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Q96D96

- HVCN1_HUMAN

UniProt

Q96D96 - HVCN1_HUMAN

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Protein

Voltage-gated hydrogen channel 1

Gene

HVCN1

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

Functioni

Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis.3 Publications

Enzyme regulationi

The dimers display cooperative channel gating (By similarity). The channel activity is inhibited by zinc ions.By similarity2 Publications

GO - Molecular functioni

  1. voltage-gated cation channel activity Source: Reactome
  2. voltage-gated proton channel activity Source: UniProtKB

GO - Biological processi

  1. cellular response to pH Source: UniProtKB
  2. cellular response to zinc ion Source: UniProtKB
  3. multicellular organism reproduction Source: Reactome
  4. proton transport Source: UniProtKB
  5. response to pH Source: HGNC
  6. response to zinc ion Source: HGNC
  7. single fertilization Source: Reactome
  8. sperm-egg recognition Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_163875. Sperm Motility And Taxes.

Protein family/group databases

TCDBi1.A.51.1.2. the voltage-gated proton channel (vpc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-gated hydrogen channel 1
Alternative name(s):
Hydrogen voltage-gated channel 1
Short name:
HV1
Voltage sensor domain-only protein
Gene namesi
Name:HVCN1
Synonyms:VSOP
ORF Names:UNQ578/PRO1140
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:28240. HVCN1.

Subcellular locationi

Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein
Note: Detected mainly at intracellular membranes upon overexpression in HeLa cells (PuMed:20147290), but not in other cell types.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 100100CytoplasmicBy similarityAdd
BLAST
Transmembranei101 – 12121Helical; Name=Segment S1By similarityAdd
BLAST
Topological domaini122 – 13817ExtracellularBy similarityAdd
BLAST
Transmembranei139 – 16123Helical; Name=Segment S2By similarityAdd
BLAST
Topological domaini162 – 1698CytoplasmicBy similarity
Transmembranei170 – 19021Helical; Name=Segment S3By similarityAdd
BLAST
Topological domaini191 – 1977ExtracellularBy similarity
Transmembranei198 – 21821Helical; Name=Segment S4By similarityAdd
BLAST
Topological domaini219 – 27355CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: HGNC
  2. integral component of plasma membrane Source: UniProtKB
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291T → A: Loss of a phosphorylation site. Reduces phosphorylation. 1 Publication
Mutagenesisi97 – 971S → A: Loss of a phosphorylation site. Strongly reduces phosphorylation. 1 Publication
Mutagenesisi112 – 1121D → A, F, N or S: Alters channel selectivity. Converts the proton channel to an anion channel. 1 Publication
Mutagenesisi112 – 1121D → E: No effect on channel activity and proton selectivity. 1 Publication
Mutagenesisi112 – 1121D → V: Abolishes channel activity. 1 Publication
Mutagenesisi140 – 1401H → A: Exhibits selectivity to protons but sensitivity to zinc ions is abolished; when associated with A-193. 2 Publications
Mutagenesisi193 – 1931H → A: Exhibits selectivity to protons but sensitivity to zinc ions is abolished; when associated with A-140. 2 Publications
Mutagenesisi205 – 2051R → A: Faster channel activation and deactivation kinetics. 1 Publication
Mutagenesisi208 – 2081R → A: Faster channel activation and deactivation kinetics. 1 Publication
Mutagenesisi211 – 2111R → A: Faster channel deactivation kinetics. 1 Publication

Organism-specific databases

PharmGKBiPA144596422.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 273273Voltage-gated hydrogen channel 1PRO_0000342187Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291Phosphothreonine1 Publication
Modified residuei97 – 971Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation may enhance channel gating.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96D96.
PaxDbiQ96D96.
PRIDEiQ96D96.

PTM databases

PhosphoSiteiQ96D96.

Expressioni

Tissue specificityi

Enriched in immune tissues, such as lymph nodes, B-lymphocytes, monocytes and spleen.1 Publication

Gene expression databases

BgeeiQ96D96.
CleanExiHS_HVCN1.
ExpressionAtlasiQ96D96. baseline and differential.
GenevestigatoriQ96D96.

Organism-specific databases

HPAiHPA039329.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi124053. 7 interactions.
DIPiDIP-46112N.
MINTiMINT-4724965.
STRINGi9606.ENSP00000349181.

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi227 – 26539Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A2AX-ray2.00A/B/C/D221-273[»]
ProteinModelPortaliQ96D96.
SMRiQ96D96. Positions 88-266.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili223 – 266441 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi46 – 5510Poly-Glu
Compositional biasi176 – 1805Poly-Val

Domaini

The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Unlike other voltage-gated ion channels it lacks the pore domain.1 Publication
The C-terminal coiled coil region mediates homodimerization and cooperative channel gating. It is essential for normal subcellular localization.1 Publication

Sequence similaritiesi

Belongs to the hydrogen channel family.Curated

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG46709.
GeneTreeiENSGT00530000063670.
HOGENOMiHOG000067871.
HOVERGENiHBG102207.
InParanoidiQ96D96.
OMAiEFSCSEK.
OrthoDBiEOG789CDV.
PhylomeDBiQ96D96.
TreeFamiTF332056.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
[Graphical view]
PfamiPF00520. Ion_trans. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q96D96-1) [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
MATWDEKAVT RRAKVAPAER MSKFLRHFTV VGDDYHAWNI NYKKWENEEE
60 70 80 90 100
EEEEEQPPPT PVSGEEGRAA APDVAPAPGP APRAPLDFRG MLRKLFSSHR
110 120 130 140 150
FQVIIICLVV LDALLVLAEL ILDLKIIQPD KNNYAAMVFH YMSITILVFF
160 170 180 190 200
MMEIIFKLFV FRLEFFHHKF EILDAVVVVV SFILDIVLLF QEHQFEALGL
210 220 230 240 250
LILLRLWRVA RIINGIIISV KTRSERQLLR LKQMNVQLAA KIQHLEFSCS
260 270
EKEQEIERLN KLLRQHGLLG EVN
Length:273
Mass (Da):31,683
Last modified:December 1, 2001 - v1
Checksum:i0F93B428AECBBC4F
GO
Isoform 2 (identifier: Q96D96-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     66-102: Missing.

Show »
Length:236
Mass (Da):27,713
Checksum:i1AD13F7D49A62C4D
GO
Isoform 3 (identifier: Q96D96-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     253-273: EQEIERLNKLLRQHGLLGEVN → PLD

Note: No experimental confirmation available.

Show »
Length:255
Mass (Da):29,538
Checksum:i092B095DD219550A
GO
Isoform 4 (identifier: Q96D96-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: Missing.

Note: No experimental confirmation available.

Show »
Length:253
Mass (Da):29,415
Checksum:iF1349C26BCC164F1
GO

Sequence cautioni

The sequence AAQ89413.1 differs from that shown. Reason: Frameshift at positions 164 and 175. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651F → Y in BAG57024. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020Missing in isoform 4. 1 PublicationVSP_045052Add
BLAST
Alternative sequencei66 – 10237Missing in isoform 2. 1 PublicationVSP_034395Add
BLAST
Alternative sequencei253 – 27321EQEIE…LGEVN → PLD in isoform 3. 1 PublicationVSP_034396Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY359054 mRNA. Translation: AAQ89413.1. Frameshift.
AK293543 mRNA. Translation: BAG57024.1.
AC144522 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97935.1.
CH471054 Genomic DNA. Translation: EAW97936.1.
BC007277 mRNA. Translation: AAH07277.1.
BC009731 mRNA. Translation: AAH09731.1.
BC032672 mRNA. Translation: AAH32672.1.
CCDSiCCDS31900.1. [Q96D96-1]
CCDS58278.1. [Q96D96-4]
RefSeqiNP_001035196.1. NM_001040107.1. [Q96D96-1]
NP_001243342.1. NM_001256413.1. [Q96D96-4]
NP_115745.2. NM_032369.3. [Q96D96-1]
XP_005254005.1. XM_005253948.1. [Q96D96-1]
XP_005254006.1. XM_005253949.1. [Q96D96-2]
XP_006719703.1. XM_006719640.1. [Q96D96-1]
UniGeneiHs.211511.
Hs.334637.

Genome annotation databases

EnsembliENST00000242607; ENSP00000242607; ENSG00000122986. [Q96D96-1]
ENST00000356742; ENSP00000349181; ENSG00000122986. [Q96D96-1]
ENST00000439744; ENSP00000412052; ENSG00000122986. [Q96D96-4]
ENST00000548312; ENSP00000449601; ENSG00000122986. [Q96D96-3]
ENST00000620084; ENSP00000479812; ENSG00000122986. [Q96D96-1]
GeneIDi84329.
KEGGihsa:84329.
UCSCiuc001trq.1. human. [Q96D96-3]
uc001trs.2. human. [Q96D96-1]

Polymorphism databases

DMDMi74751810.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY359054 mRNA. Translation: AAQ89413.1 . Frameshift.
AK293543 mRNA. Translation: BAG57024.1 .
AC144522 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97935.1 .
CH471054 Genomic DNA. Translation: EAW97936.1 .
BC007277 mRNA. Translation: AAH07277.1 .
BC009731 mRNA. Translation: AAH09731.1 .
BC032672 mRNA. Translation: AAH32672.1 .
CCDSi CCDS31900.1. [Q96D96-1 ]
CCDS58278.1. [Q96D96-4 ]
RefSeqi NP_001035196.1. NM_001040107.1. [Q96D96-1 ]
NP_001243342.1. NM_001256413.1. [Q96D96-4 ]
NP_115745.2. NM_032369.3. [Q96D96-1 ]
XP_005254005.1. XM_005253948.1. [Q96D96-1 ]
XP_005254006.1. XM_005253949.1. [Q96D96-2 ]
XP_006719703.1. XM_006719640.1. [Q96D96-1 ]
UniGenei Hs.211511.
Hs.334637.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3A2A X-ray 2.00 A/B/C/D 221-273 [» ]
ProteinModelPortali Q96D96.
SMRi Q96D96. Positions 88-266.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124053. 7 interactions.
DIPi DIP-46112N.
MINTi MINT-4724965.
STRINGi 9606.ENSP00000349181.

Chemistry

GuidetoPHARMACOLOGYi 746.

Protein family/group databases

TCDBi 1.A.51.1.2. the voltage-gated proton channel (vpc) family.

PTM databases

PhosphoSitei Q96D96.

Polymorphism databases

DMDMi 74751810.

Proteomic databases

MaxQBi Q96D96.
PaxDbi Q96D96.
PRIDEi Q96D96.

Protocols and materials databases

DNASUi 84329.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000242607 ; ENSP00000242607 ; ENSG00000122986 . [Q96D96-1 ]
ENST00000356742 ; ENSP00000349181 ; ENSG00000122986 . [Q96D96-1 ]
ENST00000439744 ; ENSP00000412052 ; ENSG00000122986 . [Q96D96-4 ]
ENST00000548312 ; ENSP00000449601 ; ENSG00000122986 . [Q96D96-3 ]
ENST00000620084 ; ENSP00000479812 ; ENSG00000122986 . [Q96D96-1 ]
GeneIDi 84329.
KEGGi hsa:84329.
UCSCi uc001trq.1. human. [Q96D96-3 ]
uc001trs.2. human. [Q96D96-1 ]

Organism-specific databases

CTDi 84329.
GeneCardsi GC12M111086.
H-InvDB HIX0011039.
HGNCi HGNC:28240. HVCN1.
HPAi HPA039329.
MIMi 611227. gene.
neXtProti NX_Q96D96.
PharmGKBi PA144596422.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46709.
GeneTreei ENSGT00530000063670.
HOGENOMi HOG000067871.
HOVERGENi HBG102207.
InParanoidi Q96D96.
OMAi EFSCSEK.
OrthoDBi EOG789CDV.
PhylomeDBi Q96D96.
TreeFami TF332056.

Enzyme and pathway databases

Reactomei REACT_163875. Sperm Motility And Taxes.

Miscellaneous databases

ChiTaRSi HVCN1. human.
GeneWikii HVCN1.
GenomeRNAii 84329.
NextBioi 74079.
PROi Q96D96.
SOURCEi Search...

Gene expression databases

Bgeei Q96D96.
CleanExi HS_HVCN1.
ExpressionAtlasi Q96D96. baseline and differential.
Genevestigatori Q96D96.

Family and domain databases

Gene3Di 1.20.120.350. 1 hit.
InterProi IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
[Graphical view ]
Pfami PF00520. Ion_trans. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
  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 4).
    Tissue: Cerebellum.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1 AND 2).
    Tissue: Eye, Lung and Testis.
  6. "A voltage-gated proton-selective channel lacking the pore domain."
    Ramsey I.S., Moran M.M., Chong J.A., Clapham D.E.
    Nature 440:1213-1216(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ENZYME REGULATION, MUTAGENESIS OF HIS-140; HIS-193; ARG-205; ARG-208 AND ARG-211.
  7. "Identification of Thr29 as a critical phosphorylation site that activates the human proton channel Hvcn1 in leukocytes."
    Musset B., Capasso M., Cherny V.V., Morgan D., Bhamrah M., Dyer M.J., DeCoursey T.E.
    J. Biol. Chem. 285:5117-5121(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-29 AND SER-97, MUTAGENESIS OF THR-29 AND SER-97, FUNCTION, SUBCELLULAR LOCATION.
  8. "Aspartate 112 is the selectivity filter of the human voltage-gated proton channel."
    Musset B., Smith S.M., Rajan S., Morgan D., Cherny V.V., Decoursey T.E.
    Nature 480:273-277(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-112; HIS-140 AND HIS-193, SUBCELLULAR LOCATION, ENZYME REGULATION.
  9. "The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1."
    Li S.J., Zhao Q., Zhou Q., Unno H., Zhai Y., Sun F.
    J. Biol. Chem. 285:12047-12054(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 221-273, SUBUNIT, SUBCELLULAR LOCATION, COILED COIL, DOMAIN.

Entry informationi

Entry nameiHVCN1_HUMAN
AccessioniPrimary (citable) accession number: Q96D96
Secondary accession number(s): A8MQ37
, B4DEB3, F8WCH5, Q6UW11, Q96IS5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 2008
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 107 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3