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Q9ULX6

- AKP8L_HUMAN

UniProt

Q9ULX6 - AKP8L_HUMAN

Protein

A-kinase anchor protein 8-like

Gene

AKAP8L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Could play a role in constitutive transport element (CTE)-mediated gene expression. Does not seem to be implicated in the binding of regulatory subunit II of PKA. May be involved in nuclear envelope breakdown and chromatin condensation. May regulate the initiation phase of DNA replication when associated with TMPO-beta.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri389 – 41325C2H2 AKAP95-type 1Add
    BLAST
    Zinc fingeri482 – 50726C2H2 AKAP95-type 2Add
    BLAST

    GO - Molecular functioni

    1. DEAD/H-box RNA helicase binding Source: UniProtKB
    2. DNA binding Source: InterPro
    3. metal ion binding Source: UniProtKB-KW
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A-kinase anchor protein 8-like
    Short name:
    AKAP8-like protein
    Alternative name(s):
    Helicase A-binding protein 95
    Short name:
    HAP95
    Homologous to AKAP95 protein
    Short name:
    HA95
    Neighbor of A-kinase-anchoring protein 95
    Short name:
    Neighbor of AKAP95
    Gene namesi
    Name:AKAP8L
    Synonyms:NAKAP, NAKAP95
    ORF Names:HRIHFB2018
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:29857. AKAP8L.

    Subcellular locationi

    Nucleus matrix. Cytoplasm
    Note: Colocalizes with PRPF40A in the nuclear matrix By similarity. Nuclear at steady state but shuttles between the nucleus and cytoplasm. Associated with the nuclear matrix.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nuclear matrix Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134867364.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 646646A-kinase anchor protein 8-likePRO_0000075384Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei257 – 2571N6-acetyllysine1 Publication
    Modified residuei283 – 2831Phosphoserine4 Publications
    Modified residuei292 – 2921Phosphothreonine2 Publications
    Modified residuei297 – 2971Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated on serine or threonine residues possibly by PKA.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9ULX6.
    PaxDbiQ9ULX6.
    PRIDEiQ9ULX6.

    PTM databases

    PhosphoSiteiQ9ULX6.

    Expressioni

    Tissue specificityi

    Expressed in the brain cortex (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9ULX6.
    BgeeiQ9ULX6.
    CleanExiHS_AKAP8L.
    GenevestigatoriQ9ULX6.

    Organism-specific databases

    HPAiHPA042485.
    HPA042546.

    Interactioni

    Subunit structurei

    Interacts with PRPF40A By similarity. Binds to the C-terminal of RNA helicase A and to TMPO-beta. Interacts with RNF43.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P299913EBI-357530,EBI-8826747From a different organism.
    RNF43Q68DV72EBI-357530,EBI-1647060

    Protein-protein interaction databases

    BioGridi117940. 28 interactions.
    DIPiDIP-27541N.
    IntActiQ9ULX6. 16 interactions.
    MINTiMINT-1134534.
    STRINGi9606.ENSP00000380557.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ULX6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi274 – 2796Nuclear localization signalSequence Analysis
    Motifi362 – 3643Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi41 – 5212Gly/Tyr-richAdd
    BLAST
    Compositional biasi589 – 5979Pro-rich
    Compositional biasi602 – 6087Pro-rich

    Sequence similaritiesi

    Belongs to the AKAP95 family.Curated
    Contains 2 C2H2 AKAP95-type zinc fingers.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri389 – 41325C2H2 AKAP95-type 1Add
    BLAST
    Zinc fingeri482 – 50726C2H2 AKAP95-type 2Add
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG47695.
    HOGENOMiHOG000169111.
    HOVERGENiHBG104297.
    InParanoidiQ9ULX6.
    KOiK15978.
    OMAiDTNANPS.
    OrthoDBiEOG79SDWZ.
    PhylomeDBiQ9ULX6.
    TreeFamiTF105407.

    Family and domain databases

    InterProiIPR007071. AKAP95.
    IPR015880. Znf_C2H2-like.
    [Graphical view]
    PANTHERiPTHR12190. PTHR12190. 1 hit.
    PfamiPF04988. AKAP95. 1 hit.
    [Graphical view]
    SMARTiSM00355. ZnF_C2H2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9ULX6-1) [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

    MSYTGFVQGS ETTLQSTYSD TSAQPTCDYG YGTWNSGTNR GYEGYGYGYG    50
    YGQDNTTNYG YGMATSHSWE MPSSDTNANT SASGSASADS VLSRINQRLD 100
    MVPHLETDMM QGGVYGSGGE RYDSYESCDS RAVLSERDLY RSGYDYSELD 150
    PEMEMAYEGQ YDAYRDQFRM RGNDTFGPRA QGWARDARSG RPMASGYGRM 200
    WEDPMGARGQ CMSGASRLPS LFSQNIIPEY GMFQGMRGGG AFPGGSRFGF 250
    GFGNGMKQMR RTWKTWTTAD FRTKKKKRKQ GGSPDEPDSK ATRTDCSDNS 300
    DSDNDEGTEG EATEGLEGTE AVEKGSRVDG EDEEGKEDGR EEGKEDPEKG 350
    ALTTQDENGQ TKRKLQAGKK SQDKQKKRQR DRMVERIQFV CSLCKYRTFY 400
    EDEMASHLDS KFHKEHFKYV GTKLPKQTAD FLQEYVTNKT KKTEELRKTV 450
    EDLDGLIHQI YRDQDLTQEI AMEHFVKKVE AAHCAACDLF IPMQFGIIQK 500
    HLKTMDHNRN RRLMMEQSKK SSLMVARSIL NNKLISKKLE RYLKGENPFT 550
    DSPEEEKEQE EAEGGALDEG AQGEAAGISE GAEGVPAQPP VPPEPAPGAV 600
    SPPPPPPPEE EEEGAVPLLG GALQRQIRGI PGLDVEDDEE GGGGAP 646
    Length:646
    Mass (Da):71,649
    Last modified:May 18, 2010 - v3
    Checksum:iEED855A81BB06585
    GO
    Isoform 2 (identifier: Q9ULX6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         61-121: Missing.

    Show »
    Length:585
    Mass (Da):65,230
    Checksum:i460F073AC534A1B9
    GO

    Sequence cautioni

    The sequence AAF86048.1 differs from that shown. Reason: Frameshift at position 553.
    The sequence BAA34791.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001D → N in AAF86048. (PubMed:10748171)Curated
    Sequence conflicti189 – 1891S → N in AAF86048. (PubMed:10748171)Curated
    Sequence conflicti351 – 3588ALTTQDEN → EFSWGAWC in BAA34791. (PubMed:9853615)Curated
    Sequence conflicti599 – 61618AVSPP…EEGAV → GRVAATAAAPRRRRRRAPW in AAF86048. (PubMed:10748171)CuratedAdd
    BLAST
    Sequence conflicti641 – 6466GGGGAP → EGRRGRPV in AAF86048. (PubMed:10748171)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti458 – 4581H → Q.7 Publications
    Corresponds to variant rs2058322 [ dbSNP | Ensembl ].
    VAR_068822

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei61 – 12161Missing in isoform 2. 1 PublicationVSP_044426Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025905 mRNA. Translation: BAA85003.1.
    AJ243467 mRNA. Translation: CAB65092.1.
    AF199414 mRNA. Translation: AAF86048.1. Frameshift.
    AK295956 mRNA. Translation: BAG58736.1.
    AB451326 mRNA. Translation: BAG70140.1.
    AB451469 mRNA. Translation: BAG70283.1.
    AC005785 Genomic DNA. No translation available.
    AC006128 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84475.1.
    BC000713 mRNA. Translation: AAH00713.1.
    AB015332 mRNA. Translation: BAA34791.1. Different initiation.
    CCDSiCCDS46005.1. [Q9ULX6-1]
    RefSeqiNP_001278407.1. NM_001291478.1.
    NP_055186.3. NM_014371.3.
    UniGeneiHs.399800.

    Genome annotation databases

    EnsembliENST00000397410; ENSP00000380557; ENSG00000011243. [Q9ULX6-1]
    ENST00000595465; ENSP00000470952; ENSG00000011243. [Q9ULX6-2]
    GeneIDi26993.
    KEGGihsa:26993.
    UCSCiuc002naw.1. human. [Q9ULX6-1]
    uc010xoh.1. human. [Q9ULX6-2]

    Polymorphism databases

    DMDMi296439446.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB025905 mRNA. Translation: BAA85003.1 .
    AJ243467 mRNA. Translation: CAB65092.1 .
    AF199414 mRNA. Translation: AAF86048.1 . Frameshift.
    AK295956 mRNA. Translation: BAG58736.1 .
    AB451326 mRNA. Translation: BAG70140.1 .
    AB451469 mRNA. Translation: BAG70283.1 .
    AC005785 Genomic DNA. No translation available.
    AC006128 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84475.1 .
    BC000713 mRNA. Translation: AAH00713.1 .
    AB015332 mRNA. Translation: BAA34791.1 . Different initiation.
    CCDSi CCDS46005.1. [Q9ULX6-1 ]
    RefSeqi NP_001278407.1. NM_001291478.1.
    NP_055186.3. NM_014371.3.
    UniGenei Hs.399800.

    3D structure databases

    ProteinModelPortali Q9ULX6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117940. 28 interactions.
    DIPi DIP-27541N.
    IntActi Q9ULX6. 16 interactions.
    MINTi MINT-1134534.
    STRINGi 9606.ENSP00000380557.

    PTM databases

    PhosphoSitei Q9ULX6.

    Polymorphism databases

    DMDMi 296439446.

    Proteomic databases

    MaxQBi Q9ULX6.
    PaxDbi Q9ULX6.
    PRIDEi Q9ULX6.

    Protocols and materials databases

    DNASUi 26993.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397410 ; ENSP00000380557 ; ENSG00000011243 . [Q9ULX6-1 ]
    ENST00000595465 ; ENSP00000470952 ; ENSG00000011243 . [Q9ULX6-2 ]
    GeneIDi 26993.
    KEGGi hsa:26993.
    UCSCi uc002naw.1. human. [Q9ULX6-1 ]
    uc010xoh.1. human. [Q9ULX6-2 ]

    Organism-specific databases

    CTDi 26993.
    GeneCardsi GC19M015490.
    H-InvDB HIX0014850.
    HIX0115658.
    HGNCi HGNC:29857. AKAP8L.
    HPAi HPA042485.
    HPA042546.
    MIMi 609475. gene.
    neXtProti NX_Q9ULX6.
    PharmGKBi PA134867364.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47695.
    HOGENOMi HOG000169111.
    HOVERGENi HBG104297.
    InParanoidi Q9ULX6.
    KOi K15978.
    OMAi DTNANPS.
    OrthoDBi EOG79SDWZ.
    PhylomeDBi Q9ULX6.
    TreeFami TF105407.

    Miscellaneous databases

    ChiTaRSi AKAP8L. human.
    GeneWikii AKAP8L.
    GenomeRNAii 26993.
    NextBioi 35472456.
    PROi Q9ULX6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ULX6.
    Bgeei Q9ULX6.
    CleanExi HS_AKAP8L.
    Genevestigatori Q9ULX6.

    Family and domain databases

    InterProi IPR007071. AKAP95.
    IPR015880. Znf_C2H2-like.
    [Graphical view ]
    PANTHERi PTHR12190. PTHR12190. 1 hit.
    Pfami PF04988. AKAP95. 1 hit.
    [Graphical view ]
    SMARTi SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of a novel human gene NAKAP95, neighbor of A-kinase anchoring protein 95 (AKAP95) on chromosome 19p13.11-p13.12 region."
      Seki N., Ueki N., Yano K., Saito T., Masuho Y., Muramatsu M.-A.
      J. Hum. Genet. 45:31-37(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    2. "Identification, cloning and characterization of a novel nuclear protein, HA95, homologous to A-kinase anchoring protein 95."
      Orstavik S., Eide T., Collas P., Han I.O., Tasken K., Kieff E., Jahnsen T., Skalhegg B.S.
      Biol. Cell 92:27-37(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-458.
    3. "A novel shuttle protein binds to RNA helicase A and activates the retroviral constitutive transport element."
      Westberg C., Yang J.-P., Tang H., Reddy T.R., Wong-Staal F.
      J. Biol. Chem. 275:21396-21401(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLN-458.
      Tissue: Placenta and T-cell lymphoma.
    4. "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 2), VARIANT GLN-458.
      Tissue: Substantia nigra.
    5. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLN-458.
    6. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLN-458.
    8. "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), VARIANT GLN-458.
      Tissue: Placenta.
    9. "Selection system for genes encoding nuclear-targeted proteins."
      Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.
      Nat. Biotechnol. 16:1338-1342(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-358 (ISOFORM 1), SUBCELLULAR LOCATION.
      Tissue: Fetal brain.
    10. "HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication."
      Martins S., Eikvar S., Furukawa K., Collas P.
      J. Cell Biol. 160:177-188(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TMPO-BETA.
    11. "In vitro modulation of the interaction between HA95 and LAP2beta by cAMP signaling."
      Martins S.B., Marstad A., Collas P.
      Biochemistry 42:10456-10461(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    12. "Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin: implications for nuclear toxicity in Huntington's disease pathogenesis."
      Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.
      NeuroMolecular Med. 7:297-310(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    13. "A cancer-associated RING finger protein, RNF43, is a ubiquitin ligase that interacts with a nuclear protein, HAP95."
      Sugiura T., Yamaguchi A., Miyamoto K.
      Exp. Cell Res. 314:1519-1528(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNF43.
    14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292 AND SER-297, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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 SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "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 SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-458, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAKP8L_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULX6
    Secondary accession number(s): B4DJ74
    , B5BU90, O94792, Q96J58, Q9NRQ0, Q9UGM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 137 of the entry and version 3 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 19
      Human chromosome 19: 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