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Q5JQC9

- AKAP4_HUMAN

UniProt

Q5JQC9 - AKAP4_HUMAN

Protein

A-kinase anchor protein 4

Gene

AKAP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
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    Functioni

    Major structural component of sperm fibrous sheath. Plays a role in sperm motility.1 Publication

    GO - Molecular functioni

    1. protein kinase A binding Source: UniProtKB

    GO - Biological processi

    1. cell projection organization Source: UniProtKB-KW
    2. cellular component movement Source: ProtInc
    3. protein localization Source: Ensembl
    4. signal transduction Source: ProtInc
    5. single fertilization Source: ProtInc
    6. sperm motility Source: UniProtKB
    7. transmembrane receptor protein serine/threonine kinase signaling pathway Source: Ensembl

    Keywords - Biological processi

    Cilium biogenesis/degradation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A-kinase anchor protein 4
    Short name:
    AKAP-4
    Alternative name(s):
    A-kinase anchor protein 82 kDa
    Short name:
    AKAP 82
    Short name:
    hAKAP82
    Major sperm fibrous sheath protein
    Short name:
    HI
    Protein kinase A-anchoring protein 4
    Short name:
    PRKA4
    Gene namesi
    Name:AKAP4Imported
    Synonyms:AKAP82
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:374. AKAP4.

    Subcellular locationi

    Cell projectionciliumflagellum 1 Publication
    Note: Localizes to the principle piece of the sperm flagellum.

    GO - Cellular componenti

    1. cAMP-dependent protein kinase complex Source: UniProtKB
    2. cytoskeleton Source: ProtInc
    3. motile cilium Source: UniProtKB
    4. nucleus Source: UniProt
    5. perinuclear region of cytoplasm Source: Ensembl
    6. sperm principal piece Source: Ensembl
    7. Z disc Source: Ensembl

    Keywords - Cellular componenti

    Cell projection, Cilium, Flagellum

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24668.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 188188Sequence AnalysisPRO_0000248230Add
    BLAST
    Chaini189 – 854666A-kinase anchor protein 4By similarityPRO_0000248231Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei300 – 3001Phosphoserine1 Publication
    Modified residuei303 – 3031Phosphotyrosine1 Publication
    Modified residuei304 – 3041Phosphoserine1 Publication
    Modified residuei447 – 4471Phosphoserine1 Publication
    Modified residuei450 – 4501Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5JQC9.
    PaxDbiQ5JQC9.
    PRIDEiQ5JQC9.

    PTM databases

    PhosphoSiteiQ5JQC9.

    Expressioni

    Tissue specificityi

    Testis specific; only expressed in round spermatids.1 Publication

    Developmental stagei

    Post-meiotic phase of spermatogenesis.1 Publication

    Gene expression databases

    ArrayExpressiQ5JQC9.
    BgeeiQ5JQC9.
    CleanExiHS_AKAP4.
    GenevestigatoriQ5JQC9.

    Organism-specific databases

    HPAiHPA005949.
    HPA020046.

    Interactioni

    Subunit structurei

    Interacts with PRKAR1A and PRKAR2A.By similarity

    Protein-protein interaction databases

    BioGridi114377. 6 interactions.
    STRINGi9606.ENSP00000351327.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5JQC9.
    SMRiQ5JQC9. Positions 771-852.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni219 – 23214PKA-RI and PKA-RII subunit binding domainBy similarityAdd
    BLAST
    Regioni336 – 34510PKA-RI-alpha subunit binding domainBy similarity

    Domaini

    RI-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.By similarity

    Sequence similaritiesi

    Belongs to the AKAP110 family.Curated

    Phylogenomic databases

    eggNOGiNOG40269.
    HOGENOMiHOG000220883.
    HOVERGENiHBG050478.
    InParanoidiQ5JQC9.
    KOiK16521.
    OMAiGEHILKE.
    PhylomeDBiQ5JQC9.
    TreeFamiTF105403.

    Family and domain databases

    InterProiIPR020799. AKAP_110.
    IPR018292. AKAP_110_C.
    IPR018459. RII_binding_1.
    IPR008382. SPHK1-interactor_AKAP_110.
    [Graphical view]
    PANTHERiPTHR10226. PTHR10226. 1 hit.
    PfamiPF05716. AKAP_110. 1 hit.
    PF10522. RII_binding_1. 1 hit.
    [Graphical view]
    SMARTiSM00807. AKAP_110. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q5JQC9-1) [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

    MMAYSDTTMM SDDIDWLRSH RGVCKVDLYN PEGQQDQDRK VICFVDVSTL    50
    NVEDKDYKDA ASSSSEGNLN LGSLEEKEII VIKDTEKKDQ SKTEGSVCLF 100
    KQAPSDPVSV LNWLLSDLQK YALGFQHALS PSTSTCKHKV GDTEGEYHRA 150
    SSENCYSVYA DQVNIDYLMN RPQNLRLEMT AAKNTNNNQS PSAPPAKPPS 200
    TQRAVISPDG ECSIDDLSFY VNRLSSLVIQ MAHKEIKEKL EGKSKCLHHS 250
    ICPSPGNKER ISPRTPASKI ASEMAYEAVE LTAAEMRGTG EESREGGQKS 300
    FLYSELSNKS KSGDKQMSQR ESKEFADSIS KGLMVYANQV ASDMMVSLMK 350
    TLKVHSSGKP IPASVVLKRV LLRHTKEIVS DLIDSCMKNL HNITGVLMTD 400
    SDFVSAVKRN LFNQWKQNAT DIMEAMLKRL VSALIGEEKE TKSQSLSYAS 450
    LKAGSHDPKC RNQSLEFSTM KAEMKERDKG KMKSDPCKSL TSAEKVGEHI 500
    LKEGLTIWNQ KQGNSCKVAT KACSNKDEKG EKINASTDSL AKDLIVSALK 550
    LIQYHLTQQT KGKDTCEEDC PGSTMGYMAQ STQYEKCGGG QSAKALSVKQ 600
    LESHRAPGPS TCQKENQHLD SQKMDMSNIV LMLIQKLLNE NPFKCEDPCE 650
    GENKCSEPRA SKAASMSNRS DKAEEQCQEH QELDCTSGMK QANGQFIDKL 700
    VESVMKLCLI MAKYSNDGAA LAELEEQAAS ANKPNFRGTR CIHSGAMPQN 750
    YQDSLGHEVI VNNQCSTNSL QKQLQAVLQW IAASQFNVPM LYFMGDKDGQ 800
    LEKLPQVSAK AAEKGYSVGG LLQEVMKFAK ERQPDEAVGK VARKQLLDWL 850
    LANL 854
    Length:854
    Mass (Da):94,477
    Last modified:February 15, 2005 - v1
    Checksum:iE440CBE8AB9394F4
    GO
    Isoform 21 Publication (identifier: Q5JQC9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-9: Missing.

    Show »
    Length:845
    Mass (Da):93,445
    Checksum:iEBB124BFF6BF3C31
    GO

    Sequence cautioni

    The sequence CAA75494.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti123 – 1231L → W in AAC79433. (PubMed:9822690)Curated
    Sequence conflicti128 – 1281A → E in AAC79433. (PubMed:9822690)Curated
    Sequence conflicti146 – 1461E → D in AAC79433. (PubMed:9822690)Curated
    Sequence conflicti369 – 3691R → W in CAA75494. (PubMed:9514854)Curated
    Sequence conflicti428 – 4292KR → IL in AAC79433. (PubMed:9822690)Curated
    Sequence conflicti517 – 5171K → M in AAC79433. (PubMed:9822690)Curated
    Sequence conflicti560 – 5601T → I in CAA75494. (PubMed:9514854)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti233 – 2331H → R.
    Corresponds to variant rs17174078 [ dbSNP | Ensembl ].
    VAR_048206
    Natural varianti673 – 6731A → G.
    Corresponds to variant rs12012704 [ dbSNP | Ensembl ].
    VAR_027266

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 99Missing in isoform 2. 1 PublicationVSP_052142

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y15195 mRNA. Translation: CAA75494.1. Sequence problems.
    AF072756 mRNA. Translation: AAC79433.1.
    FO393402 Genomic DNA. No translation available.
    BC126250 mRNA. Translation: AAI26251.1.
    BC126252 mRNA. Translation: AAI26253.1.
    CCDSiCCDS14329.1. [Q5JQC9-1]
    CCDS14330.1. [Q5JQC9-2]
    PIRiJC5986.
    RefSeqiNP_003877.2. NM_003886.2. [Q5JQC9-1]
    NP_647450.1. NM_139289.1. [Q5JQC9-2]
    UniGeneiHs.97633.

    Genome annotation databases

    EnsembliENST00000358526; ENSP00000351327; ENSG00000147081. [Q5JQC9-1]
    ENST00000376064; ENSP00000365232; ENSG00000147081. [Q5JQC9-2]
    GeneIDi8852.
    KEGGihsa:8852.
    UCSCiuc004dou.1. human. [Q5JQC9-1]

    Polymorphism databases

    DMDMi74741729.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y15195 mRNA. Translation: CAA75494.1 . Sequence problems.
    AF072756 mRNA. Translation: AAC79433.1 .
    FO393402 Genomic DNA. No translation available.
    BC126250 mRNA. Translation: AAI26251.1 .
    BC126252 mRNA. Translation: AAI26253.1 .
    CCDSi CCDS14329.1. [Q5JQC9-1 ]
    CCDS14330.1. [Q5JQC9-2 ]
    PIRi JC5986.
    RefSeqi NP_003877.2. NM_003886.2. [Q5JQC9-1 ]
    NP_647450.1. NM_139289.1. [Q5JQC9-2 ]
    UniGenei Hs.97633.

    3D structure databases

    ProteinModelPortali Q5JQC9.
    SMRi Q5JQC9. Positions 771-852.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114377. 6 interactions.
    STRINGi 9606.ENSP00000351327.

    PTM databases

    PhosphoSitei Q5JQC9.

    Polymorphism databases

    DMDMi 74741729.

    Proteomic databases

    MaxQBi Q5JQC9.
    PaxDbi Q5JQC9.
    PRIDEi Q5JQC9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358526 ; ENSP00000351327 ; ENSG00000147081 . [Q5JQC9-1 ]
    ENST00000376064 ; ENSP00000365232 ; ENSG00000147081 . [Q5JQC9-2 ]
    GeneIDi 8852.
    KEGGi hsa:8852.
    UCSCi uc004dou.1. human. [Q5JQC9-1 ]

    Organism-specific databases

    CTDi 8852.
    GeneCardsi GC0XM049955.
    HGNCi HGNC:374. AKAP4.
    HPAi HPA005949.
    HPA020046.
    MIMi 300185. gene.
    neXtProti NX_Q5JQC9.
    PharmGKBi PA24668.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40269.
    HOGENOMi HOG000220883.
    HOVERGENi HBG050478.
    InParanoidi Q5JQC9.
    KOi K16521.
    OMAi GEHILKE.
    PhylomeDBi Q5JQC9.
    TreeFami TF105403.

    Miscellaneous databases

    ChiTaRSi AKAP4. human.
    GeneWikii AKAP4.
    GenomeRNAii 8852.
    NextBioi 33231.
    PROi Q5JQC9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5JQC9.
    Bgeei Q5JQC9.
    CleanExi HS_AKAP4.
    Genevestigatori Q5JQC9.

    Family and domain databases

    InterProi IPR020799. AKAP_110.
    IPR018292. AKAP_110_C.
    IPR018459. RII_binding_1.
    IPR008382. SPHK1-interactor_AKAP_110.
    [Graphical view ]
    PANTHERi PTHR10226. PTHR10226. 1 hit.
    Pfami PF05716. AKAP_110. 1 hit.
    PF10522. RII_binding_1. 1 hit.
    [Graphical view ]
    SMARTi SM00807. AKAP_110. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of human testis mRNA specifically expressed in haploid germ cells, having structural homology with the A-kinase anchoring proteins."
      Mohapatra B., Verma S., Shankar S., Suri A.
      Biochem. Biophys. Res. Commun. 244:540-545(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: TestisImported.
    2. "An X-linked gene encodes a major human sperm fibrous sheath protein, hAKAP82. Genomic organization, protein kinase A-RII binding, and distribution of the precursor in the sperm tail."
      Turner R.M.O., Johnson L.R., Haig-Ladewig L., Gerton G.L., Moss S.B.
      J. Biol. Chem. 273:32135-32141(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      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: Testis.
    5. "Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation."
      Ficarro S., Chertihin O., Westbrook V.A., White F., Jayes F., Kalab P., Marto J.A., Shabanowitz J., Herr J.C., Hunt D.F., Visconti P.E.
      J. Biol. Chem. 278:11579-11589(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; TYR-303; SER-304; SER-447 AND SER-450, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Sperm.

    Entry informationi

    Entry nameiAKAP4_HUMAN
    AccessioniPrimary (citable) accession number: Q5JQC9
    Secondary accession number(s): A0AV85
    , O60904, O95246, Q5JQD1, Q5JQD2, Q5JQD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2006
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 87 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 X
      Human chromosome X: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3