Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q00341

- VIGLN_HUMAN

UniProt

Q00341 - VIGLN_HUMAN

(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)

Protein

Vigilin

Gene

HDLBP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

GO - Biological processi

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

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-KW
  4. plasma membrane Source: ProtInc
Complete GO annotation...

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

BgeeiQ00341.
CleanExiHS_HDLBP.
ExpressionAtlasiQ00341. baseline and differential.
GenevestigatoriQ00341.

Organism-specific databases

HPAiCAB026457.
HPA004189.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi109319. 58 interactions.
IntActiQ00341. 15 interactions.
MINTiMINT-1189333.
STRINGi9606.ENSP00000312042.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00720000108747.
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

        10         20         30         40         50
MSSVAVLTQE SFAEHRSGLV PQQIKVATLN SEEESDPPTY KDAFPPLPEK
60 70 80 90 100
AACLESAQEP SGAWGNKIRP IKASVITQVF HVPLEERKYK DMNQFGEGEQ
110 120 130 140 150
AKICLEIMQR TGAHLELSLA KDQGLSIMVS GKLDAVMKAR KDIVARLQTQ
160 170 180 190 200
ASATVAIPKE HHRFVIGKNG EKLQDLELKT ATKIQIPRPD DPSNQIKITG
210 220 230 240 250
TKEGIEKARH EVLLISAEQD KRAVERLEVE KAFHPFIAGP YNRLVGEIMQ
260 270 280 290 300
ETGTRINIPP PSVNRTEIVF TGEKEQLAQA VARIKKIYEE KKKKTTTIAV
310 320 330 340 350
EVKKSQHKYV IGPKGNSLQE ILERTGVSVE IPPSDSISET VILRGEPEKL
360 370 380 390 400
GQALTEVYAK ANSFTVSSVA APSWLHRFII GKKGQNLAKI TQQMPKVHIE
410 420 430 440 450
FTEGEDKITL EGPTEDVNVA QEQIEGMVKD LINRMDYVEI NIDHKFHRHL
460 470 480 490 500
IGKSGANINR IKDQYKVSVR IPPDSEKSNL IRIEGDPQGV QQAKRELLEL
510 520 530 540 550
ASRMENERTK DLIIEQRFHR TIIGQKGERI REIRDKFPEV IINFPDPAQK
560 570 580 590 600
SDIVQLRGPK NEVEKCTKYM QKMVADLVEN SYSISVPIFK QFHKNIIGKG
610 620 630 640 650
GANIKKIREE SNTKIDLPAE NSNSETIIIT GKRANCEAAR SRILSIQKDL
660 670 680 690 700
ANIAEVEVSI PAKLHNSLIG TKGRLIRSIM EECGGVHIHF PVEGSGSDTV
710 720 730 740 750
VIRGPSSDVE KAKKQLLHLA EEKQTKSFTV DIRAKPEYHK FLIGKGGGKI
760 770 780 790 800
RKVRDSTGAR VIFPAAEDKD QDLITIIGKE DAVREAQKEL EALIQNLDNV
810 820 830 840 850
VEDSMLVDPK HHRHFVIRRG QVLREIAEEY GGVMVSFPRS GTQSDKVTLK
860 870 880 890 900
GAKDCVEAAK KRIQEIIEDL EAQVTLECAI PQKFHRSVMG PKGSRIQQIT
910 920 930 940 950
RDFSVQIKFP DREENAVHST EPVVQENGDE AGEGREAKDC DPGSPRRCDI
960 970 980 990 1000
IIISGRKEKC EAAKEALEAL VPVTIEVEVP FDLHRYVIGQ KGSGIRKMMD
1010 1020 1030 1040 1050
EFEVNIHVPA PELQSDIIAI TGLAANLDRA KAGLLERVKE LQAEQEDRAL
1060 1070 1080 1090 1100
RSFKLSVTVD PKYHPKIIGR KGAVITQIRL EHDVNIQFPD KDDGNQPQDQ
1110 1120 1130 1140 1150
ITITGYEKNT EAARDAILRI VGELEQMVSE DVPLDHRVHA RIIGARGKAI
1160 1170 1180 1190 1200
RKIMDEFKVD IRFPQSGAPD PNCVTVTGLP ENVEEAIDHI LNLEEEYLAD
1210 1220 1230 1240 1250
VVDSEALQVY MKPPAHEEAK APSRGFVVRD APWTASSSEK APDMSSSEEF
1260
PSFGAQVAPK TLPWGPKR
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:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000427183; ENSP00000399139; ENSG00000115677.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 58 interactions.
IntActi Q00341. 15 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 ENST00000427183 ; ENSP00000399139 ; ENSG00000115677 .
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.
GeneTreei ENSGT00720000108747.
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

Bgeei Q00341.
CleanExi HS_HDLBP.
ExpressionAtlasi Q00341. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 147 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