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Protein

Protein FAM83H

Gene

Fam83h

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May play a major role in the structural organization and calcification of developing enamel. May play a role in keratin cytoskeleton disassembly by recruiting CSNK1A1 to keratin filaments. Thereby, it may regulate epithelial cell migration.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Biomineralization

Names & Taxonomyi

Protein namesi
Recommended name:
Protein FAM83HCurated
Gene namesi
Name:Fam83hImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:2145900. Fam83h.

Subcellular locationi

  • Cytoplasmcytoskeleton By similarity

  • Note: Colocalizes with keratin filaments.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12091209Protein FAM83HPRO_0000324489Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei512 – 5121PhosphoserineBy similarity
Modified residuei513 – 5131PhosphoserineBy similarity
Modified residuei515 – 5151PhosphoserineBy similarity
Modified residuei522 – 5221PhosphoserineCombined sources
Modified residuei639 – 6391PhosphoserineBy similarity
Modified residuei660 – 6601PhosphoserineBy similarity
Modified residuei749 – 7491PhosphothreonineBy similarity
Modified residuei752 – 7521PhosphoserineBy similarity
Modified residuei778 – 7781PhosphoserineBy similarity
Modified residuei806 – 8061PhosphoserineBy similarity
Modified residuei871 – 8711PhosphoserineCombined sources
Modified residuei873 – 8731PhosphothreonineBy similarity
Modified residuei882 – 8821PhosphoserineCombined sources
Modified residuei893 – 8931PhosphoserineCombined sources
Modified residuei904 – 9041PhosphoserineCombined sources
Modified residuei915 – 9151PhosphoserineCombined sources
Modified residuei917 – 9171PhosphothreonineCombined sources
Modified residuei926 – 9261PhosphoserineCombined sources
Modified residuei928 – 9281PhosphothreonineCombined sources
Modified residuei937 – 9371PhosphoserineBy similarity
Modified residuei948 – 9481PhosphoserineCombined sources
Modified residuei959 – 9591PhosphoserineCombined sources
Modified residuei970 – 9701PhosphoserineCombined sources
Modified residuei977 – 9771PhosphoserineBy similarity
Modified residuei1035 – 10351PhosphoserineBy similarity
Modified residuei1041 – 10411PhosphoserineCombined sources
Modified residuei1057 – 10571PhosphoserineBy similarity
Modified residuei1072 – 10721PhosphothreonineBy similarity
Modified residuei1080 – 10801PhosphoserineBy similarity
Modified residuei1098 – 10981PhosphoserineBy similarity
Modified residuei1177 – 11771PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ148V8.
PaxDbiQ148V8.
PeptideAtlasiQ148V8.
PRIDEiQ148V8.

PTM databases

iPTMnetiQ148V8.
PhosphoSiteiQ148V8.

Expressioni

Tissue specificityi

Expressed in tooth follicle, eye, liver and kidney.1 Publication

Gene expression databases

BgeeiQ148V8.
CleanExiMM_AA409316.
GenevisibleiQ148V8. MM.

Interactioni

Subunit structurei

Interacts with CSNK1A1; recruits CSNK1A1 to keratin filaments. Interacts with KRT18 and probably other keratins.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi222906. 1 interaction.
IntActiQ148V8. 2 interactions.
STRINGi10090.ENSMUSP00000059839.

Structurei

3D structure databases

ProteinModelPortaliQ148V8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 286286Mediates interaction with CSNK1A1 and is required for FAM83H activity in keratin cytoskeleton organizationBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the FAM83 family.Curated

Phylogenomic databases

eggNOGiENOG410IEPN. Eukaryota.
ENOG410YB0T. LUCA.
GeneTreeiENSGT00760000119168.
HOGENOMiHOG000112488.
HOVERGENiHBG107907.
InParanoidiQ148V8.
OMAiGFFQARH.
OrthoDBiEOG7P2XR9.
PhylomeDBiQ148V8.
TreeFamiTF330777.

Family and domain databases

InterProiIPR012461. DUF1669.
[Graphical view]
PANTHERiPTHR16181. PTHR16181. 5 hits.
PfamiPF07894. DUF1669. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q148V8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARRSQSSSQ GDNPLAPGYL PPHYKEYYRL AVDALTEGGP EAYNRFLASE
60 70 80 90 100
GAPDFLCPEE LEHVSRHLQP PQYVAREPPE GTPSDVDMDG SSGTYWPVNS
110 120 130 140 150
DQAVPELDLG WPLTFGFQGT EVTTLVQPPP PDSPSIKDEA RRMIRSAQQV
160 170 180 190 200
VAVVMDMFTD VDLLSEVLEA AARRVPVYIL LDEMNAQHFL DMADKCRVNL
210 220 230 240 250
HHVDFLRVRT VAGPTYYCRT GKSFKGHLKE KFLLVDCAVV MSGSYSFMWS
260 270 280 290 300
FEKIHRSLAH VFQGELVSSF DEEFRILFAQ SEPLVPSAGA LARMDAYALA
310 320 330 340 350
PYSGAGPLVG VPGVGAPTPF SFPKRAHLLF PPPREEGLGF PSFLDPDRHF
360 370 380 390 400
LSAFRREELQ RMPGGALEPH TGLRPLARPT EAGPFGELAG PRGFFQSRHL
410 420 430 440 450
EMDAFKRHSY ATPDGAGAVE NFAAARQVSR QTFLSHGDDF RFQTSHFQRD
460 470 480 490 500
QLYQQHYQWD PQFAPARPQG LFEKLRAGRP GFADPDDFAL GAGHRFPELG
510 520 530 540 550
ADVHQRLEYV PSSASREVRH GSDPAFGPSP RGLEPSGASR PNLGQRFPCQ
560 570 580 590 600
ATLRQGLDTA SEAEPERRGG PEGRAGLRHW RLASYLSGCH GDGGEEGLPM
610 620 630 640 650
EAEACEDEVL APGGRDLLPS AFRTPAAFPA KGPKPGSGSG GGDSSEREGP
660 670 680 690 700
EETSLAKQDS FRSRLNPLIQ RSSRLRSSLI FASQAEGAVG TAAATTEKVQ
710 720 730 740 750
LMHKEQTVSE TLGPSGEAVR SSASAKVAEL LEKYKGPARD PGGAGGAVTS
760 770 780 790 800
SSHSKAVVSQ AWREEVVAPG GAGTERRSLE SCLLDLRDSF AQQLHQEAER
810 820 830 840 850
HPGAASLTAA QLLDTLGGTD RLPSRFLSAQ GRSLSPQGRD SPPPEGLGTH
860 870 880 890 900
QLPYSEPKGN PTPAYPERKG SPTPAYPERK GSPTPAYPER KGSPTPAYPE
910 920 930 940 950
RKGSPTQAYP ERKGSPTSGF PNRRGSPTTG LMEQKGSPTS TYPDRRGSPV
960 970 980 990 1000
PPVPERRGSP VPPVPERRGS LTFAGESSKT GPTEEVSSGP MEVLRKGSLR
1010 1020 1030 1040 1050
LRQLLSPKNE RRGEDEGSFP TPQENGQPES PRRPSLSRGD STEAAAEERG
1060 1070 1080 1090 1100
SRVRLASATA NALYSSNLRD DTKAILEQIS AHGQKHRGVP APGPAHSSPD
1110 1120 1130 1140 1150
VGRPTTAGDL APDMSDKDKC SAIFRSDSLG TQGRLSRTLP GSAEERDRLL
1160 1170 1180 1190 1200
RRMESMRKEK RVYSRFEVFC KKDEAGSSGA GDNLADEDTR DSKMGKFVPK

ILGTFKSKK
Length:1,209
Mass (Da):131,115
Last modified:August 22, 2006 - v1
Checksum:i1954B609EA75EF25
GO

Sequence cautioni

The sequence AAH36149.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti873 – 8731T → A in BAC29093 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27559.1.
RefSeqiNP_001161725.1. NM_001168253.1.
NP_598848.2. NM_134087.2.
XP_006520300.1. XM_006520237.2.
UniGeneiMm.267178.

Genome annotation databases

EnsembliENSMUST00000060807; ENSMUSP00000059839; ENSMUSG00000046761.
ENSMUST00000170153; ENSMUSP00000126453; ENSMUSG00000046761.
GeneIDi105732.
KEGGimmu:105732.
UCSCiuc007wic.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27559.1.
RefSeqiNP_001161725.1. NM_001168253.1.
NP_598848.2. NM_134087.2.
XP_006520300.1. XM_006520237.2.
UniGeneiMm.267178.

3D structure databases

ProteinModelPortaliQ148V8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222906. 1 interaction.
IntActiQ148V8. 2 interactions.
STRINGi10090.ENSMUSP00000059839.

PTM databases

iPTMnetiQ148V8.
PhosphoSiteiQ148V8.

Proteomic databases

MaxQBiQ148V8.
PaxDbiQ148V8.
PeptideAtlasiQ148V8.
PRIDEiQ148V8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000060807; ENSMUSP00000059839; ENSMUSG00000046761.
ENSMUST00000170153; ENSMUSP00000126453; ENSMUSG00000046761.
GeneIDi105732.
KEGGimmu:105732.
UCSCiuc007wic.2. mouse.

Organism-specific databases

CTDi286077.
MGIiMGI:2145900. Fam83h.

Phylogenomic databases

eggNOGiENOG410IEPN. Eukaryota.
ENOG410YB0T. LUCA.
GeneTreeiENSGT00760000119168.
HOGENOMiHOG000112488.
HOVERGENiHBG107907.
InParanoidiQ148V8.
OMAiGFFQARH.
OrthoDBiEOG7P2XR9.
PhylomeDBiQ148V8.
TreeFamiTF330777.

Miscellaneous databases

ChiTaRSiFam83h. mouse.
PROiQ148V8.
SOURCEiSearch...

Gene expression databases

BgeeiQ148V8.
CleanExiMM_AA409316.
GenevisibleiQ148V8. MM.

Family and domain databases

InterProiIPR012461. DUF1669.
[Graphical view]
PANTHERiPTHR16181. PTHR16181. 5 hits.
PfamiPF07894. DUF1669. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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].
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-904; SER-915; THR-917; SER-926; THR-928; SER-948; SER-959; SER-970 AND SER-1041, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Liver, Lung, Pancreas and Testis.

Entry informationi

Entry nameiFA83H_MOUSE
AccessioniPrimary (citable) accession number: Q148V8
Secondary accession number(s): Q8BZF6
, Q8CI79, Q8R5C2, Q8R5D0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: August 22, 2006
Last modified: July 6, 2016
This is version 82 of the entry and version 1 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

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 one 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.