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Q9P035

- HACD3_HUMAN

UniProt

Q9P035 - HACD3_HUMAN

Protein

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3

Gene

PTPLAD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Responsible for the dehydration step in very long-chain fatty acid (VLCFA) synthesis. Involved in Rac1-signaling pathways leading to the modulation of gene expression.2 Publications

    Catalytic activityi

    A very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H2O.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei286 – 2861By similarity
    Active sitei293 – 2931By similarity

    GO - Molecular functioni

    1. GTPase activator activity Source: ProtInc
    2. lyase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. activation of JUN kinase activity Source: ProtInc
    2. fatty acid biosynthetic process Source: UniProtKB-KW
    3. I-kappaB kinase/NF-kappaB signaling Source: ProtInc
    4. positive regulation of GTPase activity Source: GOC
    5. Rac protein signal transduction Source: UniProtKB
    6. Rho protein signal transduction Source: Ensembl
    7. small GTPase mediated signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 (EC:4.2.1.134)
    Alternative name(s):
    3-hydroxyacyl-CoA dehydratase 3
    Short name:
    HACD3
    Butyrate-induced protein 1
    Short name:
    B-ind1
    Short name:
    hB-ind1
    Protein tyrosine phosphatase-like protein PTPLAD1
    Protein-tyrosine phosphatase-like A domain-containing protein 1
    Gene namesi
    Name:PTPLAD1
    Synonyms:BIND1, HACD3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:24175. PTPLAD1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671113.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 362362Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3PRO_0000313724Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei114 – 1141Phosphoserine8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9P035.
    PaxDbiQ9P035.
    PRIDEiQ9P035.

    PTM databases

    PhosphoSiteiQ9P035.

    Expressioni

    Tissue specificityi

    Highly expressed in testis, kidney, brain, liver and weakly in skeletal muscle, spleen and heart. No expression detected in leukocytes.2 Publications

    Inductioni

    By AKAP12 and histone deacetylase inhibitors such as sodium butyrate.1 Publication

    Gene expression databases

    ArrayExpressiQ9P035.
    BgeeiQ9P035.
    CleanExiHS_PTPLAD1.
    GenevestigatoriQ9P035.

    Organism-specific databases

    HPAiHPA014837.

    Interactioni

    Subunit structurei

    Interacts with the condensation enzymes of the ELOVL family. Interacts with RAC1.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q034632EBI-359013,EBI-8803426From a different organism.
    Q99IB82EBI-359013,EBI-6927873From a different organism.
    Q9WMX23EBI-359013,EBI-6863748From a different organism.

    Protein-protein interaction databases

    BioGridi119570. 24 interactions.
    IntActiQ9P035. 21 interactions.
    MINTiMINT-1135933.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P035.
    SMRiQ9P035. Positions 5-158.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 149149CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini171 – 18515LumenalSequence AnalysisAdd
    BLAST
    Topological domaini208 – 21710CytoplasmicSequence Analysis
    Topological domaini236 – 2416LumenalSequence Analysis
    Topological domaini257 – 27923CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini299 – 32224LumenalSequence AnalysisAdd
    BLAST
    Topological domaini344 – 36219CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei150 – 17021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei186 – 20722HelicalSequence AnalysisAdd
    BLAST
    Transmembranei218 – 23518HelicalSequence AnalysisAdd
    BLAST
    Transmembranei242 – 25615HelicalSequence AnalysisAdd
    BLAST
    Transmembranei280 – 29819HelicalSequence AnalysisAdd
    BLAST
    Transmembranei323 – 34321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 9490CSPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili111 – 13626Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi350 – 3534Poly-Arg
    Compositional biasi357 – 3604Poly-Lys

    Sequence similaritiesi

    Contains 1 CS domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5198.
    HOVERGENiHBG108301.
    InParanoidiQ9P035.
    OrthoDBiEOG7BP82H.
    PhylomeDBiQ9P035.
    TreeFamiTF313326.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    InterProiIPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR007482. Tyr_Pase-like_PTPLA.
    [Graphical view]
    PANTHERiPTHR11035. PTHR11035. 1 hit.
    PfamiPF04969. CS. 1 hit.
    PF04387. PTPLA. 1 hit.
    [Graphical view]
    SUPFAMiSSF49764. SSF49764. 1 hit.
    PROSITEiPS51203. CS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P035-1) [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

    MENQVLTPHV YWAQRHRELY LRVELSDVQN PAISITENVL HFKAQGHGAK    50
    GDNVYEFHLE FLDLVKPEPV YKLTQRQVNI TVQKKVSQWW ERLTKQEKRP 100
    LFLAPDFDRW LDESDAEMEL RAKEEERLNK LRLESEGSPE TLTNLRKGYL 150
    FMYNLVQFLG FSWIFVNLTV RFCILGKESF YDTFHTVADM MYFCQMLAVV 200
    ETINAAIGVT TSPVLPSLIQ LLGRNFILFI IFGTMEEMQN KAVVFFVFYL 250
    WSAIEIFRYS FYMLTCIDMD WKVLTWLRYT LWIPLYPLGC LAEAVSVIQS 300
    IPIFNETGRF SFTLPYPVKI KVRFSFFLQI YLIMIFLGLY INFRHLYKQR 350
    RRRYGQKKKK IH 362
    Length:362
    Mass (Da):43,160
    Last modified:January 15, 2008 - v2
    Checksum:i1B3591E88DD85D16
    GO
    Isoform 2 (identifier: Q9P035-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         69-123: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:307
    Mass (Da):36,431
    Checksum:iB14E762EB96B17F8
    GO

    Sequence cautioni

    The sequence AAF29085.1 differs from that shown. Reason: Frameshift at position 356.
    The sequence BAC11249.1 differs from that shown. Reason: Frameshift at position 359.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601E → K in BAB55101. (PubMed:14702039)Curated
    Sequence conflicti245 – 2451F → I in BAC11277. (PubMed:14702039)Curated
    Sequence conflicti282 – 2821W → G in AAH35508. (PubMed:15489334)Curated
    Sequence conflicti292 – 2921A → V in AAF29085. (PubMed:11042152)Curated
    Sequence conflicti352 – 36211RRYGQKKKKIH → LKMRAGAVAHACDPSALGG in CAB69070. (PubMed:10747961)CuratedAdd
    BLAST
    Sequence conflicti361 – 3611I → K in AAH35508. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561E → K.
    Corresponds to variant rs11632737 [ dbSNP | Ensembl ].
    VAR_037712
    Natural varianti269 – 2691M → L.
    Corresponds to variant rs2279854 [ dbSNP | Ensembl ].
    VAR_037713

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei69 – 12355Missing in isoform 2. 1 PublicationVSP_056070Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ271091 mRNA. Translation: CAB69070.1.
    AF161470 mRNA. Translation: AAF29085.1. Frameshift.
    AK027421 mRNA. Translation: BAB55101.1.
    AK074857 mRNA. Translation: BAC11249.1. Frameshift.
    AK074898 mRNA. Translation: BAC11277.1.
    AK299234 mRNA. Translation: BAG61266.1.
    AC011846 Genomic DNA. No translation available.
    AC027220 Genomic DNA. No translation available.
    BC019873 mRNA. Translation: AAH19873.1.
    BC035508 mRNA. Translation: AAH35508.1.
    BC047685 mRNA. Translation: AAH47685.1.
    BC058912 mRNA. Translation: AAH58912.1.
    DQ251107 Genomic DNA. Translation: ABB83547.1.
    CCDSiCCDS45282.1.
    RefSeqiNP_057479.2. NM_016395.2.
    UniGeneiHs.512973.

    Genome annotation databases

    EnsembliENST00000261875; ENSP00000261875; ENSG00000074696.
    ENST00000442729; ENSP00000392491; ENSG00000074696.
    GeneIDi51495.
    KEGGihsa:51495.
    UCSCiuc002apc.3. human.

    Polymorphism databases

    DMDMi166199462.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ271091 mRNA. Translation: CAB69070.1 .
    AF161470 mRNA. Translation: AAF29085.1 . Frameshift.
    AK027421 mRNA. Translation: BAB55101.1 .
    AK074857 mRNA. Translation: BAC11249.1 . Frameshift.
    AK074898 mRNA. Translation: BAC11277.1 .
    AK299234 mRNA. Translation: BAG61266.1 .
    AC011846 Genomic DNA. No translation available.
    AC027220 Genomic DNA. No translation available.
    BC019873 mRNA. Translation: AAH19873.1 .
    BC035508 mRNA. Translation: AAH35508.1 .
    BC047685 mRNA. Translation: AAH47685.1 .
    BC058912 mRNA. Translation: AAH58912.1 .
    DQ251107 Genomic DNA. Translation: ABB83547.1 .
    CCDSi CCDS45282.1.
    RefSeqi NP_057479.2. NM_016395.2.
    UniGenei Hs.512973.

    3D structure databases

    ProteinModelPortali Q9P035.
    SMRi Q9P035. Positions 5-158.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119570. 24 interactions.
    IntActi Q9P035. 21 interactions.
    MINTi MINT-1135933.

    PTM databases

    PhosphoSitei Q9P035.

    Polymorphism databases

    DMDMi 166199462.

    Proteomic databases

    MaxQBi Q9P035.
    PaxDbi Q9P035.
    PRIDEi Q9P035.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261875 ; ENSP00000261875 ; ENSG00000074696 .
    ENST00000442729 ; ENSP00000392491 ; ENSG00000074696 .
    GeneIDi 51495.
    KEGGi hsa:51495.
    UCSCi uc002apc.3. human.

    Organism-specific databases

    CTDi 51495.
    GeneCardsi GC15P065822.
    H-InvDB HIX0012353.
    HGNCi HGNC:24175. PTPLAD1.
    HPAi HPA014837.
    neXtProti NX_Q9P035.
    PharmGKBi PA142671113.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5198.
    HOVERGENi HBG108301.
    InParanoidi Q9P035.
    OrthoDBi EOG7BP82H.
    PhylomeDBi Q9P035.
    TreeFami TF313326.

    Miscellaneous databases

    ChiTaRSi PTPLAD1. human.
    GeneWikii PTPLAD1.
    GenomeRNAii 51495.
    NextBioi 55161.
    PROi Q9P035.

    Gene expression databases

    ArrayExpressi Q9P035.
    Bgeei Q9P035.
    CleanExi HS_PTPLAD1.
    Genevestigatori Q9P035.

    Family and domain databases

    Gene3Di 2.60.40.790. 1 hit.
    InterProi IPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR007482. Tyr_Pase-like_PTPLA.
    [Graphical view ]
    PANTHERi PTHR11035. PTHR11035. 1 hit.
    Pfami PF04969. CS. 1 hit.
    PF04387. PTPLA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49764. SSF49764. 1 hit.
    PROSITEi PS51203. CS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "B-ind1, a novel mediator of Rac1 signaling cloned from sodium butyrate-treated fibroblasts."
      Courilleau D., Chastre E., Sabbah M., Redeuilh G., Atfi A., Mester J.
      J. Biol. Chem. 275:17344-17348(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RAC1, TISSUE SPECIFICITY.
    2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    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] (ISOFORMS 1 AND 2).
    4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      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: B-cell, Duodenum, Eye and Urinary bladder.
    6. "Human B-ind1 gene promoter: cloning and regulation by histone deacetylase inhibitors."
      Sabbah M., Saucier C., Redeuilh G.
      Gene 374:128-133(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
    7. "SSeCKS/Gravin/AKAP12 attenuates expression of proliferative and angiogenic genes during suppression of v-Src-induced oncogenesis."
      Liu Y., Gao L., Gelman I.H.
      BMC Cancer 6:105-105(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY AKAP12.
    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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis."
      Ikeda M., Kanao Y., Yamanaka M., Sakuraba H., Mizutani Y., Igarashi Y., Kihara A.
      FEBS Lett. 582:2435-2440(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, INTERACTION WITH ELOVL FAMILY.
    10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiHACD3_HUMAN
    AccessioniPrimary (citable) accession number: Q9P035
    Secondary accession number(s): A0PJA1
    , B4DRF4, Q280Z3, Q6PD63, Q8IUI5, Q8NC86, Q8NCB1, Q96T12, Q9NQA7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 98 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3