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Protein

Protein unc-119 homolog B

Gene

UNC119B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Myristoyl-binding protein that acts as a cargo adapter: specifically binds the myristoyl moiety of a subset of N-terminally myristoylated proteins and is required for their localization. Binds myristoylated NPHP3 and plays a key role in localization of NPHP3 to the primary cilium membrane. Does not bind all myristoylated proteins. Probably plays a role in trafficking proteins in photoreceptor cells.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei142 – 1421LipidBy similarity

GO - Molecular functioni

  • lipid binding Source: UniProtKB

GO - Biological processi

  • cilium morphogenesis Source: UniProtKB
  • lipoprotein transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-HSA-5624138. Trafficking of myristoylated proteins to the cilium.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein unc-119 homolog B
Gene namesi
Name:UNC119B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:16488. UNC119B.

Subcellular locationi

GO - Cellular componenti

  • ciliary transition zone Source: UniProtKB
  • cytosol Source: Reactome
  • primary cilium Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi144 – 1441F → A: Reduced binding to myristoylated proteins; when associated with A-148 and A-207. 1 Publication
Mutagenesisi148 – 1481F → A: Reduced binding to myristoylated proteins; when associated with A-144 and A-207. 1 Publication
Mutagenesisi207 – 2071F → A: Reduced binding to myristoylated proteins; when associated with A-144 and A-148. 1 Publication

Organism-specific databases

PharmGKBiPA38152.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 251250Protein unc-119 homolog BPRO_0000337228Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei24 – 241N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiA6NIH7.
MaxQBiA6NIH7.
PaxDbiA6NIH7.
PeptideAtlasiA6NIH7.
PRIDEiA6NIH7.

PTM databases

iPTMnetiA6NIH7.
PhosphoSiteiA6NIH7.

Expressioni

Gene expression databases

BgeeiA6NIH7.
CleanExiHS_UNC119B.
GenevisibleiA6NIH7. HS.

Interactioni

Subunit structurei

Found in a complex with ARL3, RP2 and UNC119B; RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the release of UNC119B. Interacts with NPHP3 (when myristoylated). Interacts with CYS1 (when myristoylated). Interacts with C5orf30; interaction only takes place when UNC119B is not liganded with myristoylated proteins.1 Publication

Protein-protein interaction databases

BioGridi124237. 12 interactions.
DIPiDIP-61819N.
IntActiA6NIH7. 4 interactions.
MINTiMINT-6997631.
STRINGi9606.ENSP00000344942.

Structurei

3D structure databases

ProteinModelPortaliA6NIH7.
SMRiA6NIH7. Positions 68-249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 158Poly-Ala

Domaini

Adopts an immunoglobulin-like beta-sandwich fold forming a hydrophobic cavity that capture N-terminally myristoylated target peptides. Phe residues within the hydrophobic beta sandwich are required for myristate binding (PubMed:22085962).1 Publication

Sequence similaritiesi

Belongs to the PDE6D/unc-119 family.Curated

Phylogenomic databases

eggNOGiKOG4037. Eukaryota.
ENOG410YJ3E. LUCA.
GeneTreeiENSGT00390000014595.
HOGENOMiHOG000258286.
HOVERGENiHBG108625.
InParanoidiA6NIH7.
OMAiLMDDMIN.
OrthoDBiEOG7288SP.
PhylomeDBiA6NIH7.
TreeFamiTF314474.

Family and domain databases

Gene3Di2.70.50.40. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR008015. PDED_dom.
[Graphical view]
PfamiPF05351. GMP_PDE_delta. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.

Sequencei

Sequence statusi: Complete.

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

A6NIH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGSNPKAAA AASAAGPGGL VAGKEEKKKA GGGVLNRLKA RRQAPHHAAD
60 70 80 90 100
DGVGAAVTEQ ELLALDTIRP EHVLRLSRVT ENYLCKPEDN IYSIDFTRFK
110 120 130 140 150
IRDLETGTVL FEIAKPCVSD QEEDEEEGGG DVDISAGRFV RYQFTPAFLR
160 170 180 190 200
LRTVGATVEF TVGDKPVSNF RMIERHYFRE HLLKNFDFDF GFCIPSSRNT
210 220 230 240 250
CEHIYEFPQL SEDVIRLMIE NPYETRSDSF YFVDNKLIMH NKADYAYNGG

Q
Length:251
Mass (Da):28,137
Last modified:July 24, 2007 - v1
Checksum:i3041B68EE89B3BD4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK126367 mRNA. No translation available.
AC069234 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98216.1.
BC004815 mRNA. No translation available.
CCDSiCCDS31914.1.
RefSeqiNP_001074002.1. NM_001080533.2.
UniGeneiHs.127610.

Genome annotation databases

EnsembliENST00000344651; ENSP00000344942; ENSG00000175970.
GeneIDi84747.
KEGGihsa:84747.
UCSCiuc001tyz.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK126367 mRNA. No translation available.
AC069234 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98216.1.
BC004815 mRNA. No translation available.
CCDSiCCDS31914.1.
RefSeqiNP_001074002.1. NM_001080533.2.
UniGeneiHs.127610.

3D structure databases

ProteinModelPortaliA6NIH7.
SMRiA6NIH7. Positions 68-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124237. 12 interactions.
DIPiDIP-61819N.
IntActiA6NIH7. 4 interactions.
MINTiMINT-6997631.
STRINGi9606.ENSP00000344942.

PTM databases

iPTMnetiA6NIH7.
PhosphoSiteiA6NIH7.

Proteomic databases

EPDiA6NIH7.
MaxQBiA6NIH7.
PaxDbiA6NIH7.
PeptideAtlasiA6NIH7.
PRIDEiA6NIH7.

Protocols and materials databases

DNASUi84747.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344651; ENSP00000344942; ENSG00000175970.
GeneIDi84747.
KEGGihsa:84747.
UCSCiuc001tyz.4. human.

Organism-specific databases

CTDi84747.
GeneCardsiUNC119B.
H-InvDBHIX0201845.
HGNCiHGNC:16488. UNC119B.
neXtProtiNX_A6NIH7.
PharmGKBiPA38152.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4037. Eukaryota.
ENOG410YJ3E. LUCA.
GeneTreeiENSGT00390000014595.
HOGENOMiHOG000258286.
HOVERGENiHBG108625.
InParanoidiA6NIH7.
OMAiLMDDMIN.
OrthoDBiEOG7288SP.
PhylomeDBiA6NIH7.
TreeFamiTF314474.

Enzyme and pathway databases

ReactomeiR-HSA-5624138. Trafficking of myristoylated proteins to the cilium.

Miscellaneous databases

ChiTaRSiUNC119B. human.
GenomeRNAii84747.
PROiA6NIH7.

Gene expression databases

BgeeiA6NIH7.
CleanExiHS_UNC119B.
GenevisibleiA6NIH7. HS.

Family and domain databases

Gene3Di2.70.50.40. 1 hit.
InterProiIPR014756. Ig_E-set.
IPR008015. PDED_dom.
[Graphical view]
PfamiPF05351. GMP_PDE_delta. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Placenta.
  5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: FUNCTION, LIPID-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH NPHP3; CYS1 AND C5ORF30, IDENTIFICATION IN A COMPLEX WITH ARL3 AND RP2, MUTAGENESIS OF PHE-144; PHE-148 AND PHE-207.
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiU119B_HUMAN
AccessioniPrimary (citable) accession number: A6NIH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 24, 2007
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
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  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.