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Q5SSJ5

- HP1B3_HUMAN

UniProt

Q5SSJ5 - HP1B3_HUMAN

Protein

Heterochromatin protein 1-binding protein 3

Gene

HP1BP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Component of heterochromatin, may be involved in chromatin structure and function.By similarity

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. nucleosome assembly Source: InterPro

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heterochromatin protein 1-binding protein 3
    Alternative name(s):
    Protein HP1-BP74
    Gene namesi
    Name:HP1BP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:24973. HP1BP3.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation. Chromosome PROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleosome Source: InterPro
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671673.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 553552Heterochromatin protein 1-binding protein 3PRO_0000339642Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei6 – 61Phosphoserine1 Publication
    Modified residuei142 – 1421Phosphoserine2 Publications
    Modified residuei155 – 1551Phosphoserine1 Publication
    Modified residuei156 – 1561Phosphoserine1 Publication
    Modified residuei190 – 1901N6-acetyllysineBy similarity
    Modified residuei248 – 2481Phosphoserine2 Publications
    Modified residuei249 – 2491Phosphoserine2 Publications
    Modified residuei441 – 4411Phosphoserine1 Publication
    Modified residuei442 – 4421Phosphoserine1 Publication
    Modified residuei446 – 4461Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ5SSJ5.
    PaxDbiQ5SSJ5.
    PRIDEiQ5SSJ5.

    PTM databases

    PhosphoSiteiQ5SSJ5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5SSJ5.
    BgeeiQ5SSJ5.
    CleanExiHS_HP1BP3.
    GenevestigatoriQ5SSJ5.

    Organism-specific databases

    HPAiHPA028215.
    HPA054295.

    Interactioni

    Subunit structurei

    Interacts with CBX5.By similarity

    Protein-protein interaction databases

    BioGridi119128. 53 interactions.
    IntActiQ5SSJ5. 6 interactions.
    MINTiMINT-4719917.

    Structurei

    Secondary structure

    1
    553
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi161 – 17515
    Helixi180 – 19011
    Helixi194 – 1974
    Turni198 – 2025
    Helixi203 – 21412
    Turni224 – 2263
    Turni231 – 2344

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RQPNMR-A153-237[»]
    ProteinModelPortaliQ5SSJ5.
    SMRiQ5SSJ5. Positions 153-237, 255-334.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ5SSJ5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini157 – 23276H15 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini255 – 33076H15 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini337 – 41377H15 3PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi454 – 553100Lys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 3 H15 (linker histone H1/H5 globular) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG285312.
    HOVERGENiHBG097678.
    InParanoidiQ5SSJ5.
    OMAiASMKQRG.
    OrthoDBiEOG75QR72.
    PhylomeDBiQ5SSJ5.
    TreeFamiTF106395.

    Family and domain databases

    Gene3Di1.10.10.10. 3 hits.
    InterProiIPR005818. Histone_H1/H5_H15.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00538. Linker_histone. 3 hits.
    [Graphical view]
    SMARTiSM00526. H15. 3 hits.
    [Graphical view]
    PROSITEiPS51504. H15. 3 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5SSJ5-1) [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

    MATDTSQGEL VHPKALPLIV GAQLIHADKL GEKVEDSTMP IRRTVNSTRE    50
    TPPKSKLAEG EEEKPEPDIS SEESVSTVEE QENETPPATS SEAEQPKGEP 100
    ENEEKEENKS SEETKKDEKD QSKEKEKKVK KTIPSWATLS ASQLARAQKQ 150
    TPMASSPRPK MDAILTEAIK ACFQKSGASV VAIRKYIIHK YPSLELERRG 200
    YLLKQALKRE LNRGVIKQVK GKGASGSFVV VQKSRKTPQK SRNRKNRSSA 250
    VDPEPQVKLE DVLPLAFTRL CEPKEASYSL IRKYVSQYYP KLRVDIRPQL 300
    LKNALQRAVE RGQLEQITGK GASGTFQLKK SGEKPLLGGS LMEYAILSAI 350
    AAMNEPKTCS TTALKKYVLE NHPGTNSNYQ MHLLKKTLQK CEKNGWMEQI 400
    SGKGFSGTFQ LCFPYYPSPG VLFPKKEPDD SRDEDEDEDE SSEEDSEDEE 450
    PPPKRRLQKK TPAKSPGKAA SVKQRGSKPA PKVSAAQRGK ARPLPKKAPP 500
    KAKTPAKKTR PSSTVIKKPS GGSSKKPATS ARKEVKLPGK GKSTMKKSFR 550
    VKK 553
    Length:553
    Mass (Da):61,207
    Last modified:December 21, 2004 - v1
    Checksum:iD18B28EE0156F09B
    GO
    Isoform 2 (identifier: Q5SSJ5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-38: Missing.

    Show »
    Length:515
    Mass (Da):57,211
    Checksum:i130AD6B3FFD97525
    GO
    Isoform 3 (identifier: Q5SSJ5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-152: Missing.

    Show »
    Length:401
    Mass (Da):44,435
    Checksum:i31A31A118D2508B7
    GO
    Isoform 4 (identifier: Q5SSJ5-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         117-133: DEKDQSKEKEKKVKKTI → ERADSIHSTLFIIGQNS
         134-553: Missing.

    Show »
    Length:133
    Mass (Da):14,594
    Checksum:i87E1DE4A3A8FB907
    GO

    Sequence cautioni

    The sequence AAF14871.1 differs from that shown. Reason: Frameshift at positions 226, 237 and 243.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti262 – 2621V → G in AAF14871. (PubMed:10931946)Curated
    Sequence conflicti267 – 2671F → S in BAF83941. (PubMed:14702039)Curated
    Sequence conflicti499 – 4991P → S in BAG64972. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 152152Missing in isoform 3. 2 PublicationsVSP_034168Add
    BLAST
    Alternative sequencei1 – 3838Missing in isoform 2. 1 PublicationVSP_034169Add
    BLAST
    Alternative sequencei117 – 13317DEKDQ…VKKTI → ERADSIHSTLFIIGQNS in isoform 4. 1 PublicationVSP_034170Add
    BLAST
    Alternative sequencei134 – 553420Missing in isoform 4. 1 PublicationVSP_034171Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF113534 mRNA. Translation: AAF14871.1. Frameshift.
    AK023129 mRNA. Translation: BAG51160.1.
    AK291252 mRNA. Translation: BAF83941.1.
    AK304065 mRNA. Translation: BAG64972.1.
    AL833978 mRNA. Translation: CAD38822.1.
    AL606477, AL663074 Genomic DNA. Translation: CAI12528.1.
    AL606477, AL663074 Genomic DNA. Translation: CAI12530.1.
    AL606477 Genomic DNA. Translation: CAI12531.1.
    AL606477 Genomic DNA. Translation: CAI12532.1.
    AL606477, AL663074 Genomic DNA. Translation: CAI12533.1.
    AL663074, AL606477 Genomic DNA. Translation: CAI23387.1.
    AL663074, AL606477 Genomic DNA. Translation: CAI23388.1.
    AL663074, AL606477 Genomic DNA. Translation: CAI23389.1.
    CH471134 Genomic DNA. Translation: EAW94953.1.
    BC032139 mRNA. Translation: AAH32139.1.
    BC045660 mRNA. Translation: AAH45660.1.
    CCDSiCCDS30621.1. [Q5SSJ5-1]
    RefSeqiNP_057371.2. NM_016287.3. [Q5SSJ5-1]
    XP_005245932.1. XM_005245875.2. [Q5SSJ5-1]
    XP_005245933.1. XM_005245876.2. [Q5SSJ5-1]
    XP_005245934.1. XM_005245877.2. [Q5SSJ5-1]
    XP_005245935.1. XM_005245878.2. [Q5SSJ5-1]
    XP_005245936.1. XM_005245879.2. [Q5SSJ5-2]
    UniGeneiHs.142442.

    Genome annotation databases

    EnsembliENST00000312239; ENSP00000312625; ENSG00000127483. [Q5SSJ5-1]
    ENST00000375000; ENSP00000364139; ENSG00000127483. [Q5SSJ5-5]
    ENST00000375003; ENSP00000364142; ENSG00000127483. [Q5SSJ5-3]
    GeneIDi50809.
    KEGGihsa:50809.
    UCSCiuc001bdv.1. human. [Q5SSJ5-1]
    uc001bea.2. human. [Q5SSJ5-2]
    uc001beb.3. human. [Q5SSJ5-5]

    Polymorphism databases

    DMDMi74743691.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF113534 mRNA. Translation: AAF14871.1 . Frameshift.
    AK023129 mRNA. Translation: BAG51160.1 .
    AK291252 mRNA. Translation: BAF83941.1 .
    AK304065 mRNA. Translation: BAG64972.1 .
    AL833978 mRNA. Translation: CAD38822.1 .
    AL606477 , AL663074 Genomic DNA. Translation: CAI12528.1 .
    AL606477 , AL663074 Genomic DNA. Translation: CAI12530.1 .
    AL606477 Genomic DNA. Translation: CAI12531.1 .
    AL606477 Genomic DNA. Translation: CAI12532.1 .
    AL606477 , AL663074 Genomic DNA. Translation: CAI12533.1 .
    AL663074 , AL606477 Genomic DNA. Translation: CAI23387.1 .
    AL663074 , AL606477 Genomic DNA. Translation: CAI23388.1 .
    AL663074 , AL606477 Genomic DNA. Translation: CAI23389.1 .
    CH471134 Genomic DNA. Translation: EAW94953.1 .
    BC032139 mRNA. Translation: AAH32139.1 .
    BC045660 mRNA. Translation: AAH45660.1 .
    CCDSi CCDS30621.1. [Q5SSJ5-1 ]
    RefSeqi NP_057371.2. NM_016287.3. [Q5SSJ5-1 ]
    XP_005245932.1. XM_005245875.2. [Q5SSJ5-1 ]
    XP_005245933.1. XM_005245876.2. [Q5SSJ5-1 ]
    XP_005245934.1. XM_005245877.2. [Q5SSJ5-1 ]
    XP_005245935.1. XM_005245878.2. [Q5SSJ5-1 ]
    XP_005245936.1. XM_005245879.2. [Q5SSJ5-2 ]
    UniGenei Hs.142442.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RQP NMR - A 153-237 [» ]
    ProteinModelPortali Q5SSJ5.
    SMRi Q5SSJ5. Positions 153-237, 255-334.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119128. 53 interactions.
    IntActi Q5SSJ5. 6 interactions.
    MINTi MINT-4719917.

    PTM databases

    PhosphoSitei Q5SSJ5.

    Polymorphism databases

    DMDMi 74743691.

    Proteomic databases

    MaxQBi Q5SSJ5.
    PaxDbi Q5SSJ5.
    PRIDEi Q5SSJ5.

    Protocols and materials databases

    DNASUi 50809.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000312239 ; ENSP00000312625 ; ENSG00000127483 . [Q5SSJ5-1 ]
    ENST00000375000 ; ENSP00000364139 ; ENSG00000127483 . [Q5SSJ5-5 ]
    ENST00000375003 ; ENSP00000364142 ; ENSG00000127483 . [Q5SSJ5-3 ]
    GeneIDi 50809.
    KEGGi hsa:50809.
    UCSCi uc001bdv.1. human. [Q5SSJ5-1 ]
    uc001bea.2. human. [Q5SSJ5-2 ]
    uc001beb.3. human. [Q5SSJ5-5 ]

    Organism-specific databases

    CTDi 50809.
    GeneCardsi GC01M021069.
    HGNCi HGNC:24973. HP1BP3.
    HPAi HPA028215.
    HPA054295.
    neXtProti NX_Q5SSJ5.
    PharmGKBi PA142671673.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG285312.
    HOVERGENi HBG097678.
    InParanoidi Q5SSJ5.
    OMAi ASMKQRG.
    OrthoDBi EOG75QR72.
    PhylomeDBi Q5SSJ5.
    TreeFami TF106395.

    Miscellaneous databases

    ChiTaRSi HP1BP3. human.
    EvolutionaryTracei Q5SSJ5.
    GeneWikii HP1BP3.
    GenomeRNAii 50809.
    NextBioi 53250.
    PROi Q5SSJ5.

    Gene expression databases

    ArrayExpressi Q5SSJ5.
    Bgeei Q5SSJ5.
    CleanExi HS_HP1BP3.
    Genevestigatori Q5SSJ5.

    Family and domain databases

    Gene3Di 1.10.10.10. 3 hits.
    InterProi IPR005818. Histone_H1/H5_H15.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00538. Linker_histone. 3 hits.
    [Graphical view ]
    SMARTi SM00526. H15. 3 hits.
    [Graphical view ]
    PROSITEi PS51504. H15. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hypothalamus.
    2. "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 2).
      Tissue: Teratocarcinoma and Trachea.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 3 AND 4).
      Tissue: Brain and Testis.
    7. Bienvenut W.V., Calvo F., Kolch W.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 132-146; 176-184; 275-282; 284-291; 294-302 AND 312-329, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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.
    13. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-142; SER-155; SER-156; SER-248 AND SER-249, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-441; SER-442 AND SER-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHP1B3_HUMAN
    AccessioniPrimary (citable) accession number: Q5SSJ5
    Secondary accession number(s): A6NI71
    , A8K5D7, B3KMZ8, B4E210, Q05BI0, Q5SSJ6, Q5SWC6, Q6PIM9, Q8NDF0, Q9UHY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 102 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

    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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3