Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q00341

- VIGLN_HUMAN

UniProt

Q00341 - VIGLN_HUMAN

Protein

Vigilin

Gene

HDLBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Appears to play a role in cell sterol metabolism. It may function to protect cells from over-accumulation of cholesterol.

    GO - Molecular functioni

    1. lipid binding Source: ProtInc
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cholesterol metabolic process Source: ProtInc
    2. lipid transport Source: UniProtKB-KW

    Keywords - Biological processi

    Cholesterol metabolism, Lipid metabolism, Lipid transport, Steroid metabolism, Sterol metabolism, Transport

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vigilin
    Alternative name(s):
    High density lipoprotein-binding protein
    Short name:
    HDL-binding protein
    Gene namesi
    Name:HDLBP
    Synonyms:HBP, VGL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:4857. HDLBP.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. high-density lipoprotein particle Source: UniProtKB-KW
    3. nucleus Source: UniProtKB-SubCell
    4. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasm, HDL, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29235.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 12681267VigilinPRO_0000050131Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei31 – 311Phosphoserine5 Publications
    Modified residuei295 – 2951PhosphothreonineSequence Analysis
    Modified residuei296 – 2961PhosphothreonineSequence Analysis
    Modified residuei437 – 4371Phosphotyrosine1 Publication
    Modified residuei991 – 9911N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ00341.
    PaxDbiQ00341.
    PeptideAtlasiQ00341.
    PRIDEiQ00341.

    PTM databases

    PhosphoSiteiQ00341.

    Expressioni

    Gene expression databases

    ArrayExpressiQ00341.
    BgeeiQ00341.
    CleanExiHS_HDLBP.
    GenevestigatoriQ00341.

    Organism-specific databases

    HPAiCAB026457.
    HPA004189.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTCFP497114EBI-1049478,EBI-932887

    Protein-protein interaction databases

    BioGridi109319. 50 interactions.
    IntActiQ00341. 14 interactions.
    MINTiMINT-1189333.
    STRINGi9606.ENSP00000312042.

    Structurei

    Secondary structure

    1
    1268
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi151 – 1566
    Turni159 – 1613
    Helixi162 – 1665
    Beta strandi168 – 1703
    Helixi172 – 1798
    Beta strandi195 – 2006
    Helixi202 – 22019
    Beta strandi365 – 3706
    Helixi376 – 3805
    Turni381 – 3844
    Helixi386 – 3938
    Beta strandi395 – 4017
    Beta strandi403 – 4053
    Beta strandi407 – 4126
    Helixi414 – 43421
    Beta strandi436 – 4427
    Helixi446 – 4505
    Turni452 – 4543
    Helixi457 – 4648
    Beta strandi468 – 4703
    Beta strandi476 – 48712
    Helixi488 – 49912
    Beta strandi656 – 6594
    Helixi662 – 6698
    Beta strandi671 – 6733
    Helixi674 – 68310
    Beta strandi687 – 6893
    Turni693 – 6964
    Beta strandi699 – 7046
    Helixi706 – 72318
    Beta strandi973 – 9786
    Helixi981 – 9888
    Beta strandi990 – 9923
    Helixi993 – 10019
    Beta strandi1005 – 10073
    Turni1011 – 10133
    Beta strandi1017 – 10226
    Helixi1024 – 105027
    Beta strandi1054 – 10585
    Turni1061 – 10633
    Helixi1064 – 10674
    Beta strandi1070 – 10723
    Helixi1074 – 10829
    Beta strandi1085 – 10873
    Turni1091 – 10933
    Beta strandi1098 – 11058
    Helixi1107 – 112620
    Beta strandi1130 – 11334
    Turni1136 – 11383
    Helixi1139 – 11435
    Beta strandi1145 – 11473
    Helixi1149 – 11579
    Beta strandi1160 – 11623
    Beta strandi1173 – 11786
    Helixi1180 – 119819

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VIGNMR-A432-502[»]
    1VIHNMR-A432-502[»]
    2CTENMR-A142-222[»]
    2CTFNMR-A346-434[»]
    2CTJNMR-A645-726[»]
    2CTKNMR-A964-1054[»]
    2CTLNMR-A1044-1127[»]
    2CTMNMR-A1119-1200[»]
    ProteinModelPortaliQ00341.
    SMRiQ00341. Positions 142-223, 345-502, 646-727, 795-873, 962-1200.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00341.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini158 – 22972KH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini230 – 30273KH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini303 – 37169KH 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini372 – 44271KH 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini443 – 51472KH 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini515 – 58874KH 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini589 – 66072KH 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini661 – 73474KH 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini735 – 80773KH 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini808 – 88073KH 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini881 – 97999KH 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini980 – 105980KH 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1060 – 113475KH 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1135 – 120975KH 14PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 14 KH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG313207.
    HOGENOMiHOG000007687.
    HOVERGENiHBG054107.
    InParanoidiQ00341.
    OMAiQHHKFLI.
    OrthoDBiEOG7KH9HW.
    PhylomeDBiQ00341.
    TreeFamiTF323767.

    Family and domain databases

    Gene3Di3.30.1370.10. 15 hits.
    InterProiIPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view]
    PfamiPF00013. KH_1. 14 hits.
    [Graphical view]
    SMARTiSM00322. KH. 14 hits.
    [Graphical view]
    SUPFAMiSSF54791. SSF54791. 13 hits.
    PROSITEiPS50084. KH_TYPE_1. 14 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q00341-1) [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

    MSSVAVLTQE SFAEHRSGLV PQQIKVATLN SEEESDPPTY KDAFPPLPEK     50
    AACLESAQEP SGAWGNKIRP IKASVITQVF HVPLEERKYK DMNQFGEGEQ 100
    AKICLEIMQR TGAHLELSLA KDQGLSIMVS GKLDAVMKAR KDIVARLQTQ 150
    ASATVAIPKE HHRFVIGKNG EKLQDLELKT ATKIQIPRPD DPSNQIKITG 200
    TKEGIEKARH EVLLISAEQD KRAVERLEVE KAFHPFIAGP YNRLVGEIMQ 250
    ETGTRINIPP PSVNRTEIVF TGEKEQLAQA VARIKKIYEE KKKKTTTIAV 300
    EVKKSQHKYV IGPKGNSLQE ILERTGVSVE IPPSDSISET VILRGEPEKL 350
    GQALTEVYAK ANSFTVSSVA APSWLHRFII GKKGQNLAKI TQQMPKVHIE 400
    FTEGEDKITL EGPTEDVNVA QEQIEGMVKD LINRMDYVEI NIDHKFHRHL 450
    IGKSGANINR IKDQYKVSVR IPPDSEKSNL IRIEGDPQGV QQAKRELLEL 500
    ASRMENERTK DLIIEQRFHR TIIGQKGERI REIRDKFPEV IINFPDPAQK 550
    SDIVQLRGPK NEVEKCTKYM QKMVADLVEN SYSISVPIFK QFHKNIIGKG 600
    GANIKKIREE SNTKIDLPAE NSNSETIIIT GKRANCEAAR SRILSIQKDL 650
    ANIAEVEVSI PAKLHNSLIG TKGRLIRSIM EECGGVHIHF PVEGSGSDTV 700
    VIRGPSSDVE KAKKQLLHLA EEKQTKSFTV DIRAKPEYHK FLIGKGGGKI 750
    RKVRDSTGAR VIFPAAEDKD QDLITIIGKE DAVREAQKEL EALIQNLDNV 800
    VEDSMLVDPK HHRHFVIRRG QVLREIAEEY GGVMVSFPRS GTQSDKVTLK 850
    GAKDCVEAAK KRIQEIIEDL EAQVTLECAI PQKFHRSVMG PKGSRIQQIT 900
    RDFSVQIKFP DREENAVHST EPVVQENGDE AGEGREAKDC DPGSPRRCDI 950
    IIISGRKEKC EAAKEALEAL VPVTIEVEVP FDLHRYVIGQ KGSGIRKMMD 1000
    EFEVNIHVPA PELQSDIIAI TGLAANLDRA KAGLLERVKE LQAEQEDRAL 1050
    RSFKLSVTVD PKYHPKIIGR KGAVITQIRL EHDVNIQFPD KDDGNQPQDQ 1100
    ITITGYEKNT EAARDAILRI VGELEQMVSE DVPLDHRVHA RIIGARGKAI 1150
    RKIMDEFKVD IRFPQSGAPD PNCVTVTGLP ENVEEAIDHI LNLEEEYLAD 1200
    VVDSEALQVY MKPPAHEEAK APSRGFVVRD APWTASSSEK APDMSSSEEF 1250
    PSFGAQVAPK TLPWGPKR 1268
    Length:1,268
    Mass (Da):141,456
    Last modified:December 16, 2008 - v2
    Checksum:i530C61A3CA9239CD
    GO
    Isoform 2 (identifier: Q00341-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MHLAERDRWLFVATVMMHFVSIKSGFPGLCVGVRSTM
         291-359: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,235
    Mass (Da):137,987
    Checksum:i9A49873E7937B9D4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti61 – 611S → A.4 Publications
    Corresponds to variant rs11891776 [ dbSNP | Ensembl ].
    VAR_047976
    Natural varianti229 – 2291V → I.
    Corresponds to variant rs7572799 [ dbSNP | Ensembl ].
    VAR_055981
    Natural varianti418 – 4181N → S.
    Corresponds to variant rs7578199 [ dbSNP | Ensembl ].
    VAR_024511
    Natural varianti568 – 5681K → N in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036052
    Natural varianti939 – 9391D → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036053
    Natural varianti1264 – 12641W → L.
    Corresponds to variant rs12281 [ dbSNP | Ensembl ].
    VAR_029279

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MHLAERDRWLFVATVMMHFV SIKSGFPGLCVGVRSTM in isoform 2. 1 PublicationVSP_044924
    Alternative sequencei291 – 35969Missing in isoform 2. 1 PublicationVSP_044925Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64098 mRNA. Translation: AAA35962.1.
    AK300312 mRNA. Translation: BAG62064.1.
    AC104841 Genomic DNA. Translation: AAY14717.1.
    BC001179 mRNA. Translation: AAH01179.1.
    CCDSiCCDS2547.1. [Q00341-1]
    CCDS58760.1. [Q00341-2]
    PIRiA44125.
    RefSeqiNP_001230829.1. NM_001243900.1.
    NP_005327.1. NM_005336.4.
    NP_976221.1. NM_203346.3.
    XP_005247057.2. XM_005247000.2.
    XP_005247058.2. XM_005247001.2.
    XP_005247059.2. XM_005247002.2.
    XP_005247060.2. XM_005247003.2.
    XP_006712538.1. XM_006712475.1.
    UniGeneiHs.471851.
    Hs.732361.

    Genome annotation databases

    EnsembliENST00000310931; ENSP00000312042; ENSG00000115677. [Q00341-1]
    ENST00000391975; ENSP00000375836; ENSG00000115677. [Q00341-1]
    ENST00000391976; ENSP00000375837; ENSG00000115677. [Q00341-1]
    ENST00000427183; ENSP00000399139; ENSG00000115677. [Q00341-2]
    GeneIDi3069.
    KEGGihsa:3069.
    UCSCiuc002waz.3. human. [Q00341-1]

    Polymorphism databases

    DMDMi218511884.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64098 mRNA. Translation: AAA35962.1 .
    AK300312 mRNA. Translation: BAG62064.1 .
    AC104841 Genomic DNA. Translation: AAY14717.1 .
    BC001179 mRNA. Translation: AAH01179.1 .
    CCDSi CCDS2547.1. [Q00341-1 ]
    CCDS58760.1. [Q00341-2 ]
    PIRi A44125.
    RefSeqi NP_001230829.1. NM_001243900.1.
    NP_005327.1. NM_005336.4.
    NP_976221.1. NM_203346.3.
    XP_005247057.2. XM_005247000.2.
    XP_005247058.2. XM_005247001.2.
    XP_005247059.2. XM_005247002.2.
    XP_005247060.2. XM_005247003.2.
    XP_006712538.1. XM_006712475.1.
    UniGenei Hs.471851.
    Hs.732361.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VIG NMR - A 432-502 [» ]
    1VIH NMR - A 432-502 [» ]
    2CTE NMR - A 142-222 [» ]
    2CTF NMR - A 346-434 [» ]
    2CTJ NMR - A 645-726 [» ]
    2CTK NMR - A 964-1054 [» ]
    2CTL NMR - A 1044-1127 [» ]
    2CTM NMR - A 1119-1200 [» ]
    ProteinModelPortali Q00341.
    SMRi Q00341. Positions 142-223, 345-502, 646-727, 795-873, 962-1200.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109319. 50 interactions.
    IntActi Q00341. 14 interactions.
    MINTi MINT-1189333.
    STRINGi 9606.ENSP00000312042.

    PTM databases

    PhosphoSitei Q00341.

    Polymorphism databases

    DMDMi 218511884.

    Proteomic databases

    MaxQBi Q00341.
    PaxDbi Q00341.
    PeptideAtlasi Q00341.
    PRIDEi Q00341.

    Protocols and materials databases

    DNASUi 3069.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310931 ; ENSP00000312042 ; ENSG00000115677 . [Q00341-1 ]
    ENST00000391975 ; ENSP00000375836 ; ENSG00000115677 . [Q00341-1 ]
    ENST00000391976 ; ENSP00000375837 ; ENSG00000115677 . [Q00341-1 ]
    ENST00000427183 ; ENSP00000399139 ; ENSG00000115677 . [Q00341-2 ]
    GeneIDi 3069.
    KEGGi hsa:3069.
    UCSCi uc002waz.3. human. [Q00341-1 ]

    Organism-specific databases

    CTDi 3069.
    GeneCardsi GC02M242166.
    HGNCi HGNC:4857. HDLBP.
    HPAi CAB026457.
    HPA004189.
    MIMi 142695. gene.
    neXtProti NX_Q00341.
    PharmGKBi PA29235.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313207.
    HOGENOMi HOG000007687.
    HOVERGENi HBG054107.
    InParanoidi Q00341.
    OMAi QHHKFLI.
    OrthoDBi EOG7KH9HW.
    PhylomeDBi Q00341.
    TreeFami TF323767.

    Miscellaneous databases

    ChiTaRSi HDLBP. human.
    EvolutionaryTracei Q00341.
    GeneWikii HDLBP.
    GenomeRNAii 3069.
    NextBioi 12141.
    PROi Q00341.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00341.
    Bgeei Q00341.
    CleanExi HS_HDLBP.
    Genevestigatori Q00341.

    Family and domain databases

    Gene3Di 3.30.1370.10. 15 hits.
    InterProi IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view ]
    Pfami PF00013. KH_1. 14 hits.
    [Graphical view ]
    SMARTi SM00322. KH. 14 hits.
    [Graphical view ]
    SUPFAMi SSF54791. SSF54791. 13 hits.
    PROSITEi PS50084. KH_TYPE_1. 14 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of a cellular high density lipoprotein-binding protein that is up-regulated by cholesterol loading of cells."
      McKnight G.L., Reasoner J., Gilbert T., Sundquist K.O., Hokland B., McKernan P.A., Champagne J., Johnson C.J., Bailey M.C., Holly R., O'Hara P.J., Oram J.F.
      J. Biol. Chem. 267:12131-12141(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-61.
    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] (ISOFORM 2), VARIANT ALA-61.
      Tissue: Placenta.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ALA-61.
      Tissue: Muscle.
    5. Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W., Glen H., Frame M.C.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-16; 73-87; 147-159; 208-222; 232-283; 315-324; 350-377; 483-494; 496-503; 535-557; 649-663; 902-908 AND 1120-1137, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Mammary carcinoma and Osteosarcoma.
    6. "Vigilin contains a functional nuclear localisation sequence and is present in both the cytoplasm and the nucleus."
      Kugler S., Grunweller A., Probst C., Klinger M., Mueller P.K., Kruse C.
      FEBS Lett. 382:330-334(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-437, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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-31, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Solution structure of the 1st, 4th, 8th, 12th, 13th and 14th KH type-I domains from human vigilin."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 142-222; 345-434; 645-727 AND 964-1200.
    16. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-568 AND VAL-939.
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiVIGLN_HUMAN
    AccessioniPrimary (citable) accession number: Q00341
    Secondary accession number(s): B4DTQ2
    , E7EM71, Q53QU2, Q9UCY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 145 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 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3