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Q00341 (VIGLN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vigilin
Alternative name(s):
High density lipoprotein-binding protein
Short name=HDL-binding protein
Gene names
Name:HDLBP
Synonyms:HBP, VGL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1268 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Cytoplasm. Nucleus Ref.6.

Sequence similarities

Contains 14 KH domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q00341-1)

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.
Isoform 2 (identifier: Q00341-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MHLAERDRWLFVATVMMHFVSIKSGFPGLCVGVRSTM
     291-359: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 12681267Vigilin
PRO_0000050131

Regions

Domain158 – 22972KH 1
Domain230 – 30273KH 2
Domain303 – 37169KH 3
Domain372 – 44271KH 4
Domain443 – 51472KH 5
Domain515 – 58874KH 6
Domain589 – 66072KH 7
Domain661 – 73474KH 8
Domain735 – 80773KH 9
Domain808 – 88073KH 10
Domain881 – 97999KH 11
Domain980 – 105980KH 12
Domain1060 – 113475KH 13
Domain1135 – 120975KH 14

Amino acid modifications

Modified residue21N-acetylserine Ref.5 Ref.9 Ref.14
Modified residue311Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12 Ref.13
Modified residue2951Phosphothreonine Potential
Modified residue2961Phosphothreonine Potential
Modified residue4371Phosphotyrosine Ref.7
Modified residue9911N6-acetyllysine By similarity

Natural variations

Alternative sequence11M → MHLAERDRWLFVATVMMHFV SIKSGFPGLCVGVRSTM in isoform 2.
VSP_044924
Alternative sequence291 – 35969Missing in isoform 2.
VSP_044925
Natural variant611S → A. Ref.1 Ref.2 Ref.4 Ref.17
Corresponds to variant rs11891776 [ dbSNP | Ensembl ].
VAR_047976
Natural variant2291V → I.
Corresponds to variant rs7572799 [ dbSNP | Ensembl ].
VAR_055981
Natural variant4181N → S.
Corresponds to variant rs7578199 [ dbSNP | Ensembl ].
VAR_024511
Natural variant5681K → N in a breast cancer sample; somatic mutation. Ref.16
VAR_036052
Natural variant9391D → V in a breast cancer sample; somatic mutation. Ref.16
VAR_036053
Natural variant12641W → L.
Corresponds to variant rs12281 [ dbSNP | Ensembl ].
VAR_029279

Secondary structure

........................................................................................................ 1268
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 530C61A3CA9239CD

FASTA1,268141,456
        10         20         30         40         50         60 
MSSVAVLTQE SFAEHRSGLV PQQIKVATLN SEEESDPPTY KDAFPPLPEK AACLESAQEP 

        70         80         90        100        110        120 
SGAWGNKIRP IKASVITQVF HVPLEERKYK DMNQFGEGEQ AKICLEIMQR TGAHLELSLA 

       130        140        150        160        170        180 
KDQGLSIMVS GKLDAVMKAR KDIVARLQTQ ASATVAIPKE HHRFVIGKNG EKLQDLELKT 

       190        200        210        220        230        240 
ATKIQIPRPD DPSNQIKITG TKEGIEKARH EVLLISAEQD KRAVERLEVE KAFHPFIAGP 

       250        260        270        280        290        300 
YNRLVGEIMQ ETGTRINIPP PSVNRTEIVF TGEKEQLAQA VARIKKIYEE KKKKTTTIAV 

       310        320        330        340        350        360 
EVKKSQHKYV IGPKGNSLQE ILERTGVSVE IPPSDSISET VILRGEPEKL GQALTEVYAK 

       370        380        390        400        410        420 
ANSFTVSSVA APSWLHRFII GKKGQNLAKI TQQMPKVHIE FTEGEDKITL EGPTEDVNVA 

       430        440        450        460        470        480 
QEQIEGMVKD LINRMDYVEI NIDHKFHRHL IGKSGANINR IKDQYKVSVR IPPDSEKSNL 

       490        500        510        520        530        540 
IRIEGDPQGV QQAKRELLEL ASRMENERTK DLIIEQRFHR TIIGQKGERI REIRDKFPEV 

       550        560        570        580        590        600 
IINFPDPAQK SDIVQLRGPK NEVEKCTKYM QKMVADLVEN SYSISVPIFK QFHKNIIGKG 

       610        620        630        640        650        660 
GANIKKIREE SNTKIDLPAE NSNSETIIIT GKRANCEAAR SRILSIQKDL ANIAEVEVSI 

       670        680        690        700        710        720 
PAKLHNSLIG TKGRLIRSIM EECGGVHIHF PVEGSGSDTV VIRGPSSDVE KAKKQLLHLA 

       730        740        750        760        770        780 
EEKQTKSFTV DIRAKPEYHK FLIGKGGGKI RKVRDSTGAR VIFPAAEDKD QDLITIIGKE 

       790        800        810        820        830        840 
DAVREAQKEL EALIQNLDNV VEDSMLVDPK HHRHFVIRRG QVLREIAEEY GGVMVSFPRS 

       850        860        870        880        890        900 
GTQSDKVTLK GAKDCVEAAK KRIQEIIEDL EAQVTLECAI PQKFHRSVMG PKGSRIQQIT 

       910        920        930        940        950        960 
RDFSVQIKFP DREENAVHST EPVVQENGDE AGEGREAKDC DPGSPRRCDI IIISGRKEKC 

       970        980        990       1000       1010       1020 
EAAKEALEAL VPVTIEVEVP FDLHRYVIGQ KGSGIRKMMD EFEVNIHVPA PELQSDIIAI 

      1030       1040       1050       1060       1070       1080 
TGLAANLDRA KAGLLERVKE LQAEQEDRAL RSFKLSVTVD PKYHPKIIGR KGAVITQIRL 

      1090       1100       1110       1120       1130       1140 
EHDVNIQFPD KDDGNQPQDQ ITITGYEKNT EAARDAILRI VGELEQMVSE DVPLDHRVHA 

      1150       1160       1170       1180       1190       1200 
RIIGARGKAI RKIMDEFKVD IRFPQSGAPD PNCVTVTGLP ENVEEAIDHI LNLEEEYLAD 

      1210       1220       1230       1240       1250       1260 
VVDSEALQVY MKPPAHEEAK APSRGFVVRD APWTASSSEK APDMSSSEEF PSFGAQVAPK 


TLPWGPKR 

« Hide

Isoform 2 [UniParc].

Checksum: 9A49873E7937B9D4
Show »

FASTA1,235137,987

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-568 AND VAL-939.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64098 mRNA. Translation: AAA35962.1.
AK300312 mRNA. Translation: BAG62064.1.
AC104841 Genomic DNA. Translation: AAY14717.1.
BC001179 mRNA. Translation: AAH01179.1.
PIRA44125.
RefSeqNP_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.
UniGeneHs.471851.
Hs.732361.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ00341.
SMRQ00341. Positions 142-292, 345-795, 803-866, 874-911, 962-1200.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109319. 47 interactions.
IntActQ00341. 13 interactions.
MINTMINT-1189333.
STRING9606.ENSP00000312042.

PTM databases

PhosphoSiteQ00341.

Polymorphism databases

DMDM218511884.

Proteomic databases

PaxDbQ00341.
PeptideAtlasQ00341.
PRIDEQ00341.

Protocols and materials databases

DNASU3069.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310931; ENSP00000312042; ENSG00000115677. [Q00341-1]
ENST00000391975; ENSP00000375836; ENSG00000115677. [Q00341-1]
ENST00000391976; ENSP00000375837; ENSG00000115677. [Q00341-1]
ENST00000427183; ENSP00000399139; ENSG00000115677. [Q00341-2]
GeneID3069.
KEGGhsa:3069.
UCSCuc002waz.3. human. [Q00341-1]

Organism-specific databases

CTD3069.
GeneCardsGC02M242166.
HGNCHGNC:4857. HDLBP.
HPACAB026457.
HPA004189.
MIM142695. gene.
neXtProtNX_Q00341.
PharmGKBPA29235.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313207.
HOGENOMHOG000007687.
HOVERGENHBG054107.
InParanoidQ00341.
OMAQHHKFLI.
OrthoDBEOG7KH9HW.
PhylomeDBQ00341.
TreeFamTF323767.

Gene expression databases

ArrayExpressQ00341.
BgeeQ00341.
CleanExHS_HDLBP.
GenevestigatorQ00341.

Family and domain databases

Gene3D3.30.1370.10. 15 hits.
InterProIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]
PfamPF00013. KH_1. 14 hits.
[Graphical view]
SMARTSM00322. KH. 14 hits.
[Graphical view]
SUPFAMSSF54791. SSF54791. 13 hits.
PROSITEPS50084. KH_TYPE_1. 14 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHDLBP. human.
EvolutionaryTraceQ00341.
GeneWikiHDLBP.
GenomeRNAi3069.
NextBio12141.
PROQ00341.
SOURCESearch...

Entry information

Entry nameVIGLN_HUMAN
AccessionPrimary (citable) accession number: Q00341
Secondary accession number(s): B4DTQ2 expand/collapse secondary AC list , E7EM71, Q53QU2, Q9UCY3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 16, 2008
Last modified: April 16, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM