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Q86UC2

- RSPH3_HUMAN

UniProt

Q86UC2 - RSPH3_HUMAN

Protein

Radial spoke head protein 3 homolog

Gene

RSPH3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Functions as a protein kinase A-anchoring protein that scaffolds the cAMP-dependent protein kinase holoenzyme. May serve as a point of convergence for MAPK and PKA signaling in cilia.1 Publication

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Radial spoke head protein 3 homolog
    Alternative name(s):
    A-kinase anchor protein RSPH3
    Radial spoke head-like protein 2
    Gene namesi
    Name:RSPH3
    Synonyms:RSHL2, RSP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21054. RSPH3.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162402248.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 560560Radial spoke head protein 3 homologPRO_0000313741Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei286 – 2861Phosphothreonine; by MAPK11 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ86UC2.
    PRIDEiQ86UC2.

    PTM databases

    PhosphoSiteiQ86UC2.

    Expressioni

    Gene expression databases

    BgeeiQ86UC2.
    CleanExiHS_RSPH3.
    GenevestigatoriQ86UC2.

    Organism-specific databases

    HPAiHPA039109.
    HPA040230.

    Interactioni

    Subunit structurei

    Interacts with phosphorylated MAPK1. Interacts with MEK1. Interact with PKA regulatory subunits PRKAR1A and PRKAR1B.1 Publication

    Protein-protein interaction databases

    BioGridi123776. 3 interactions.
    IntActiQ86UC2. 1 interaction.
    MINTiMINT-1209207.
    STRINGi9606.ENSP00000252655.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86UC2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili215 – 23925Sequence AnalysisAdd
    BLAST
    Coiled coili331 – 38555Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the flagellar radial spoke RSP3 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG86709.
    HOGENOMiHOG000259276.
    HOVERGENiHBG067489.
    InParanoidiQ86UC2.
    OMAiWEIVHKH.
    OrthoDBiEOG7B8S49.
    PhylomeDBiQ86UC2.
    TreeFamiTF324184.

    Family and domain databases

    InterProiIPR009290. Radial_spoke_3.
    [Graphical view]
    PANTHERiPTHR21648. PTHR21648. 1 hit.
    PfamiPF06098. Radial_spoke_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86UC2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTVKPAKAAS LARNLAKRRR TYLGGAAGRS QEPEVPCAAV LPGKPGDRNC    50
    PEFPPPDRTL GCWATDAAPA AGLCGAGSEP SIAPTSCAGN LPSRPPPLLS 100
    PLLASRNPCP WHYLHLSGSH NTLAPTCFKA KLHRKRGSQP PDMASALTDR 150
    TSRAPSTYTY TSRPRALPCQ RSRYRDSLTQ PDEEPMHYGN IMYDRRVIRG 200
    NTYALQTGPL LGRPDSLELQ RQREARKRAL ARKQAQEQLR PQTPEPVEGR 250
    KHVDVQTELY LEEIADRIIE VDMECQTDAF LDRPPTPLFI PAKTGKDVAT 300
    QILEGELFDF DLEVKPVLEV LVGKTIEQSL LEVMEEEELA NLRASQREYE 350
    ELRNSERAEV QRLEEQERRH REEKERRKKQ QWEIMHKHNE TSQKIAARAF 400
    AQRYLADLLP SVFGSLRDSG YFYDPIERDI EIGFLPWLMN EVEKTMEYSM 450
    VGRTVLDMLI REVVEKRLCM YEHGEDTHQS PEPEDEPGGP GAMTESLEAS 500
    EFLEQSMSQT RELLLDGGYL QRTTYDRRSS QERKFMEERE LLGQDEETAM 550
    RKSLGEEELS 560
    Length:560
    Mass (Da):63,687
    Last modified:June 1, 2003 - v1
    Checksum:iEEAC4B64D1099019
    GO
    Isoform 2 (identifier: Q86UC2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         212-307: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:464
    Mass (Da):52,686
    Checksum:iEB69C3CDC21F115D
    GO

    Sequence cautioni

    The sequence AAK26432.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB71544.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI19235.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI19236.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti99 – 991L → S in BAB71615. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti201 – 2011N → S.
    Corresponds to variant rs16889320 [ dbSNP | Ensembl ].
    VAR_037720
    Natural varianti213 – 2131R → Q.
    Corresponds to variant rs34582178 [ dbSNP | Ensembl ].
    VAR_037721
    Natural varianti398 – 3981R → Q.
    Corresponds to variant rs10455840 [ dbSNP | Ensembl ].
    VAR_037722
    Natural varianti439 – 4391M → T.
    Corresponds to variant rs768994 [ dbSNP | Ensembl ].
    VAR_037723
    Natural varianti484 – 4841E → K.
    Corresponds to variant rs12204826 [ dbSNP | Ensembl ].
    VAR_037724
    Natural varianti518 – 5181G → D.
    Corresponds to variant rs3756987 [ dbSNP | Ensembl ].
    VAR_037725

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei212 – 30796Missing in isoform 2. 1 PublicationVSP_030128Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK057655 mRNA. Translation: BAB71544.1. Different initiation.
    AK057931 mRNA. Translation: BAB71615.1.
    AL035530 Genomic DNA. Translation: CAI19235.1. Different initiation.
    AL035530 Genomic DNA. Translation: CAI19236.1. Different initiation.
    CH471051 Genomic DNA. Translation: EAW47643.1.
    BC050604 mRNA. Translation: AAH50604.1.
    AF353618 mRNA. Translation: AAK26432.1. Different initiation.
    CCDSiCCDS5260.1. [Q86UC2-1]
    RefSeqiNP_114130.3. NM_031924.4. [Q86UC2-1]
    XP_005267210.1. XM_005267153.2. [Q86UC2-2]
    UniGeneiHs.154628.

    Genome annotation databases

    EnsembliENST00000252655; ENSP00000252655; ENSG00000130363. [Q86UC2-1]
    ENST00000367069; ENSP00000356036; ENSG00000130363.
    ENST00000449822; ENSP00000393195; ENSG00000130363.
    GeneIDi83861.
    KEGGihsa:83861.
    UCSCiuc003qrx.3. human. [Q86UC2-1]
    uc010kju.3. human. [Q86UC2-2]

    Polymorphism databases

    DMDMi74750415.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK057655 mRNA. Translation: BAB71544.1 . Different initiation.
    AK057931 mRNA. Translation: BAB71615.1 .
    AL035530 Genomic DNA. Translation: CAI19235.1 . Different initiation.
    AL035530 Genomic DNA. Translation: CAI19236.1 . Different initiation.
    CH471051 Genomic DNA. Translation: EAW47643.1 .
    BC050604 mRNA. Translation: AAH50604.1 .
    AF353618 mRNA. Translation: AAK26432.1 . Different initiation.
    CCDSi CCDS5260.1. [Q86UC2-1 ]
    RefSeqi NP_114130.3. NM_031924.4. [Q86UC2-1 ]
    XP_005267210.1. XM_005267153.2. [Q86UC2-2 ]
    UniGenei Hs.154628.

    3D structure databases

    ProteinModelPortali Q86UC2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123776. 3 interactions.
    IntActi Q86UC2. 1 interaction.
    MINTi MINT-1209207.
    STRINGi 9606.ENSP00000252655.

    PTM databases

    PhosphoSitei Q86UC2.

    Polymorphism databases

    DMDMi 74750415.

    Proteomic databases

    PaxDbi Q86UC2.
    PRIDEi Q86UC2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252655 ; ENSP00000252655 ; ENSG00000130363 . [Q86UC2-1 ]
    ENST00000367069 ; ENSP00000356036 ; ENSG00000130363 .
    ENST00000449822 ; ENSP00000393195 ; ENSG00000130363 .
    GeneIDi 83861.
    KEGGi hsa:83861.
    UCSCi uc003qrx.3. human. [Q86UC2-1 ]
    uc010kju.3. human. [Q86UC2-2 ]

    Organism-specific databases

    CTDi 83861.
    GeneCardsi GC06M159397.
    HGNCi HGNC:21054. RSPH3.
    HPAi HPA039109.
    HPA040230.
    neXtProti NX_Q86UC2.
    PharmGKBi PA162402248.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG86709.
    HOGENOMi HOG000259276.
    HOVERGENi HBG067489.
    InParanoidi Q86UC2.
    OMAi WEIVHKH.
    OrthoDBi EOG7B8S49.
    PhylomeDBi Q86UC2.
    TreeFami TF324184.

    Miscellaneous databases

    GeneWikii RSPH3.
    GenomeRNAii 83861.
    NextBioi 72869.
    PROi Q86UC2.

    Gene expression databases

    Bgeei Q86UC2.
    CleanExi HS_RSPH3.
    Genevestigatori Q86UC2.

    Family and domain databases

    InterProi IPR009290. Radial_spoke_3.
    [Graphical view ]
    PANTHERi PTHR21648. PTHR21648. 1 hit.
    Pfami PF06098. Radial_spoke_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 66-560 (ISOFORM 2).
      Tissue: Epithelium and Trachea.
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [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] (ISOFORM 1).
      Tissue: Skin.
    5. "Molecular characterization of the human radial spoke protein 3 as an A-kinase anchoring protein."
      DeKorte M., Carr D.W.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-560 (ISOFORM 1).
      Tissue: Testis.
    6. "Radial spoke protein 3 is a mammalian protein kinase A-anchoring protein that binds ERK1/2."
      Jivan A., Earnest S., Juang Y.C., Cobb M.H.
      J. Biol. Chem. 284:29437-29445(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, PHOSPHORYLATION AT THR-286.

    Entry informationi

    Entry nameiRSPH3_HUMAN
    AccessioniPrimary (citable) accession number: Q86UC2
    Secondary accession number(s): Q96LQ5, Q96LX2, Q9BX75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 86 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 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3