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Q05682

- CALD1_HUMAN

UniProt

Q05682 - CALD1_HUMAN

Protein

Caldesmon

Gene

CALD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (28 Jun 2011)
      Previous versions | rss
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    Functioni

    Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration By similarity.By similarity

    GO - Molecular functioni

    1. actin binding Source: ProtInc
    2. calmodulin binding Source: ProtInc
    3. tropomyosin binding Source: ProtInc

    GO - Biological processi

    1. cellular component movement Source: UniProtKB
    2. muscle contraction Source: Reactome

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Actin-binding, Calmodulin-binding

    Enzyme and pathway databases

    ReactomeiREACT_20558. Smooth Muscle Contraction.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Caldesmon
    Short name:
    CDM
    Gene namesi
    Name:CALD1
    Synonyms:CAD, CDM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:1441. CALD1.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. Cytoplasmmyofibril By similarity
    Note: On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle).By similarity

    GO - Cellular componenti

    1. actin cap Source: Ensembl
    2. actin cytoskeleton Source: HPA
    3. cytoskeleton Source: UniProtKB
    4. cytosol Source: Reactome
    5. myofibril Source: UniProtKB-SubCell
    6. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26034.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 793793CaldesmonPRO_0000089288Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei73 – 731Phosphoserine1 Publication
    Modified residuei643 – 6431Phosphoserine1 Publication
    Modified residuei724 – 7241Phosphoserine2 Publications
    Modified residuei730 – 7301Phosphothreonine4 Publications
    Modified residuei753 – 7531Phosphothreonine2 Publications
    Modified residuei759 – 7591PhosphoserineBy similarity
    Modified residuei789 – 7891Phosphoserine2 Publications

    Post-translational modificationi

    In non-muscle cells, phosphorylation by CDK1 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividing smooth muscle cells with similar effects on the interaction with actin and calmodulin and on microfilaments reorganization. CDK1-mediated phosphorylation promotes Schwann cell migration during peripheral nerve regeneration By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ05682.
    PaxDbiQ05682.
    PRIDEiQ05682.

    2D gel databases

    OGPiQ05682.

    PTM databases

    PhosphoSiteiQ05682.

    Expressioni

    Tissue specificityi

    High-molecular-weight caldesmon (isoform 1) is predominantly expressed in smooth muscles, whereas low-molecular-weight caldesmon (isoforms 2, 3, 4 and 5) are widely distributed in non-muscle tissues and cells. Not expressed in skeletal muscle or heart.

    Gene expression databases

    ArrayExpressiQ05682.
    BgeeiQ05682.
    CleanExiHS_CAD.
    HS_CALD1.
    GenevestigatoriQ05682.

    Organism-specific databases

    HPAiCAB000006.
    HPA008066.
    HPA017330.

    Interactioni

    Protein-protein interaction databases

    BioGridi107251. 25 interactions.
    IntActiQ05682. 7 interactions.
    STRINGi9606.ENSP00000354826.

    Structurei

    3D structure databases

    ProteinModelPortaliQ05682.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati319 – 332141Add
    BLAST
    Repeati333 – 346142Add
    BLAST
    Repeati347 – 360143Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni26 – 207182Myosin and calmodulin-bindingBy similarityAdd
    BLAST
    Regioni319 – 375573 X 14 AA tandem repeats of E-E-E-K-R-A-A-E-E-R-Q-R-I-KAdd
    BLAST
    Regioni564 – 62158Tropomyosin-bindingSequence AnalysisAdd
    BLAST
    Regioni653 – 68634Strong actin-bindingBy similarityAdd
    BLAST
    Regioni664 – 67411Tropomyosin-bindingSequence AnalysisAdd
    BLAST
    Regioni716 – 7227Calmodulin-bindingBy similarity
    Regioni768 – 79326Weak actin-bindingBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi39 – 468Poly-Arg
    Compositional biasi81 – 866Poly-Thr
    Compositional biasi189 – 1968Poly-Glu
    Compositional biasi376 – 3794Poly-Glu
    Compositional biasi540 – 5434Poly-Arg
    Compositional biasi580 – 5834Poly-Glu
    Compositional biasi597 – 6004Poly-Glu

    Domaini

    The N-terminal part seems to be a myosin/calmodulin-binding domain, and the C-terminal a tropomyosin/actin/calmodulin-binding domain. These two domains are separated by a central helical region in the smooth-muscle form.

    Sequence similaritiesi

    Belongs to the caldesmon family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG253189.
    HOGENOMiHOG000013012.
    HOVERGENiHBG050785.
    InParanoidiQ05682.
    KOiK12327.
    OMAiTHKLKHA.
    OrthoDBiEOG7FNC7W.
    PhylomeDBiQ05682.
    TreeFamiTF331771.

    Family and domain databases

    InterProiIPR006017. Caldesmon.
    IPR006018. Caldesmon_LSP.
    [Graphical view]
    PANTHERiPTHR18949. PTHR18949. 1 hit.
    PTHR18949:SF0. PTHR18949:SF0. 1 hit.
    PfamiPF02029. Caldesmon. 2 hits.
    [Graphical view]
    PRINTSiPR01076. CALDESMON.

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q05682-1) [UniParc]FASTAAdd to Basket

    Also known as: H-CAD

    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

    MDDFERRREL RRQKREEMRL EAERIAYQRN DDDEEEAARE RRRRARQERL    50
    RQKQEEESLG QVTDQVEVNA QNSVPDEEAK TTTTNTQVEG DDEAAFLERL 100
    ARREERRQKR LQEALERQKE FDPTITDASL SLPSRRMQND TAENETTEKE 150
    EKSESRQERY EIEETETVTK SYQKNDWRDA EENKKEDKEK EEEEEEKPKR 200
    GSIGENQVEV MVEEKTTESQ EETVVMSLKN GQISSEEPKQ EEEREQGSDE 250
    ISHHEKMEEE DKERAEAERA RLEAEERERI KAEQDKKIAD ERARIEAEEK 300
    AAAQERERRE AEERERMREE EKRAAEERQR IKEEEKRAAE ERQRIKEEEK 350
    RAAEERQRIK EEEKRAAEER QRARAEEEEK AKVEEQKRNK QLEEKKHAMQ 400
    ETKIKGEKVE QKIEGKWVNE KKAQEDKLQT AVLKKQGEEK GTKVQAKREK 450
    LQEDKPTFKK EEIKDEKIKK DKEPKEEVKS FMDRKKGFTE VKSQNGEFMT 500
    HKLKHTENTF SRPGGRASVD TKEAEGAPQV EAGKRLEELR RRRGETESEE 550
    FEKLKQKQQE AALELEELKK KREERRKVLE EEEQRRKQEE ADRKLREEEE 600
    KRRLKEEIER RRAEAAEKRQ KMPEDGLSDD KKPFKCFTPK GSSLKIEERA 650
    EFLNKSVQKS SGVKSTHQAA IVSKIDSRLE QYTSAIEGTK SAKPTKPAAS 700
    DLPVPAEGVR NIKSMWEKGN VFSSPTAAGT PNKETAGLKV GVSSRINEWL 750
    TKTPDGNKSP APKPSDLRPG DVSSKRNLWE KQSVDKVTSP TKV 793
    Length:793
    Mass (Da):93,231
    Last modified:June 28, 2011 - v3
    Checksum:i7468E2C3E40BF697
    GO
    Isoform 2 (identifier: Q05682-2) [UniParc]FASTAAdd to Basket

    Also known as: WI-38 L-CAD I

    The sequence of this isoform differs from the canonical sequence as follows:
         208-436: Missing.

    Note: Contains a phosphoserine at position 202.

    Show »
    Length:564
    Mass (Da):65,707
    Checksum:i57791B75720D2902
    GO
    Isoform 3 (identifier: Q05682-3) [UniParc]FASTAAdd to Basket

    Also known as: HELA L-CAD I

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: MDDFERRRELRRQKREEMRLEAER → MLGGSGSHGRRSLAALSQ
         208-436: Missing.

    Note: Contains a phosphoserine at position 196. Contains a phosphoserine at position 12. Contains a phosphotyrosine at position 21.

    Show »
    Length:558
    Mass (Da):64,256
    Checksum:iAA511974B9C483DC
    GO
    Isoform 4 (identifier: Q05682-4) [UniParc]FASTAAdd to Basket

    Also known as: WI-38 L-CAD II, 1-CAD

    The sequence of this isoform differs from the canonical sequence as follows:
         208-462: Missing.

    Note: Contains a phosphoserine at position 202.

    Show »
    Length:538
    Mass (Da):62,663
    Checksum:i7EBF78B53217E77A
    GO
    Isoform 5 (identifier: Q05682-5) [UniParc]FASTAAdd to Basket

    Also known as: HELA L-CAD II

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: MDDFERRRELRRQKREEMRLEAER → MLGGSGSHGRRSLAALSQ
         208-462: Missing.

    Note: Contains a phosphoserine at position 196. Contains a phosphoserine at position 12. Contains a phosphotyrosine at position 21.

    Show »
    Length:532
    Mass (Da):61,213
    Checksum:i2A222B2C1AD79975
    GO
    Isoform 6 (identifier: Q05682-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         208-436: Missing.
         660-660: Missing.

    Note: No experimental confirmation available. Contains a phosphoserine at position 202.

    Show »
    Length:563
    Mass (Da):65,620
    Checksum:iFF15BFCFCF19C248
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti530 – 5301V → M in AAA35636. (PubMed:1885618)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti397 – 3971H → R.1 Publication
    Corresponds to variant rs6973420 [ dbSNP | Ensembl ].
    VAR_065254

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2424MDDFE…LEAER → MLGGSGSHGRRSLAALSQ in isoform 3 and isoform 5. 1 PublicationVSP_004154Add
    BLAST
    Alternative sequencei208 – 462255Missing in isoform 4 and isoform 5. 4 PublicationsVSP_004156Add
    BLAST
    Alternative sequencei208 – 436229Missing in isoform 2, isoform 3 and isoform 6. 2 PublicationsVSP_004155Add
    BLAST
    Alternative sequencei660 – 6601Missing in isoform 6. 1 PublicationVSP_043292

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64110 mRNA. Translation: AAA35636.1.
    M83216 mRNA. Translation: AAA58420.1.
    M83216 mRNA. Translation: AAA58419.1.
    D90452 mRNA. Translation: BAA14418.1.
    D90453 mRNA. Translation: BAA14419.1.
    AK289686 mRNA. Translation: BAF82375.1.
    AC019014 Genomic DNA. No translation available.
    AC083870 Genomic DNA. No translation available.
    BC040354 mRNA. Translation: AAH40354.1.
    CCDSiCCDS47716.1. [Q05682-3]
    CCDS47717.1. [Q05682-5]
    CCDS5834.1. [Q05682-4]
    CCDS5835.1. [Q05682-1]
    CCDS5836.2. [Q05682-6]
    PIRiJH0628.
    RefSeqiNP_004333.1. NM_004342.6. [Q05682-4]
    NP_149129.2. NM_033138.3. [Q05682-1]
    NP_149130.1. NM_033139.3. [Q05682-3]
    NP_149131.1. NM_033140.3. [Q05682-5]
    NP_149347.2. NM_033157.3. [Q05682-6]
    UniGeneiHs.490203.

    Genome annotation databases

    EnsembliENST00000361675; ENSP00000354826; ENSG00000122786. [Q05682-1]
    ENST00000361901; ENSP00000354513; ENSG00000122786. [Q05682-4]
    ENST00000393118; ENSP00000376826; ENSG00000122786. [Q05682-3]
    ENST00000417172; ENSP00000398826; ENSG00000122786. [Q05682-4]
    ENST00000422748; ENSP00000395710; ENSG00000122786. [Q05682-6]
    ENST00000424922; ENSP00000393621; ENSG00000122786. [Q05682-5]
    GeneIDi800.
    KEGGihsa:800.
    UCSCiuc003vrz.3. human. [Q05682-1]
    uc003vsb.3. human. [Q05682-4]
    uc003vsc.3. human. [Q05682-3]
    uc003vsd.3. human. [Q05682-5]
    uc010lmm.3. human. [Q05682-6]

    Polymorphism databases

    DMDMi338817891.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64110 mRNA. Translation: AAA35636.1 .
    M83216 mRNA. Translation: AAA58420.1 .
    M83216 mRNA. Translation: AAA58419.1 .
    D90452 mRNA. Translation: BAA14418.1 .
    D90453 mRNA. Translation: BAA14419.1 .
    AK289686 mRNA. Translation: BAF82375.1 .
    AC019014 Genomic DNA. No translation available.
    AC083870 Genomic DNA. No translation available.
    BC040354 mRNA. Translation: AAH40354.1 .
    CCDSi CCDS47716.1. [Q05682-3 ]
    CCDS47717.1. [Q05682-5 ]
    CCDS5834.1. [Q05682-4 ]
    CCDS5835.1. [Q05682-1 ]
    CCDS5836.2. [Q05682-6 ]
    PIRi JH0628.
    RefSeqi NP_004333.1. NM_004342.6. [Q05682-4 ]
    NP_149129.2. NM_033138.3. [Q05682-1 ]
    NP_149130.1. NM_033139.3. [Q05682-3 ]
    NP_149131.1. NM_033140.3. [Q05682-5 ]
    NP_149347.2. NM_033157.3. [Q05682-6 ]
    UniGenei Hs.490203.

    3D structure databases

    ProteinModelPortali Q05682.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107251. 25 interactions.
    IntActi Q05682. 7 interactions.
    STRINGi 9606.ENSP00000354826.

    PTM databases

    PhosphoSitei Q05682.

    Polymorphism databases

    DMDMi 338817891.

    2D gel databases

    OGPi Q05682.

    Proteomic databases

    MaxQBi Q05682.
    PaxDbi Q05682.
    PRIDEi Q05682.

    Protocols and materials databases

    DNASUi 800.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361675 ; ENSP00000354826 ; ENSG00000122786 . [Q05682-1 ]
    ENST00000361901 ; ENSP00000354513 ; ENSG00000122786 . [Q05682-4 ]
    ENST00000393118 ; ENSP00000376826 ; ENSG00000122786 . [Q05682-3 ]
    ENST00000417172 ; ENSP00000398826 ; ENSG00000122786 . [Q05682-4 ]
    ENST00000422748 ; ENSP00000395710 ; ENSG00000122786 . [Q05682-6 ]
    ENST00000424922 ; ENSP00000393621 ; ENSG00000122786 . [Q05682-5 ]
    GeneIDi 800.
    KEGGi hsa:800.
    UCSCi uc003vrz.3. human. [Q05682-1 ]
    uc003vsb.3. human. [Q05682-4 ]
    uc003vsc.3. human. [Q05682-3 ]
    uc003vsd.3. human. [Q05682-5 ]
    uc010lmm.3. human. [Q05682-6 ]

    Organism-specific databases

    CTDi 800.
    GeneCardsi GC07P134429.
    HGNCi HGNC:1441. CALD1.
    HPAi CAB000006.
    HPA008066.
    HPA017330.
    MIMi 114213. gene.
    neXtProti NX_Q05682.
    PharmGKBi PA26034.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG253189.
    HOGENOMi HOG000013012.
    HOVERGENi HBG050785.
    InParanoidi Q05682.
    KOi K12327.
    OMAi THKLKHA.
    OrthoDBi EOG7FNC7W.
    PhylomeDBi Q05682.
    TreeFami TF331771.

    Enzyme and pathway databases

    Reactomei REACT_20558. Smooth Muscle Contraction.

    Miscellaneous databases

    ChiTaRSi CALD1. human.
    GeneWikii Caldesmon.
    GenomeRNAii 800.
    NextBioi 3252.
    PROi Q05682.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05682.
    Bgeei Q05682.
    CleanExi HS_CAD.
    HS_CALD1.
    Genevestigatori Q05682.

    Family and domain databases

    InterProi IPR006017. Caldesmon.
    IPR006018. Caldesmon_LSP.
    [Graphical view ]
    PANTHERi PTHR18949. PTHR18949. 1 hit.
    PTHR18949:SF0. PTHR18949:SF0. 1 hit.
    Pfami PF02029. Caldesmon. 2 hits.
    [Graphical view ]
    PRINTSi PR01076. CALDESMON.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNA clones encoding a human fibroblast caldesmon isoform and analysis of caldesmon expression in normal and transformed cells."
      Novy R.E., Lin J.L.-C., Lin J.J.-C.
      J. Biol. Chem. 266:16917-16924(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
      Tissue: Lung fibroblast.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), VARIANT ARG-397.
      Tissue: Aorta.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
    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 6).
      Tissue: Amygdala.
    5. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 4).
      Tissue: Skin.
    7. "Identification of functioning regulatory sites and a new myosin binding site in the C-terminal 288 amino acids of caldesmon expressed from a human clone."
      Huber P.A.J., Redwood C.S., Avent N.D., Tanner M.J.A., Marston S.B.
      J. Muscle Res. Cell Motil. 14:385-391(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 497-793, FUNCTION.
      Tissue: Fetal liver.
    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 THR-730, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-730, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724; THR-730; THR-753 AND SER-789, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-724; THR-730 AND THR-753, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; TYR-21 AND SER-196 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-73; SER-643 AND SER-789, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCALD1_HUMAN
    AccessioniPrimary (citable) accession number: Q05682
    Secondary accession number(s): A8K0X1
    , Q13978, Q13979, Q14741, Q14742, Q9UD91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 142 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 7
      Human chromosome 7: 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