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Q9HBG4

- VPP4_HUMAN

UniProt

Q9HBG4 - VPP4_HUMAN

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Protein

V-type proton ATPase 116 kDa subunit a isoform 4

Gene

ATP6V0A4

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

Functioni

Part of the proton channel of the V-ATPase that is involved in normal vectorial acid transport into the urine by the kidney.By similarity

GO - Molecular functioni

  1. ATPase binding Source: UniProtKB
  2. hydrogen ion transmembrane transporter activity Source: InterPro

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: Ensembl
  2. cellular iron ion homeostasis Source: Reactome
  3. excretion Source: HGNC
  4. insulin receptor signaling pathway Source: Reactome
  5. interaction with host Source: Reactome
  6. ossification Source: HGNC
  7. phagosome maturation Source: Reactome
  8. proton transport Source: HGNC
  9. regulation of pH Source: HGNC
  10. sensory perception of sound Source: HGNC
  11. transferrin transport Source: Reactome
  12. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000105929-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Protein family/group databases

TCDBi3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase 116 kDa subunit a isoform 4
Short name:
V-ATPase 116 kDa isoform a4
Alternative name(s):
Vacuolar proton translocating ATPase 116 kDa subunit a isoform 4
Vacuolar proton translocating ATPase 116 kDa subunit a kidney isoform
Gene namesi
Name:ATP6V0A4
Synonyms:ATP6N1B, ATP6N2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:866. ATP6V0A4.

Subcellular locationi

Apical cell membrane; Multi-pass membrane protein
Note: Present at high density almost exclusively on the apical surface of alpha-intercalated cells in the cortical collecting ducts of the distal nephron.

GO - Cellular componenti

  1. apical part of cell Source: UniProtKB
  2. apical plasma membrane Source: UniProtKB
  3. brush border membrane Source: HGNC
  4. endosome Source: UniProtKB
  5. endosome membrane Source: Reactome
  6. extracellular vesicular exosome Source: UniProt
  7. integral component of membrane Source: UniProtKB-KW
  8. lysosomal membrane Source: UniProtKB
  9. phagocytic vesicle membrane Source: Reactome
  10. plasma membrane Source: UniProtKB
  11. vacuolar proton-transporting V-type ATPase, V0 domain Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Renal tubular acidosis, distal, autosomal recessive (RTADR) [MIM:602722]: An autosomal recessive disease characterized by reduced ability to acidify urine, variable hyperchloremic hypokalemic metabolic acidosis, nephrocalcinosis, and nephrolithiasis. It is due to functional failure of alpha-intercalated cells of the cortical collecting duct of the distal nephron, where vectorial proton transport is required for urinary acidification.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti175 – 1751G → D in RTADR. 1 Publication
VAR_020993
Natural varianti237 – 2371Missing in RTADR. 1 Publication
VAR_020994
Natural varianti449 – 4491R → H in RTADR. 1 Publication
VAR_020995
Natural varianti524 – 5241P → L in RTADR. 1 Publication
VAR_017255
Natural varianti580 – 5801M → T in RTADR. 1 Publication
Corresponds to variant rs3807153 [ dbSNP | Ensembl ].
VAR_017256
Natural varianti807 – 8071R → Q in RTADR. 1 Publication
Corresponds to variant rs28939081 [ dbSNP | Ensembl ].
VAR_020996
Natural varianti820 – 8201G → R in RTADR. 1 Publication
VAR_017257

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi602722. phenotype.
Orphaneti402041. Autosomal recessive distal renal tubular acidosis.
PharmGKBiPA25147.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 840840V-type proton ATPase 116 kDa subunit a isoform 4PRO_0000119219Add
BLAST

Proteomic databases

MaxQBiQ9HBG4.
PaxDbiQ9HBG4.
PRIDEiQ9HBG4.

PTM databases

PhosphoSiteiQ9HBG4.

Expressioni

Tissue specificityi

Expressed in adult and fetal kidney. Found in the inner ear.1 Publication

Gene expression databases

BgeeiQ9HBG4.
CleanExiHS_ATP6V0A4.
GenevestigatoriQ9HBG4.

Organism-specific databases

HPAiHPA018029.

Interactioni

Subunit structurei

The V-ATPase is a heteromultimeric enzyme composed of at least thirteen different subunits. It has a membrane peripheral V1 sector for ATP hydrolysis and an integral V0 for proton translocation. The V1 sector comprises subunits A-H, whereas V0 includes subunits a, d, c, c', and c''.

Protein-protein interaction databases

BioGridi119097. 2 interactions.
STRINGi9606.ENSP00000253856.

Structurei

3D structure databases

ProteinModelPortaliQ9HBG4.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 390390CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini410 – 4112VacuolarSequence Analysis
Topological domaini429 – 44315CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini474 – 53865VacuolarSequence AnalysisAdd
BLAST
Topological domaini559 – 57618CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini598 – 64245VacuolarSequence AnalysisAdd
BLAST
Topological domaini663 – 72765CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini753 – 77321VacuolarSequence AnalysisAdd
BLAST
Topological domaini813 – 84028CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei391 – 40919HelicalSequence AnalysisAdd
BLAST
Transmembranei412 – 42817HelicalSequence AnalysisAdd
BLAST
Transmembranei444 – 47330HelicalSequence AnalysisAdd
BLAST
Transmembranei539 – 55820HelicalSequence AnalysisAdd
BLAST
Transmembranei577 – 59721HelicalSequence AnalysisAdd
BLAST
Transmembranei643 – 66220HelicalSequence AnalysisAdd
BLAST
Transmembranei728 – 75225HelicalSequence AnalysisAdd
BLAST
Transmembranei774 – 81239HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase 116 kDa subunit family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1269.
GeneTreeiENSGT00390000004941.
HOGENOMiHOG000037059.
HOVERGENiHBG014606.
InParanoidiQ9HBG4.
KOiK02154.
OMAiHRAVSYL.
OrthoDBiEOG74FF04.
PhylomeDBiQ9HBG4.
TreeFamiTF300346.

Family and domain databases

InterProiIPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view]
PANTHERiPTHR11629. PTHR11629. 1 hit.
PfamiPF01496. V_ATPase_I. 1 hit.
[Graphical view]
PIRSFiPIRSF001293. ATP6V0A1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HBG4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVSVFRSEEM CLSQLFLQVE AAYCCVAELG ELGLVQFKDL NMNVNSFQRK
60 70 80 90 100
FVNEVRRCES LERILRFLED EMQNEIVVQL LEKSPLTPLP REMITLETVL
110 120 130 140 150
EKLEGELQEA NQNQQALKQS FLELTELKYL LKKTQDFFET ETNLADDFFT
160 170 180 190 200
EDTSGLLELK AVPAYMTGKL GFIAGVINRE RMASFERLLW RICRGNVYLK
210 220 230 240 250
FSEMDAPLED PVTKEEIQKN IFIIFYQGEQ LRQKIKKICD GFRATVYPCP
260 270 280 290 300
EPAVERREML ESVNVRLEDL ITVITQTESH RQRLLQEAAA NWHSWLIKVQ
310 320 330 340 350
KMKAVYHILN MCNIDVTQQC VIAEIWFPVA DATRIKRALE QGMELSGSSM
360 370 380 390 400
APIMTTVQSK TAPPTFNRTN KFTAGFQNIV DAYGVGSYRE INPAPYTIIT
410 420 430 440 450
FPFLFAVMFG DCGHGTVMLL AALWMILNER RLLSQKTDNE IWNTFFHGRY
460 470 480 490 500
LILLMGIFSI YTGLIYNDCF SKSLNIFGSS WSVQPMFRNG TWNTHVMEES
510 520 530 540 550
LYLQLDPAIP GVYFGNPYPF GIDPIWNLAS NKLTFLNSYK MKMSVILGIV
560 570 580 590 600
QMVFGVILSL FNHIYFRRTL NIILQFIPEM IFILCLFGYL VFMIIFKWCC
610 620 630 640 650
FDVHVSQHAP SILIHFINMF LFNYSDSSNA PLYKHQQEVQ SFFVVMALIS
660 670 680 690 700
VPWMLLIKPF ILRASHRKSQ LQASRIQEDA TENIEGDSSS PSSRSGQRTS
710 720 730 740 750
ADTHGALDDH GEEFNFGDVF VHQAIHTIEY CLGCISNTAS YLRLWALSLA
760 770 780 790 800
HAQLSEVLWT MVMNSGLQTR GWGGIVGVFI IFAVFAVLTV AILLIMEGLS
810 820 830 840
AFLHALRLHW VEFQNKFYVG DGYKFSPFSF KHILDGTAEE
Length:840
Mass (Da):96,386
Last modified:October 5, 2010 - v2
Checksum:i449964EBC01D4649
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2521P → R in AAI09305. (PubMed:15489334)Curated
Sequence conflicti252 – 2521P → R in AAI09306. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21V → A.2 Publications
Corresponds to variant rs10258719 [ dbSNP | Ensembl ].
VAR_020992
Natural varianti175 – 1751G → D in RTADR. 1 Publication
VAR_020993
Natural varianti237 – 2371Missing in RTADR. 1 Publication
VAR_020994
Natural varianti449 – 4491R → H in RTADR. 1 Publication
VAR_020995
Natural varianti524 – 5241P → L in RTADR. 1 Publication
VAR_017255
Natural varianti554 – 5541F → L.
Corresponds to variant rs1026435 [ dbSNP | Ensembl ].
VAR_066612
Natural varianti580 – 5801M → T in RTADR. 1 Publication
Corresponds to variant rs3807153 [ dbSNP | Ensembl ].
VAR_017256
Natural varianti604 – 6041H → Q.
Corresponds to variant rs3807154 [ dbSNP | Ensembl ].
VAR_066613
Natural varianti807 – 8071R → Q in RTADR. 1 Publication
Corresponds to variant rs28939081 [ dbSNP | Ensembl ].
VAR_020996
Natural varianti820 – 8201G → R in RTADR. 1 Publication
VAR_017257

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF245517 mRNA. Translation: AAG11415.1.
AK292945 mRNA. Translation: BAF85634.1.
AC018663 Genomic DNA. No translation available.
AC020983 Genomic DNA. No translation available.
CH236950 Genomic DNA. Translation: EAL24043.1.
CH471070 Genomic DNA. Translation: EAW83892.1.
BC109304 mRNA. Translation: AAI09305.1.
BC109305 mRNA. Translation: AAI09306.1.
CCDSiCCDS5849.1.
RefSeqiNP_065683.2. NM_020632.2.
NP_570855.2. NM_130840.2.
NP_570856.2. NM_130841.2.
XP_005250450.1. XM_005250393.1.
XP_005250451.1. XM_005250394.1.
UniGeneiHs.98967.

Genome annotation databases

EnsembliENST00000310018; ENSP00000308122; ENSG00000105929.
ENST00000353492; ENSP00000253856; ENSG00000105929.
ENST00000393054; ENSP00000376774; ENSG00000105929.
GeneIDi50617.
KEGGihsa:50617.
UCSCiuc003vuf.3. human.

Polymorphism databases

DMDMi308153516.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF245517 mRNA. Translation: AAG11415.1 .
AK292945 mRNA. Translation: BAF85634.1 .
AC018663 Genomic DNA. No translation available.
AC020983 Genomic DNA. No translation available.
CH236950 Genomic DNA. Translation: EAL24043.1 .
CH471070 Genomic DNA. Translation: EAW83892.1 .
BC109304 mRNA. Translation: AAI09305.1 .
BC109305 mRNA. Translation: AAI09306.1 .
CCDSi CCDS5849.1.
RefSeqi NP_065683.2. NM_020632.2.
NP_570855.2. NM_130840.2.
NP_570856.2. NM_130841.2.
XP_005250450.1. XM_005250393.1.
XP_005250451.1. XM_005250394.1.
UniGenei Hs.98967.

3D structure databases

ProteinModelPortali Q9HBG4.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119097. 2 interactions.
STRINGi 9606.ENSP00000253856.

Protein family/group databases

TCDBi 3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSitei Q9HBG4.

Polymorphism databases

DMDMi 308153516.

Proteomic databases

MaxQBi Q9HBG4.
PaxDbi Q9HBG4.
PRIDEi Q9HBG4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000310018 ; ENSP00000308122 ; ENSG00000105929 .
ENST00000353492 ; ENSP00000253856 ; ENSG00000105929 .
ENST00000393054 ; ENSP00000376774 ; ENSG00000105929 .
GeneIDi 50617.
KEGGi hsa:50617.
UCSCi uc003vuf.3. human.

Organism-specific databases

CTDi 50617.
GeneCardsi GC07M138391.
H-InvDB HIX0007123.
HGNCi HGNC:866. ATP6V0A4.
HPAi HPA018029.
MIMi 602722. phenotype.
605239. gene.
neXtProti NX_Q9HBG4.
Orphaneti 402041. Autosomal recessive distal renal tubular acidosis.
PharmGKBi PA25147.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1269.
GeneTreei ENSGT00390000004941.
HOGENOMi HOG000037059.
HOVERGENi HBG014606.
InParanoidi Q9HBG4.
KOi K02154.
OMAi HRAVSYL.
OrthoDBi EOG74FF04.
PhylomeDBi Q9HBG4.
TreeFami TF300346.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000105929-MONOMER.
Reactomei REACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Miscellaneous databases

GeneWikii ATP6V0A4.
GenomeRNAii 50617.
NextBioi 53132.
PROi Q9HBG4.
SOURCEi Search...

Gene expression databases

Bgeei Q9HBG4.
CleanExi HS_ATP6V0A4.
Genevestigatori Q9HBG4.

Family and domain databases

InterProi IPR002490. V-ATPase_116kDa_su.
IPR026028. V-type_ATPase_116kDa_su_euka.
[Graphical view ]
PANTHERi PTHR11629. PTHR11629. 1 hit.
Pfami PF01496. V_ATPase_I. 1 hit.
[Graphical view ]
PIRSFi PIRSF001293. ATP6V0A1. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mutations in ATP6N1B, encoding a new kidney vacuolar proton pump 116-kD subunit, cause recessive distal renal tubular acidosis with preserved hearing."
    Smith A.N., Skaug J., Choate K.A., Nayir A., Bakkaloglu A., Ozen S., Hulton S.A., Sanjad S.A., Al-Sabban E.A., Lifton R.P., Scherer S.W., Karet F.E.
    Nat. Genet. 26:71-75(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS RTADR LEU-524; THR-580 AND ARG-820, VARIANT ALA-2.
    Tissue: Kidney.
  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], VARIANT ALA-2.
    Tissue: Trachea.
  3. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Cited for: TISSUE SPECIFICITY, VARIANTS RTADR ASP-175; LYS-237 DEL; HIS-449 AND GLN-807.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiVPP4_HUMAN
AccessioniPrimary (citable) accession number: Q9HBG4
Secondary accession number(s): A4D1R4, A8KA80, Q32M47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: October 5, 2010
Last modified: October 29, 2014
This is version 116 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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