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Q148V8 (FA83H_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Protein FAM83H
Gene names
Name:Fam83h
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1209 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a major role in the structural organization and calcification of developing enamel By similarity.

Tissue specificity

Expressed in tooth follicle, eye, liver and kidney. Ref.4

Sequence similarities

Belongs to the FAM83 family.

Sequence caution

The sequence AAH36149.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processBiomineralization
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbiomineral tissue development

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12091209Protein FAM83H
PRO_0000324489

Amino acid modifications

Modified residue5221Phosphoserine Ref.6
Modified residue6391Phosphoserine By similarity
Modified residue7521Phosphoserine By similarity
Modified residue7781Phosphoserine By similarity
Modified residue8711Phosphoserine Ref.5
Modified residue8731Phosphothreonine By similarity
Modified residue8821Phosphoserine Ref.5
Modified residue8931Phosphoserine Ref.5
Modified residue9041Phosphoserine Ref.6
Modified residue9151Phosphoserine Ref.6
Modified residue9261Phosphoserine Ref.3
Modified residue9371Phosphoserine By similarity
Modified residue9481Phosphoserine Ref.6
Modified residue9591Phosphoserine Ref.6
Modified residue9701Phosphoserine Ref.6
Modified residue9771Phosphoserine By similarity
Modified residue10351Phosphoserine By similarity
Modified residue10571Phosphoserine By similarity
Modified residue10721Phosphothreonine By similarity
Modified residue10801Phosphoserine By similarity

Experimental info

Sequence conflict8731T → A in BAC29093. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q148V8 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 1954B609EA75EF25

FASTA1,209131,115
        10         20         30         40         50         60 
MARRSQSSSQ GDNPLAPGYL PPHYKEYYRL AVDALTEGGP EAYNRFLASE GAPDFLCPEE 

        70         80         90        100        110        120 
LEHVSRHLQP PQYVAREPPE GTPSDVDMDG SSGTYWPVNS DQAVPELDLG WPLTFGFQGT 

       130        140        150        160        170        180 
EVTTLVQPPP PDSPSIKDEA RRMIRSAQQV VAVVMDMFTD VDLLSEVLEA AARRVPVYIL 

       190        200        210        220        230        240 
LDEMNAQHFL DMADKCRVNL HHVDFLRVRT VAGPTYYCRT GKSFKGHLKE KFLLVDCAVV 

       250        260        270        280        290        300 
MSGSYSFMWS FEKIHRSLAH VFQGELVSSF DEEFRILFAQ SEPLVPSAGA LARMDAYALA 

       310        320        330        340        350        360 
PYSGAGPLVG VPGVGAPTPF SFPKRAHLLF PPPREEGLGF PSFLDPDRHF LSAFRREELQ 

       370        380        390        400        410        420 
RMPGGALEPH TGLRPLARPT EAGPFGELAG PRGFFQSRHL EMDAFKRHSY ATPDGAGAVE 

       430        440        450        460        470        480 
NFAAARQVSR QTFLSHGDDF RFQTSHFQRD QLYQQHYQWD PQFAPARPQG LFEKLRAGRP 

       490        500        510        520        530        540 
GFADPDDFAL GAGHRFPELG ADVHQRLEYV PSSASREVRH GSDPAFGPSP RGLEPSGASR 

       550        560        570        580        590        600 
PNLGQRFPCQ ATLRQGLDTA SEAEPERRGG PEGRAGLRHW RLASYLSGCH GDGGEEGLPM 

       610        620        630        640        650        660 
EAEACEDEVL APGGRDLLPS AFRTPAAFPA KGPKPGSGSG GGDSSEREGP EETSLAKQDS 

       670        680        690        700        710        720 
FRSRLNPLIQ RSSRLRSSLI FASQAEGAVG TAAATTEKVQ LMHKEQTVSE TLGPSGEAVR 

       730        740        750        760        770        780 
SSASAKVAEL LEKYKGPARD PGGAGGAVTS SSHSKAVVSQ AWREEVVAPG GAGTERRSLE 

       790        800        810        820        830        840 
SCLLDLRDSF AQQLHQEAER HPGAASLTAA QLLDTLGGTD RLPSRFLSAQ GRSLSPQGRD 

       850        860        870        880        890        900 
SPPPEGLGTH QLPYSEPKGN PTPAYPERKG SPTPAYPERK GSPTPAYPER KGSPTPAYPE 

       910        920        930        940        950        960 
RKGSPTQAYP ERKGSPTSGF PNRRGSPTTG LMEQKGSPTS TYPDRRGSPV PPVPERRGSP 

       970        980        990       1000       1010       1020 
VPPVPERRGS LTFAGESSKT GPTEEVSSGP MEVLRKGSLR LRQLLSPKNE RRGEDEGSFP 

      1030       1040       1050       1060       1070       1080 
TPQENGQPES PRRPSLSRGD STEAAAEERG SRVRLASATA NALYSSNLRD DTKAILEQIS 

      1090       1100       1110       1120       1130       1140 
AHGQKHRGVP APGPAHSSPD VGRPTTAGDL APDMSDKDKC SAIFRSDSLG TQGRLSRTLP 

      1150       1160       1170       1180       1190       1200 
GSAEERDRLL RRMESMRKEK RVYSRFEVFC KKDEAGSSGA GDNLADEDTR DSKMGKFVPK 


ILGTFKSKK 

« Hide

References

« Hide 'large scale' 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: Urinary bladder.
[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: Czech II and FVB/N.
Tissue: Mammary tumor.
[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-926, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"FAM83H mutations in families with autosomal-dominant hypocalcified amelogenesis imperfecta."
Kim J.-W., Lee S.-K., Lee Z.H., Park J.-C., Lee K.-E., Lee M.-H., Park J.-T., Seo B.-M., Hu J.C.-C., Simmer J.P.
Am. J. Hum. Genet. 82:489-494(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871; SER-882 AND SER-893, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[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-522; SER-904; SER-915; SER-948; SER-959 AND SER-970, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK035531 mRNA. Translation: BAC29093.1.
BC022937 mRNA. Translation: AAH22937.1.
BC023045 mRNA. Translation: AAH23045.1.
BC036149 mRNA. Translation: AAH36149.1. Different initiation.
BC117947 mRNA. Translation: AAI17948.1.
BC117948 mRNA. Translation: AAI17949.1.
CCDSCCDS27559.1.
RefSeqNP_001161725.1. NM_001168253.1.
NP_598848.2. NM_134087.2.
XP_006520300.1. XM_006520237.1.
UniGeneMm.267178.

3D structure databases

ProteinModelPortalQ148V8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid222906. 1 interaction.
IntActQ148V8. 2 interactions.

PTM databases

PhosphoSiteQ148V8.

Proteomic databases

MaxQBQ148V8.
PaxDbQ148V8.
PRIDEQ148V8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000060807; ENSMUSP00000059839; ENSMUSG00000046761.
ENSMUST00000170153; ENSMUSP00000126453; ENSMUSG00000046761.
GeneID105732.
KEGGmmu:105732.
UCSCuc007wic.2. mouse.

Organism-specific databases

CTD286077.
MGIMGI:2145900. Fam83h.

Phylogenomic databases

eggNOGNOG78323.
GeneTreeENSGT00740000115020.
HOGENOMHOG000112488.
HOVERGENHBG107907.
InParanoidQ148V8.
OMAARHLEMD.
OrthoDBEOG7P2XR9.
PhylomeDBQ148V8.
TreeFamTF330777.

Gene expression databases

BgeeQ148V8.
CleanExMM_AA409316.
GenevestigatorQ148V8.

Family and domain databases

InterProIPR012461. DUF1669.
[Graphical view]
PANTHERPTHR16181. PTHR16181. 1 hit.
PfamPF07894. DUF1669. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFAM83H. mouse.
NextBio357852.
PROQ148V8.
SOURCESearch...

Entry information

Entry nameFA83H_MOUSE
AccessionPrimary (citable) accession number: Q148V8
Secondary accession number(s): Q8BZF6 expand/collapse secondary AC list , Q8CI79, Q8R5C2, Q8R5D0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: August 22, 2006
Last modified: July 9, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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