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Q92667

- AKAP1_HUMAN

UniProt

Q92667 - AKAP1_HUMAN

Protein

A-kinase anchor protein 1, mitochondrial

Gene

AKAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. RNA binding Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A-kinase anchor protein 1, mitochondrial
    Alternative name(s):
    A-kinase anchor protein 149 kDa
    Short name:
    AKAP 149
    Dual specificity A-kinase-anchoring protein 1
    Short name:
    D-AKAP-1
    Protein kinase A-anchoring protein 1
    Short name:
    PRKA1
    Spermatid A-kinase anchor protein 84
    Short name:
    S-AKAP84
    Gene namesi
    Name:AKAP1
    Synonyms:AKAP149, PRKA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:367. AKAP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. integral component of membrane Source: UniProtKB-KW
    3. membrane Source: UniProtKB
    4. mitochondrial outer membrane Source: UniProtKB-SubCell
    5. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24661.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929MitochondrionSequence AnalysisAdd
    BLAST
    Chaini30 – 903874A-kinase anchor protein 1, mitochondrialPRO_0000016659Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei70 – 701Phosphothreonine1 Publication
    Modified residuei105 – 1051PhosphoserineBy similarity
    Modified residuei107 – 1071PhosphoserineBy similarity
    Modified residuei169 – 1691Phosphoserine1 Publication
    Modified residuei429 – 4291Phosphoserine1 Publication
    Modified residuei447 – 4471Phosphothreonine1 Publication
    Modified residuei533 – 5331Phosphothreonine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ92667.
    PaxDbiQ92667.
    PRIDEiQ92667.

    PTM databases

    PhosphoSiteiQ92667.

    Miscellaneous databases

    PMAP-CutDBQ92667.

    Expressioni

    Tissue specificityi

    AKAP149 is highly expressed in prostate and small intestine whereas S-AKAP84 is expressed in kidney, pancreas, liver, lung and brain. AKAP149 is also expressed in colon carcinoma.

    Gene expression databases

    ArrayExpressiQ92667.
    BgeeiQ92667.
    CleanExiHS_AKAP1.
    GenevestigatoriQ92667.

    Organism-specific databases

    HPAiCAB019286.
    HPA008691.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MAATS1Q7Z4T9-43EBI-2120060,EBI-2119735
    MYCBPQ994172EBI-2120060,EBI-716185
    PRKAR2AP138613EBI-2119593,EBI-2556122

    Protein-protein interaction databases

    BioGridi113818. 14 interactions.
    IntActiQ92667. 10 interactions.
    MINTiMINT-2411938.
    STRINGi9606.ENSP00000337736.

    Structurei

    3D structure databases

    ProteinModelPortaliQ92667.
    SMRiQ92667. Positions 758-867.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini607 – 67165KHPROSITE-ProRule annotationAdd
    BLAST
    Domaini758 – 81760TudorPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni344 – 35714PKA-RII subunit binding domainAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Contains 1 KH domain.PROSITE-ProRule annotation
    Contains 1 Tudor domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide, Transmembrane

    Phylogenomic databases

    eggNOGiNOG306785.
    HOGENOMiHOG000013170.
    HOVERGENiHBG057436.
    InParanoidiQ92667.
    KOiK16518.
    OMAiDLIIWEI.
    OrthoDBiEOG779NXH.
    PhylomeDBiQ92667.
    TreeFamiTF105401.

    Family and domain databases

    Gene3Di3.30.1370.10. 1 hit.
    InterProiIPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR002999. Tudor.
    [Graphical view]
    PfamiPF00013. KH_1. 1 hit.
    PF00567. TUDOR. 1 hit.
    [Graphical view]
    SMARTiSM00322. KH. 1 hit.
    SM00333. TUDOR. 1 hit.
    [Graphical view]
    SUPFAMiSSF54791. SSF54791. 1 hit.
    PROSITEiPS50084. KH_TYPE_1. 1 hit.
    PS50304. TUDOR. 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 1 (identifier: Q92667-1) [UniParc]FASTAAdd to Basket

    Also known as: AKAP149

    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

    MAIQFRSLFP LALPGMLALL GWWWFFSRKK GHVSSHDEQQ VEAGAVQLRA    50
    DPAIKEPLPV EDVCPKVVST PPSVTEPPEK ELSTVSKLPA EPPALLQTHP 100
    PCRRSESSGI LPNTTDMRLR PGTRRDDSTK LELALTGGEA KSIPLECPLS 150
    SPKGVLFSSK SAEVCKQDSP FSRVPRKVQP GYPVVPAEKR SSGERARETG 200
    GAEGTGDAVL GEKVLEEALL SREHVLELEN SKGPSLASLE GEEDKGKSSS 250
    SQVVGPVQEE EYVAEKLPSR FIESAHTELA KDDAAPAPPV ADAKAQDRGV 300
    EGELGNEESL DRNEEGLDRN EEGLDRNEES LDRNEEGLDR NEEIKRAAFQ 350
    IISQVISEAT EQVLATTVGK VAGRVCQASQ LQGQKEESCV PVHQKTVLGP 400
    DTAEPATAEA AVAPPDAGLP LPGLPAEGSP PPKTYVSCLK SLLSSPTKDS 450
    KPNISAHHIS LASCLALTTP SEELPDRAGI LVEDATCVTC MSDSSQSVPL 500
    VASPGHCSDS FSTSGLEDSC TETSSSPRDK AITPPLPEST VPFSNGVLKG 550
    ELSDLGAEDG WTMDAEADHS GGSDRNSMDS VDSCCSLKKT ESFQNAQAGS 600
    NPKKVDLIIW EIEVPKHLVG RLIGKQGRYV SFLKQTSGAK IYISTLPYTQ 650
    SVQICHIEGS QHHVDKALNL IGKKFKELNL TNIYAPPLPS LALPSLPMTS 700
    WLMLPDGITV EVIVVNQVNA GHLFVQQHTH PTFHALRSLD QQMYLCYSQP 750
    GIPTLPTPVE ITVICAAPGA DGAWWRAQVV ASYEETNEVE IRYVDYGGYK 800
    RVKVDVLRQI RSDFVTLPFQ GAEVLLDSVM PLSDDDQFSP EADAAMSEMT 850
    GNTALLAQVT SYSPTGLPLI QLWSVVGDEV VLINRSLVER GLAQWVDSYY 900
    TSL 903
    Length:903
    Mass (Da):97,342
    Last modified:February 1, 1997 - v1
    Checksum:i0C906FAFFB0DBAF7
    GO
    Isoform 2 (identifier: Q92667-2) [UniParc]FASTAAdd to Basket

    Also known as: S-AKAP84

    The sequence of this isoform differs from the canonical sequence as follows:
         572-593: GSDRNSMDSVDSCCSLKKTESF → VAAPPPGKRGTLITRCPGFFEC
         594-903: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:593
    Mass (Da):62,921
    Checksum:i3F2FC6A1381EFEC1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti795 – 7951D → H in AAH00729. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181A → V.
    Corresponds to variant rs17761023 [ dbSNP | Ensembl ].
    VAR_049676
    Natural varianti60 – 601V → M.
    Corresponds to variant rs2230770 [ dbSNP | Ensembl ].
    VAR_024512
    Natural varianti102 – 1021C → Y.
    Corresponds to variant rs2230771 [ dbSNP | Ensembl ].
    VAR_049677
    Natural varianti124 – 1241R → C.
    Corresponds to variant rs17833723 [ dbSNP | Ensembl ].
    VAR_049678

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei572 – 59322GSDRN…KTESF → VAAPPPGKRGTLITRCPGFF EC in isoform 2. 1 PublicationVSP_002845Add
    BLAST
    Alternative sequencei594 – 903310Missing in isoform 2. 1 PublicationVSP_002846Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97335 mRNA. Translation: CAA66000.1.
    U34074 mRNA. Translation: AAC50279.1.
    AK292416 mRNA. Translation: BAF85105.1.
    CH471109 Genomic DNA. Translation: EAW94515.1.
    CH471109 Genomic DNA. Translation: EAW94516.1.
    CH471109 Genomic DNA. Translation: EAW94518.1.
    BC000729 mRNA. Translation: AAH00729.1.
    CCDSiCCDS11594.1. [Q92667-1]
    PIRiI39173.
    RefSeqiNP_001229831.1. NM_001242902.1. [Q92667-1]
    NP_001229832.1. NM_001242903.1. [Q92667-1]
    NP_003479.1. NM_003488.3. [Q92667-1]
    XP_005257764.1. XM_005257707.1. [Q92667-1]
    XP_005257766.1. XM_005257709.1. [Q92667-1]
    XP_006722189.1. XM_006722126.1. [Q92667-1]
    XP_006722190.1. XM_006722127.1. [Q92667-1]
    UniGeneiHs.463506.

    Genome annotation databases

    EnsembliENST00000314126; ENSP00000314075; ENSG00000121057. [Q92667-2]
    ENST00000337714; ENSP00000337736; ENSG00000121057. [Q92667-1]
    ENST00000481416; ENSP00000433212; ENSG00000121057. [Q92667-2]
    ENST00000539273; ENSP00000443139; ENSG00000121057. [Q92667-1]
    ENST00000571629; ENSP00000459968; ENSG00000121057. [Q92667-1]
    ENST00000572557; ENSP00000459895; ENSG00000121057. [Q92667-1]
    GeneIDi8165.
    KEGGihsa:8165.
    UCSCiuc002iux.3. human. [Q92667-1]

    Polymorphism databases

    DMDMi8134304.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X97335 mRNA. Translation: CAA66000.1 .
    U34074 mRNA. Translation: AAC50279.1 .
    AK292416 mRNA. Translation: BAF85105.1 .
    CH471109 Genomic DNA. Translation: EAW94515.1 .
    CH471109 Genomic DNA. Translation: EAW94516.1 .
    CH471109 Genomic DNA. Translation: EAW94518.1 .
    BC000729 mRNA. Translation: AAH00729.1 .
    CCDSi CCDS11594.1. [Q92667-1 ]
    PIRi I39173.
    RefSeqi NP_001229831.1. NM_001242902.1. [Q92667-1 ]
    NP_001229832.1. NM_001242903.1. [Q92667-1 ]
    NP_003479.1. NM_003488.3. [Q92667-1 ]
    XP_005257764.1. XM_005257707.1. [Q92667-1 ]
    XP_005257766.1. XM_005257709.1. [Q92667-1 ]
    XP_006722189.1. XM_006722126.1. [Q92667-1 ]
    XP_006722190.1. XM_006722127.1. [Q92667-1 ]
    UniGenei Hs.463506.

    3D structure databases

    ProteinModelPortali Q92667.
    SMRi Q92667. Positions 758-867.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113818. 14 interactions.
    IntActi Q92667. 10 interactions.
    MINTi MINT-2411938.
    STRINGi 9606.ENSP00000337736.

    Chemistry

    BindingDBi Q92667.

    PTM databases

    PhosphoSitei Q92667.

    Polymorphism databases

    DMDMi 8134304.

    Proteomic databases

    MaxQBi Q92667.
    PaxDbi Q92667.
    PRIDEi Q92667.

    Protocols and materials databases

    DNASUi 8165.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314126 ; ENSP00000314075 ; ENSG00000121057 . [Q92667-2 ]
    ENST00000337714 ; ENSP00000337736 ; ENSG00000121057 . [Q92667-1 ]
    ENST00000481416 ; ENSP00000433212 ; ENSG00000121057 . [Q92667-2 ]
    ENST00000539273 ; ENSP00000443139 ; ENSG00000121057 . [Q92667-1 ]
    ENST00000571629 ; ENSP00000459968 ; ENSG00000121057 . [Q92667-1 ]
    ENST00000572557 ; ENSP00000459895 ; ENSG00000121057 . [Q92667-1 ]
    GeneIDi 8165.
    KEGGi hsa:8165.
    UCSCi uc002iux.3. human. [Q92667-1 ]

    Organism-specific databases

    CTDi 8165.
    GeneCardsi GC17P055162.
    HGNCi HGNC:367. AKAP1.
    HPAi CAB019286.
    HPA008691.
    MIMi 602449. gene.
    neXtProti NX_Q92667.
    PharmGKBi PA24661.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG306785.
    HOGENOMi HOG000013170.
    HOVERGENi HBG057436.
    InParanoidi Q92667.
    KOi K16518.
    OMAi DLIIWEI.
    OrthoDBi EOG779NXH.
    PhylomeDBi Q92667.
    TreeFami TF105401.

    Enzyme and pathway databases

    Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    ChiTaRSi AKAP1. human.
    GeneWikii AKAP1.
    GenomeRNAii 8165.
    NextBioi 30837.
    PMAP-CutDB Q92667.
    PROi Q92667.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92667.
    Bgeei Q92667.
    CleanExi HS_AKAP1.
    Genevestigatori Q92667.

    Family and domain databases

    Gene3Di 3.30.1370.10. 1 hit.
    InterProi IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR002999. Tudor.
    [Graphical view ]
    Pfami PF00013. KH_1. 1 hit.
    PF00567. TUDOR. 1 hit.
    [Graphical view ]
    SMARTi SM00322. KH. 1 hit.
    SM00333. TUDOR. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54791. SSF54791. 1 hit.
    PROSITEi PS50084. KH_TYPE_1. 1 hit.
    PS50304. TUDOR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of AKAP149, a novel A kinase anchor protein with a KH domain."
      Trendelenburg G., Hummel M., Riecken E.-O., Hanski C.
      Biochem. Biophys. Res. Commun. 225:313-319(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Colon.
    2. "Characterization of S-AKAP84, a novel developmentally regulated A kinase anchor protein of male germ cells."
      Lin R.-Y., Moss S.B., Rubin C.S.
      J. Biol. Chem. 270:27804-27811(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Testis.
    3. "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).
      Tissue: Testis.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Brain.
    6. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429 AND THR-533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70 AND THR-533, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAKAP1_HUMAN
    AccessioniPrimary (citable) accession number: Q92667
    Secondary accession number(s): A8K8Q1
    , D3DTZ0, Q13320, Q9BW14
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 144 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 17
      Human chromosome 17: 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