Q00341 (VIGLN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vigilin

Alternative name(s):
High density lipoprotein-binding protein
Short name=HDL-binding protein

Gene names

Name:	HDLBP
Synonyms:	HBP, VGL

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1268 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cholesterol metabolism Lipid metabolism Lipid transport Steroid metabolism Sterol metabolism Transport
Cellular component	Cytoplasm HDL Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cholesterol metabolic process Traceable author statement Ref.1. Source: ProtInc lipid transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA high-density lipoprotein particle Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW lipid binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5

Chain

2 – 1268

1267

Vigilin

PRO_0000050131

Regions

Domain

158 – 229

72

KH 1

Domain

230 – 302

73

KH 2

Domain

303 – 371

69

KH 3

Domain

372 – 442

71

KH 4

Domain

443 – 514

72

KH 5

Domain

515 – 588

74

KH 6

Domain

589 – 660

72

KH 7

Domain

661 – 734

74

KH 8

Domain

735 – 807

73

KH 9

Domain

808 – 880

73

KH 10

Domain

881 – 979

99

KH 11

Domain

980 – 1059

80

KH 12

Domain

1060 – 1134

75

KH 13

Domain

1135 – 1209

75

KH 14

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.5

Modified residue

31

1

Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Modified residue

295

1

Phosphothreonine Potential

Modified residue

296

1

Phosphothreonine Potential

Modified residue

437

1

Phosphotyrosine Ref.7

Modified residue

944

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1

1

M → MHLAERDRWLFVATVMMHFV SIKSGFPGLCVGVRSTM in isoform 2.

VSP_044924

Alternative sequence

291 – 359

69

Missing in isoform 2.

VSP_044925

Natural variant

61

1

S → A. Ref.1 Ref.2 Ref.4 Ref.15
Corresponds to variant rs11891776 [ dbSNP | Ensembl ].

VAR_047976

Natural variant

229

1

V → I.
Corresponds to variant rs7572799 [ dbSNP | Ensembl ].

VAR_055981

Natural variant

418

1

N → S.
Corresponds to variant rs7578199 [ dbSNP | Ensembl ].

VAR_024511

Natural variant

568

1

K → N in a breast cancer sample; somatic mutation. Ref.14

VAR_036052

Natural variant

939

1

D → V in a breast cancer sample; somatic mutation. Ref.14

VAR_036053

Natural variant

1264

1

W → L.
Corresponds to variant rs12281 [ dbSNP | Ensembl ].

VAR_029279

Secondary structure

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1268

Helix Strand Turn

Details...

Beta strand

151 – 156

6

Turn

159 – 161

3

Helix

162 – 166

5

Beta strand

168 – 170

3

Helix

172 – 179

8

Beta strand

195 – 200

6

Helix

202 – 220

19

Beta strand

365 – 370

6

Helix

376 – 380

5

Turn

381 – 384

4

Helix

386 – 393

8

Beta strand

395 – 401

7

Beta strand

403 – 405

3

Beta strand

407 – 412

6

Helix

414 – 434

21

Beta strand

436 – 442

7

Helix

446 – 450

5

Turn

452 – 454

3

Helix

457 – 464

8

Beta strand

468 – 470

3

Beta strand

476 – 487

12

Helix

488 – 499

12

Beta strand

656 – 659

4

Helix

662 – 669

8

Beta strand

671 – 673

3

Helix

674 – 683

10

Beta strand

687 – 689

3

Turn

693 – 696

4

Beta strand

699 – 704

6

Helix

706 – 723

18

Beta strand

973 – 978

6

Helix

981 – 988

8

Beta strand

990 – 992

3

Helix

993 – 1001

9

Beta strand

1005 – 1007

3

Turn

1011 – 1013

3

Beta strand

1017 – 1022

6

Helix

1024 – 1050

27

Beta strand

1054 – 1058

5

Turn

1061 – 1063

3

Helix

1064 – 1067

4

Beta strand

1070 – 1072

3

Helix

1074 – 1082

9

Beta strand

1085 – 1087

3

Turn

1091 – 1093

3

Beta strand

1098 – 1105

8

Helix

1107 – 1126

20

Beta strand

1130 – 1133

4

Turn

1136 – 1138

3

Helix

1139 – 1143

5

Beta strand

1145 – 1147

3

Helix

1149 – 1157

9

Beta strand

1160 – 1162

3

Beta strand

1173 – 1178

6

Helix

1180 – 1198

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 530C61A3CA9239CD	FASTA	1,268	141,456
	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
	Isoform 2 [UniParc]. Checksum: 9A49873E7937B9D4	FASTA	1,235	137,987
	10 20 30 40 50 60 MHLAERDRWL FVATVMMHFV SIKSGFPGLC VGVRSTMSSV AVLTQESFAE HRSGLVPQQI 70 80 90 100 110 120 KVATLNSEEE SDPPTYKDAF PPLPEKAACL ESAQEPSGAW GNKIRPIKAS VITQVFHVPL 130 140 150 160 170 180 EERKYKDMNQ FGEGEQAKIC LEIMQRTGAH LELSLAKDQG LSIMVSGKLD AVMKARKDIV 190 200 210 220 230 240 ARLQTQASAT VAIPKEHHRF VIGKNGEKLQ DLELKTATKI QIPRPDDPSN QIKITGTKEG 250 260 270 280 290 300 IEKARHEVLL ISAEQDKRAV ERLEVEKAFH PFIAGPYNRL VGEIMQETGT RINIPPPSVN 310 320 330 340 350 360 RTEIVFTGEK EQLAQAVARI KKIYEEKANS FTVSSVAAPS WLHRFIIGKK GQNLAKITQQ 370 380 390 400 410 420 MPKVHIEFTE GEDKITLEGP TEDVNVAQEQ IEGMVKDLIN RMDYVEINID HKFHRHLIGK 430 440 450 460 470 480 SGANINRIKD QYKVSVRIPP DSEKSNLIRI EGDPQGVQQA KRELLELASR MENERTKDLI 490 500 510 520 530 540 IEQRFHRTII GQKGERIREI RDKFPEVIIN FPDPAQKSDI VQLRGPKNEV EKCTKYMQKM 550 560 570 580 590 600 VADLVENSYS ISVPIFKQFH KNIIGKGGAN IKKIREESNT KIDLPAENSN SETIIITGKR 610 620 630 640 650 660 ANCEAARSRI LSIQKDLANI AEVEVSIPAK LHNSLIGTKG RLIRSIMEEC GGVHIHFPVE 670 680 690 700 710 720 GSGSDTVVIR GPSSDVEKAK KQLLHLAEEK QTKSFTVDIR AKPEYHKFLI GKGGGKIRKV 730 740 750 760 770 780 RDSTGARVIF PAAEDKDQDL ITIIGKEDAV REAQKELEAL IQNLDNVVED SMLVDPKHHR 790 800 810 820 830 840 HFVIRRGQVL REIAEEYGGV MVSFPRSGTQ SDKVTLKGAK DCVEAAKKRI QEIIEDLEAQ 850 860 870 880 890 900 VTLECAIPQK FHRSVMGPKG SRIQQITRDF SVQIKFPDRE ENAVHSTEPV VQENGDEAGE 910 920 930 940 950 960 GREAKDCDPG SPRRCDIIII SGRKEKCEAA KEALEALVPV TIEVEVPFDL HRYVIGQKGS 970 980 990 1000 1010 1020 GIRKMMDEFE VNIHVPAPEL QSDIIAITGL AANLDRAKAG LLERVKELQA EQEDRALRSF 1030 1040 1050 1060 1070 1080 KLSVTVDPKY HPKIIGRKGA VITQIRLEHD VNIQFPDKDD GNQPQDQITI TGYEKNTEAA 1090 1100 1110 1120 1130 1140 RDAILRIVGE LEQMVSEDVP LDHRVHARII GARGKAIRKI MDEFKVDIRF PQSGAPDPNC 1150 1160 1170 1180 1190 1200 VTVTGLPENV EEAIDHILNL EEEYLADVVD SEALQVYMKP PAHEEAKAPS RGFVVRDAPW 1210 1220 1230 TASSSEKAPD MSSSEEFPSF GAQVAPKTLP WGPKR

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY.
[10]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, MASS SPECTROMETRY.
[13]	"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.
[14]	"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. , 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.
[15]	"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, MASS SPECTROMETRY.
+	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.

IPI

IPI00022228.
IPI00894287.

PIR

A44125.

RefSeq

NP_001230829.1. NM_001243900.1.
NP_005327.1. NM_005336.4.
NP_976221.1. NM_203346.3.

UniGene

Hs.471851.
Hs.732361.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q00341.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q00341. 7 interactions.

MINT

MINT-1189333.

STRING

9606.ENSP00000312042.

PTM databases

PhosphoSite

Q00341.

Polymorphism databases

DMDM

218511884.

Proteomic databases

PaxDb

Q00341.

PeptideAtlas

Q00341.

PRIDE

Q00341.

Protocols and materials databases

DNASU

3069.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310931; ENSP00000312042; ENSG00000115677.
ENST00000391975; ENSP00000375836; ENSG00000115677.
ENST00000391976; ENSP00000375837; ENSG00000115677.
ENST00000427183; ENSP00000399139; ENSG00000115677.

GeneID

3069.

KEGG

hsa:3069.

UCSC

uc002waz.3. human.

Organism-specific databases

CTD

3069.

GeneCards

GC02M242188.

HGNC

HGNC:4857. HDLBP.

HPA

CAB026457.
HPA004189.

MIM

142695. gene.

neXtProt

NX_Q00341.

PharmGKB

PA29235.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG313207.

HOGENOM

HOG000007687.

HOVERGEN

HBG054107.

InParanoid

Q00341.

OMA

YEKNTEA.

OrthoDB

EOG4M65GT.

PhylomeDB

Q00341.

Gene expression databases

ArrayExpress

Q00341.

Bgee

Q00341.

CleanEx

HS_HDLBP.

Genevestigator

Q00341.

GermOnline

ENSG00000115677. Homo sapiens.

Family and domain databases

InterPro

IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
[Graphical view]

Pfam

PF00013. KH_1. 14 hits.
[Graphical view]

SMART

SM00322. KH. 14 hits.
[Graphical view]

PROSITE

PS50084. KH_TYPE_1. 14 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

HDLBP. human.

EvolutionaryTrace

Q00341.

GenomeRNAi

3069.

NextBio

12141.

SOURCE

Search...

Entry information

Entry name

VIGLN_HUMAN

Accession

Primary (citable) accession number: Q00341
Secondary accession number(s): B4DTQ2 , E7EM71, Q53QU2, Q9UCY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.