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Q9HB71

- CYBP_HUMAN

UniProt

Q9HB71 - CYBP_HUMAN

Protein

Calcyclin-binding protein

Gene

CACYBP

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 124 (01 Oct 2014)
      Sequence version 2 (26 Apr 2004)
      Previous versions | rss
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    Functioni

    May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1).1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. cardiac muscle cell differentiation Source: Ensembl
    3. cellular response to calcium ion Source: Ensembl
    4. negative regulation of cell death Source: Ensembl
    5. positive regulation of DNA replication Source: Ensembl
    6. response to growth hormone Source: Ensembl

    Keywords - Biological processi

    Ubl conjugation pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcyclin-binding protein
    Short name:
    CacyBP
    Short name:
    hCacyBP
    Alternative name(s):
    S100A6-binding protein
    Siah-interacting protein
    Gene namesi
    Name:CACYBP
    Synonyms:S100A6BP, SIP
    ORF Names:PNAS-107
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:30423. CACYBP.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Cytoplasmic at low calcium concentrations. In neuroblastoma cells, after a retinoic acid (RA) induction and calcium increase, it localizes in both the nucleus and cytoplasm. The nuclear fraction may be phosphorylated.

    GO - Cellular componenti

    1. beta-catenin destruction complex Source: UniProtKB
    2. cell body Source: Ensembl
    3. cytoplasm Source: HPA
    4. extracellular vesicular exosome Source: UniProt
    5. neuron projection Source: Ensembl
    6. nuclear envelope lumen Source: Ensembl
    7. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi23 – 264KRVR → AAVA: Abolishes interaction with SIAH1.
    Mutagenesisi64 – 641V → N: Abolishes interaction with SIAH1; when associated with N-66. 1 Publication
    Mutagenesisi66 – 661P → N: Abolishes interaction with SIAH1; when associated with N-64. 1 Publication

    Organism-specific databases

    PharmGKBiPA134894213.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed6 Publications
    Chaini2 – 228227Calcyclin-binding proteinPRO_0000185389Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine6 Publications
    Modified residuei8 – 81N6-acetyllysine1 Publication
    Modified residuei19 – 191N6-acetyllysine1 Publication
    Modified residuei85 – 851N6-acetyllysine1 Publication
    Modified residuei118 – 1181N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated on serine residues. Phosphorylated upon induction by RA or at high calcium concentrations.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9HB71.
    PaxDbiQ9HB71.
    PRIDEiQ9HB71.

    2D gel databases

    UCD-2DPAGEQ9HB71.

    PTM databases

    PhosphoSiteiQ9HB71.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HB71.
    BgeeiQ9HB71.
    CleanExiHS_CACYBP.
    GenevestigatoriQ9HB71.

    Organism-specific databases

    HPAiHPA025753.
    HPA057038.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with proteins of the S100 family S100A1, S100A6, S100B, S100P and S100A12 in a calcium-dependent manner By similarity. Component of some large E3 complex at least composed of UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts directly with SIAH1, SIAH2 and SKP1.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi118001. 32 interactions.
    IntActiQ9HB71. 83 interactions.
    MINTiMINT-200516.
    STRINGi9606.ENSP00000356652.

    Structurei

    Secondary structure

    1
    228
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1917
    Helixi23 – 4624
    Beta strandi61 – 644
    Beta strandi79 – 835
    Beta strandi86 – 927
    Turni94 – 985
    Beta strandi103 – 1086
    Beta strandi110 – 1178
    Beta strandi121 – 1233
    Beta strandi125 – 1306
    Beta strandi132 – 1343
    Turni138 – 1403
    Beta strandi142 – 1465
    Beta strandi149 – 1557
    Beta strandi157 – 1604
    Beta strandi164 – 1674
    Helixi168 – 1747

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X5MNMR-A63-176[»]
    2A25X-ray2.20B58-70[»]
    2A26X-ray1.20A/B/C1-47[»]
    ProteinModelPortaliQ9HB71.
    SMRiQ9HB71. Positions 1-47, 61-180, 188-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HB71.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini73 – 16795CSPROSITE-ProRule annotationAdd
    BLAST
    Domaini168 – 22861SGSPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 8079Interaction with SIAH1Add
    BLAST
    Regioni73 – 228156Interaction with SKP1Add
    BLAST
    Regioni154 – 22875Interaction with S100A6By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CS domain.PROSITE-ProRule annotation
    Contains 1 SGS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG247905.
    HOGENOMiHOG000238284.
    HOVERGENiHBG003242.
    InParanoidiQ9HB71.
    KOiK04507.
    OMAiVNFTERS.
    OrthoDBiEOG7K9K4J.
    PhylomeDBiQ9HB71.
    TreeFamiTF323891.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    InterProiIPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR007699. SGS.
    IPR015120. Siah-Interact_N.
    [Graphical view]
    PfamiPF04969. CS. 1 hit.
    PF05002. SGS. 1 hit.
    PF09032. Siah-Interact_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF49764. SSF49764. 1 hit.
    PROSITEiPS51203. CS. 1 hit.
    PS51048. SGS. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HB71-1) [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

    MASEELQKDL EEVKVLLEKA TRKRVRDALT AEKSKIETEI KNKMQQKSQK    50
    KAELLDNEKP AAVVAPITTG YTVKISNYGW DQSDKFVKIY ITLTGVHQVP 100
    TENVQVHFTE RSFDLLVKNL NGKSYSMIVN NLLKPISVEG SSKKVKTDTV 150
    LILCRKKVEN TRWDYLTQVE KECKEKEKPS YDTETDPSEG LMNVLKKIYE 200
    DGDDDMKRTI NKAWVESREK QAKGDTEF 228
    Length:228
    Mass (Da):26,210
    Last modified:April 26, 2004 - v2
    Checksum:i88C822FB14A7EF89
    GO
    Isoform 2 (identifier: Q9HB71-2) [UniParc]FASTAAdd to Basket

    Also known as: SIP-S, S

    The sequence of this isoform differs from the canonical sequence as follows:
         73-80: VKISNYGW → DGISQISL
         81-228: Missing.

    Show »
    Length:80
    Mass (Da):8,956
    Checksum:i13A2FAC2429FA9FD
    GO
    Isoform 3 (identifier: Q9HB71-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-43: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:185
    Mass (Da):21,228
    Checksum:i99286837B26B2395
    GO

    Sequence cautioni

    The sequence AAG23817.1 differs from that shown. Reason: Frameshift at position 203.
    The sequence BAG52713.1 differs from that shown. Reason: Frameshift at position 3.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441M → V in AAG23817. 1 PublicationCurated
    Sequence conflicti177 – 1771E → K in AAG23817. 1 PublicationCurated
    Sequence conflicti183 – 1831T → P in AAG23817. 1 PublicationCurated
    Sequence conflicti226 – 2261T → P in AAG23817. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4343Missing in isoform 3. 1 PublicationVSP_046862Add
    BLAST
    Alternative sequencei73 – 808VKISNYGW → DGISQISL in isoform 2. CuratedVSP_010171
    Alternative sequencei81 – 228148Missing in isoform 2. CuratedVSP_010172Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF057356 mRNA. Translation: AAC21458.1.
    AF314752 mRNA. Translation: AAG34170.1.
    AL035305 mRNA. Translation: CAA22910.1.
    AF275803 mRNA. Translation: AAG23817.1. Frameshift.
    AY423723 mRNA. Translation: AAS00486.1.
    AK093425 mRNA. Translation: BAG52713.1. Frameshift.
    AK313278 mRNA. Translation: BAG36086.1.
    Z99127 Genomic DNA. Translation: CAI18938.1.
    Z99127 Genomic DNA. Translation: CAQ52581.1.
    CH471067 Genomic DNA. Translation: EAW90982.1.
    BC005975 mRNA. Translation: AAH05975.1.
    BC022352 mRNA. Translation: AAH22352.1.
    BC078151 mRNA. Translation: AAH78151.1.
    CCDSiCCDS1315.1. [Q9HB71-1]
    CCDS30942.1. [Q9HB71-3]
    RefSeqiNP_001007215.1. NM_001007214.1. [Q9HB71-3]
    NP_055227.1. NM_014412.2. [Q9HB71-1]
    XP_005245149.1. XM_005245092.1. [Q9HB71-3]
    UniGeneiHs.508524.

    Genome annotation databases

    EnsembliENST00000367679; ENSP00000356652; ENSG00000116161. [Q9HB71-1]
    ENST00000405362; ENSP00000385771; ENSG00000116161. [Q9HB71-3]
    ENST00000406752; ENSP00000384139; ENSG00000116161. [Q9HB71-2]
    GeneIDi27101.
    KEGGihsa:27101.
    UCSCiuc001gki.1. human. [Q9HB71-1]

    Polymorphism databases

    DMDMi46576651.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF057356 mRNA. Translation: AAC21458.1 .
    AF314752 mRNA. Translation: AAG34170.1 .
    AL035305 mRNA. Translation: CAA22910.1 .
    AF275803 mRNA. Translation: AAG23817.1 . Frameshift.
    AY423723 mRNA. Translation: AAS00486.1 .
    AK093425 mRNA. Translation: BAG52713.1 . Frameshift.
    AK313278 mRNA. Translation: BAG36086.1 .
    Z99127 Genomic DNA. Translation: CAI18938.1 .
    Z99127 Genomic DNA. Translation: CAQ52581.1 .
    CH471067 Genomic DNA. Translation: EAW90982.1 .
    BC005975 mRNA. Translation: AAH05975.1 .
    BC022352 mRNA. Translation: AAH22352.1 .
    BC078151 mRNA. Translation: AAH78151.1 .
    CCDSi CCDS1315.1. [Q9HB71-1 ]
    CCDS30942.1. [Q9HB71-3 ]
    RefSeqi NP_001007215.1. NM_001007214.1. [Q9HB71-3 ]
    NP_055227.1. NM_014412.2. [Q9HB71-1 ]
    XP_005245149.1. XM_005245092.1. [Q9HB71-3 ]
    UniGenei Hs.508524.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X5M NMR - A 63-176 [» ]
    2A25 X-ray 2.20 B 58-70 [» ]
    2A26 X-ray 1.20 A/B/C 1-47 [» ]
    ProteinModelPortali Q9HB71.
    SMRi Q9HB71. Positions 1-47, 61-180, 188-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118001. 32 interactions.
    IntActi Q9HB71. 83 interactions.
    MINTi MINT-200516.
    STRINGi 9606.ENSP00000356652.

    PTM databases

    PhosphoSitei Q9HB71.

    Polymorphism databases

    DMDMi 46576651.

    2D gel databases

    UCD-2DPAGE Q9HB71.

    Proteomic databases

    MaxQBi Q9HB71.
    PaxDbi Q9HB71.
    PRIDEi Q9HB71.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367679 ; ENSP00000356652 ; ENSG00000116161 . [Q9HB71-1 ]
    ENST00000405362 ; ENSP00000385771 ; ENSG00000116161 . [Q9HB71-3 ]
    ENST00000406752 ; ENSP00000384139 ; ENSG00000116161 . [Q9HB71-2 ]
    GeneIDi 27101.
    KEGGi hsa:27101.
    UCSCi uc001gki.1. human. [Q9HB71-1 ]

    Organism-specific databases

    CTDi 27101.
    GeneCardsi GC01P174968.
    HGNCi HGNC:30423. CACYBP.
    HPAi HPA025753.
    HPA057038.
    MIMi 606186. gene.
    neXtProti NX_Q9HB71.
    PharmGKBi PA134894213.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG247905.
    HOGENOMi HOG000238284.
    HOVERGENi HBG003242.
    InParanoidi Q9HB71.
    KOi K04507.
    OMAi VNFTERS.
    OrthoDBi EOG7K9K4J.
    PhylomeDBi Q9HB71.
    TreeFami TF323891.

    Miscellaneous databases

    ChiTaRSi CACYBP. human.
    EvolutionaryTracei Q9HB71.
    GeneWikii CACYBP.
    GenomeRNAii 27101.
    NextBioi 49757.
    PROi Q9HB71.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HB71.
    Bgeei Q9HB71.
    CleanExi HS_CACYBP.
    Genevestigatori Q9HB71.

    Family and domain databases

    Gene3Di 2.60.40.790. 1 hit.
    InterProi IPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR007699. SGS.
    IPR015120. Siah-Interact_N.
    [Graphical view ]
    Pfami PF04969. CS. 1 hit.
    PF05002. SGS. 1 hit.
    PF09032. Siah-Interact_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49764. SSF49764. 1 hit.
    PROSITEi PS51203. CS. 1 hit.
    PS51048. SGS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of human calcyclin binding protein (hCacyBP) gene."
      Liu W.X., Wu J., Zhao Z., Zhou Y., Peng X.Z., Yuan J.G., Qiang B.Q.
      Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:181-186(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Amplification and overexpression of the gene encoding the human calcyclin binding protein on chromosome 1q24-q25 in advanced lung carcinomas."
      Petersen S., Schluens K., Dietel M., Petersen I.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Rhodes S.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Human acute promyelocytic leukemia cell line NB4's apoptosis related genes."
      Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Promyelocytic leukemia.
    5. "Identification of a human growth inhibition gene 5 (GIG5)."
      Kim J.W.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "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] (ISOFORMS 1 AND 3).
      Tissue: Skeletal muscle and Testis.
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 and Skin.
    10. Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14; 34-41; 112-118 AND 124-143, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hepatoma.
    11. Bienvenut W.V., Heiserich L., Gottlieb E.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-19 AND 112-118, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    12. "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses."
      Matsuzawa S., Reed J.C.
      Mol. Cell 7:915-926(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 2), SUBUNIT OF A COMPLEX WITH UBE2D1; SIAH1; SKP1; APC AND TBL1X, INTERACTION WITH SIAH1; SIAH2 AND SKP1.
    13. "Translocation and phosphorylation of calcyclin binding protein during retinoic acid-induced neuronal differentiation of neuroblastoma SH-SY5Y cells."
      Wu J., Tan X., Peng X.Z., Yuan J.G., Qiang B.Q.
      J. Biochem. Mol. Biol. 36:354-358(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    14. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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 ALA-2; LYS-8; LYS-19; LYS-85 AND LYS-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex."
      Santelli E., Leone M., Li C., Fukushima T., Preece N.E., Olson A.J., Ely K.R., Reed J.C., Pellecchia M., Liddington R.C., Matsuzawa S.
      J. Biol. Chem. 280:34278-34287(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 1-70, SUBUNIT, MUTAGENESIS OF 23-LYS--ARG-26; VAL-64 AND PRO-66, FUNCTION, INTERACTION WITH SIAH1.
    21. "Solution structure of the core domain of calcyclin binding protein; SIAH-interacting protein (SIP)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 63-176.

    Entry informationi

    Entry nameiCYBP_HUMAN
    AccessioniPrimary (citable) accession number: Q9HB71
    Secondary accession number(s): B2ZWH2
    , B3KSF1, O60666, Q5R370, Q5R371
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: April 26, 2004
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3