequence conflict1091T → A in BAC38508. Ref.1
Sequence conflict1131D → G in BAC38508. Ref.1
Sequence conflict4771P → T in BAC38508. Ref.1
Sequence conflict875 – 8784KAED → GRVG in AAH24503. Ref.2
Sequence conflict10291E → G in BAC31513. Ref.1
Sequence conflict11761L → V in BAC31513. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6GQT9 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 0F71587617C444A7

FASTA1,214133,420
        10         20         30         40         50         60 
MRAGRCAAAL LLLLLSGAGR AIGSEDIVVG CGGFVKSDVE INYSLIEIKL YTKHGTLKYQ 

        70         80         90        100        110        120 
TDCAPNNGYF MIPLYDKGDF ILKIEPPLGW SFEPTNVELR VDGVSDICTK GGDINFLFTG 

       130        140        150        160        170        180 
FSVNGKVLSK GQPLGPAGVQ VSLRSTGADS KIQSTVTQPG GKFAFFKVLP GDYEILATHP 

       190        200        210        220        230        240 
TWALKEASTT VRVTNSNANA AGPLIVAGYN VSGSVRSDGE PMKGVKFLLF SSLVNKEDVL 

       250        260        270        280        290        300 
GCNVSPVSGF QPPDESLVYL CYAVSKEDGS FSFYSLPSGG YTVVPFYRGE RITFDVAPSR 

       310        320        330        340        350        360 
LDFTVEHDSL RIEPVFHVMG FSVTGRVLNG PDGEGVPEAV VTLNNQIKVK TKADGSFRLE 

       370        380        390        400        410        420 
NITTGTYTIH AQKEHLYFEM VTIKIAPNTP QLADLIATGF SICGQIAIVR SPDTIKQMSK 

       430        440        450        460        470        480 
YRVVLSSQDK DKALLTVDSD AHGSFCFKAK PGAYKVQVVV PEAETRAGLM LKPQVFPLTV 

       490        500        510        520        530        540 
TNRPVMDVAF VQFLASVSGK VSCLDTCGDL LVTLQSLSRQ GEKRSLQLSG KVNSMTFTFD 

       550        560        570        580        590        600 
KVLPGRYKIS IMHEDWCWRN KSLEVEVLED DVSAVEFRQT GYMLRCALSH AITLEFHQDG 

       610        620        630        640        650        660 
NGPENVGIYN LSRGVNRFCL SKPGVYKVTP RSCHRFEQAF YTYDTSSPSI LTLTAIRHHV 

       670        680        690        700        710        720 
LGTIITDKMM DVTVTIKSSI DSEPALVLGP LKSAQELRRE QQLAEIETRR QEREKNGKEE 

       730        740        750        760        770        780 
GEEGRARPPG QEMVDELQGP FSYDFSYWAR SGEKITVTPS SKELLFYPPS MEATVSGESC 

       790        800        810        820        830        840 
PGKLIEIHGK AGLFLEGQIH PELEGVEIVI SEKGASSPLI TVFTDDKGAY SVGPLHSDLE 

       850        860        870        880        890        900 
YTVNSQKEGY VLTAVEGTVG DFKAYALAGV SFEIKAEDDQ PLPGVLLSLS GGVFRSNLLT 

       910        920        930        940        950        960 
QDNGILTFSN LSPGQYYFKP MMKEFRFEPS SQMIEVQEGQ NLRITITGFR TAYSCYGTVS 

       970        980        990       1000       1010       1020 
SLNGEPEQGV AVEAVGQKDC SIYGEDTVTD EEGKFRLRGL LPGCMYHVQL KAEGNDHIER 

      1030       1040       1050       1060       1070       1080 
ALPHHRVIEV GNNDVDDVNI IVFRQINQFD LSGNVITSSE YLSTLWVKLY KSESLDNPIQ 

      1090       1100       1110       1120       1130       1140 
TVSLGQSLFF HFPPLLRDGE NYVVLLDTTL PRSQYDYVLP QVSFTAVGYH KHITLVFSPT 

      1150       1160       1170       1180       1190       1200 
RKLPEQDIAQ GSYIALPLTL LLLLAGYNHD KLIPLLLQLT SRLQGVRALG QAASDSSGPE 

      1210 
DMKRQTKKQK TRRT 

« Hide

References

[1]"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. expand/collapse author list , 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.
Tissue: Blastocyst, Cerebellum and Embryonic spinal cord.
[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: C57BL/6 and FVB/N.
Tissue: Brain, Colon and Liver.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1196 AND SER-1197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK043279 mRNA. Translation: BAC31513.1.
AK082495 mRNA. Translation: BAC38508.1.
AK082963 mRNA. Translation: BAC38713.1. Different initiation.
AK166764 mRNA. Translation: BAE39002.1.
BC024503 mRNA. Translation: AAH24503.1. Different initiation.
BC033923 mRNA. Translation: AAH33923.1. Different initiation.
BC072630 mRNA. Translation: AAH72630.1.
CCDSCCDS21273.1.
RefSeqNP_694697.3. NM_153057.4.
UniGeneMm.274811.

3D structure databases

ProteinModelPortalQ6GQT9.
SMRQ6GQT9. Positions 66-93, 123-179, 263-289, 322-390, 420-462, 507-555, 823-850, 869-944, 954-1042.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229243. 1 interaction.
IntActQ6GQT9. 2 interactions.
MINTMINT-4110969.
STRING10090.ENSMUSP00000033121.

PTM databases

PhosphoSiteQ6GQT9.

Proteomic databases

MaxQBQ6GQT9.
PaxDbQ6GQT9.
PRIDEQ6GQT9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033121; ENSMUSP00000033121; ENSMUSG00000030835.
GeneID211548.
KEGGmmu:211548.
UCSCuc009gyb.2. mouse.

Organism-specific databases

CTD23420.
MGIMGI:2385850. Nomo1.

Phylogenomic databases

eggNOGNOG237157.
GeneTreeENSGT00390000000089.
HOVERGENHBG071511.
InParanoidQ8R1I7.
OMAEFSYWAR.
OrthoDBEOG77M8NC.
PhylomeDBQ6GQT9.
TreeFamTF313696.

Gene expression databases

BgeeQ6GQT9.
GenevestigatorQ6GQT9.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.1120. 2 hits.
InterProIPR013784. Carb-bd-like_fold.
IPR008969. CarboxyPept-like_regulatory.
IPR014766. CarboxyPept_regulatory_dom.
IPR013783. Ig-like_fold.
[Graphical view]
SUPFAMSSF49452. SSF49452. 3 hits.
SSF49464. SSF49464. 1 hit.
ProtoNetSearch...

Other

NextBio373278.
PROQ6GQT9.
SOURCESearch...

Entry information

Entry nameNOMO1_MOUSE
AccessionPrimary (citable) accession number: Q6GQT9
Secondary accession number(s): Q3TKZ1 expand/collapse secondary AC list , Q8BJM1, Q8BJM8, Q8BLS9, Q8K074, Q8R1I7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot