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P07510

- ACHG_HUMAN

UniProt

P07510 - ACHG_HUMAN

Protein

Acetylcholine receptor subunit gamma

Gene

CHRNG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (20 Feb 2007)
      Previous versions | rss
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    Functioni

    After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.

    GO - Molecular functioni

    1. acetylcholine-activated cation-selective channel activity Source: Ensembl
    2. acetylcholine receptor activity Source: ProtInc
    3. channel activity Source: ProtInc

    GO - Biological processi

    1. muscle contraction Source: ProtInc
    2. regulation of membrane potential Source: Ensembl
    3. signal transduction Source: ProtInc
    4. synaptic transmission Source: Reactome
    5. transmembrane transport Source: GOC
    6. transport Source: ProtInc

    Keywords - Molecular functioni

    Ion channel, Ligand-gated ion channel, Receptor

    Keywords - Biological processi

    Ion transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_22223. Highly sodium permeable acetylcholine nicotinic receptors.

    Protein family/group databases

    TCDBi1.A.9.1.1. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetylcholine receptor subunit gamma
    Gene namesi
    Name:CHRNG
    Synonyms:ACHRG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:1967. CHRNG.

    Subcellular locationi

    GO - Cellular componenti

    1. acetylcholine-gated channel complex Source: Ensembl
    2. cell junction Source: UniProtKB-KW
    3. integral component of membrane Source: UniProtKB-KW
    4. integral component of plasma membrane Source: ProtInc
    5. plasma membrane Source: Reactome
    6. postsynaptic membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Involvement in diseasei

    Multiple pterygium syndrome, lethal type (LMPS) [MIM:253290]: Multiple pterygia are found infrequently in children with arthrogryposis and in fetuses with fetal akinesia syndrome. In lethal multiple pterygium syndrome there is intrauterine growth retardation, multiple pterygia, and flexion contractures causing severe arthrogryposis and fetal akinesia. Subcutaneous edema can be severe, causing fetal hydrops with cystic hygroma and lung hypoplasia. Oligohydramnios and facial anomalies are frequent.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071V → G in EVMPS and LMPS. 1 Publication
    VAR_030753
    Natural varianti239 – 2391R → C in EVMPS and LMPS. 1 Publication
    VAR_030755
    Multiple pterygium syndrome, Escobar variant (EVMPS) [MIM:265000]: Non-lethal form of arthrogryposis multiplex congenita. It is an autosomal recessive condition characterized by excessive webbing (pterygia), congenital contractures (arthrogryposis), and scoliosis. Variable other features include intrauterine death, congenital respiratory distress, short stature, faciocranial dysmorphism, ptosis, low-set ears, arachnodactyly and cryptorchism in males. Congenital contractures are common and may be caused by reduced fetal movements at sensitive times of development. Possible causes of decreased fetal mobility include space constraints such as oligohydramnion, drugs, metabolic conditions or neuromuscular disorders including myasthenia gravis.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071V → G in EVMPS and LMPS. 1 Publication
    VAR_030753
    Natural varianti239 – 2391R → C in EVMPS and LMPS. 1 Publication
    VAR_030755

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi253290. phenotype.
    265000. phenotype.
    Orphaneti2990. Autosomal recessive multiple pterygium syndrome.
    33108. Lethal multiple pterygium syndrome.
    PharmGKBiPA26499.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 517495Acetylcholine receptor subunit gammaPRO_0000000334Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi52 – 521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi150 ↔ 164By similarity
    Glycosylationi163 – 1631N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP07510.
    PRIDEiP07510.

    PTM databases

    PhosphoSiteiP07510.

    Expressioni

    Gene expression databases

    ArrayExpressiP07510.
    BgeeiP07510.
    CleanExiHS_CHRNG.
    GenevestigatoriP07510.

    Interactioni

    Subunit structurei

    Pentamer of two alpha chains, and one each of the beta, delta, and gamma (in immature muscle) or epsilon (in mature muscle) chains.

    Protein-protein interaction databases

    BioGridi107568. 1 interaction.
    STRINGi9606.ENSP00000374145.

    Structurei

    3D structure databases

    ProteinModelPortaliP07510.
    SMRiP07510. Positions 24-338, 436-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 240218ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini331 – 474144CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei241 – 26525HelicalSequence AnalysisAdd
    BLAST
    Transmembranei275 – 29319HelicalSequence AnalysisAdd
    BLAST
    Transmembranei309 – 33022HelicalSequence AnalysisAdd
    BLAST
    Transmembranei475 – 49521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG291810.
    HOGENOMiHOG000006757.
    HOVERGENiHBG003756.
    InParanoidiP07510.
    KOiK04818.
    OMAiVFYLLIQ.
    OrthoDBiEOG7H7925.
    PhylomeDBiP07510.
    TreeFamiTF315605.

    Family and domain databases

    Gene3Di1.20.120.370. 2 hits.
    2.70.170.10. 1 hit.
    InterProiIPR027361. Acetylcholine_rcpt_TM.
    IPR006202. Neur_chan_lig-bd.
    IPR006201. Neur_channel.
    IPR006029. Neurotrans-gated_channel_TM.
    IPR018000. Neurotransmitter_ion_chnl_CS.
    IPR002394. Nicotinic_acetylcholine_rcpt.
    [Graphical view]
    PANTHERiPTHR18945. PTHR18945. 1 hit.
    PfamiPF02931. Neur_chan_LBD. 1 hit.
    PF02932. Neur_chan_memb. 1 hit.
    [Graphical view]
    PRINTSiPR00254. NICOTINICR.
    PR00252. NRIONCHANNEL.
    SUPFAMiSSF63712. SSF63712. 1 hit.
    SSF90112. SSF90112. 1 hit.
    PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
    [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: P07510-1) [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

    MHGGQGPLLL LLLLAVCLGA QGRNQEERLL ADLMQNYDPN LRPAERDSDV    50
    VNVSLKLTLT NLISLNEREE ALTTNVWIEM QWCDYRLRWD PRDYEGLWVL 100
    RVPSTMVWRP DIVLENNVDG VFEVALYCNV LVSPDGCIYW LPPAIFRSAC 150
    SISVTYFPFD WQNCSLIFQS QTYSTNEIDL QLSQEDGQTI EWIFIDPEAF 200
    TENGEWAIQH RPAKMLLDPA APAQEAGHQK VVFYLLIQRK PLFYVINIIA 250
    PCVLISSVAI LIHFLPAKAG GQKCTVAINV LLAQTVFLFL VAKKVPETSQ 300
    AVPLISKYLT FLLVVTILIV VNAVVVLNVS LRSPHTHSMA RGVRKVFLRL 350
    LPQLLRMHVR PLAPAAVQDT QSRLQNGSSG WSITTGEEVA LCLPRSELLF 400
    QQWQRQGLVA AALEKLEKGP ELGLSQFCGS LKQAAPAIQA CVEACNLIAC 450
    ARHQQSHFDN GNEEWFLVGR VLDRVCFLAM LSLFICGTAG IFLMAHYNRV 500
    PALPFPGDPR PYLPSPD 517
    Length:517
    Mass (Da):57,883
    Last modified:February 20, 2007 - v2
    Checksum:i7C78F533D4997D7A
    GO
    Isoform 2 (identifier: P07510-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         117-169: NVDGVFEVALYCNVLVSPDGCIYWLPPAIFRSACSISVTYFPFDWQNCSLIFQ → K

    Note: No experimental confirmation available.

    Show »
    Length:465
    Mass (Da):52,020
    Checksum:i6EB30D70535EFAE3
    GO

    Sequence cautioni

    The sequence AAY24103.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAA25861.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti189 – 1891T → S in AAI11803. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti107 – 1071V → G in EVMPS and LMPS. 1 Publication
    VAR_030753
    Natural varianti149 – 1491A → T.
    Corresponds to variant rs2289080 [ dbSNP | Ensembl ].
    VAR_030754
    Natural varianti239 – 2391R → C in EVMPS and LMPS. 1 Publication
    VAR_030755

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei117 – 16953NVDGV…SLIFQ → K in isoform 2. 1 PublicationVSP_055775Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01715
    , X01716, X01717, X01718, X01719, X01720, X01721, X04759 Genomic DNA. Translation: CAA25861.1. Sequence problems.
    AK125362 mRNA. Translation: BAG54190.1.
    AC092165 Genomic DNA. Translation: AAY24103.1. Sequence problems.
    BC111802 mRNA. Translation: AAI11803.1.
    CCDSiCCDS33400.1.
    PIRiA23261.
    RefSeqiNP_005190.4. NM_005199.4.
    UniGeneiHs.248101.

    Genome annotation databases

    EnsembliENST00000389492; ENSP00000374143; ENSG00000196811. [P07510-2]
    ENST00000389494; ENSP00000374145; ENSG00000196811. [P07510-1]
    GeneIDi1146.
    KEGGihsa:1146.
    UCSCiuc002vsx.1. human.

    Polymorphism databases

    DMDMi126302510.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01715
    , X01716 , X01717 , X01718 , X01719 , X01720 , X01721 , X04759 Genomic DNA. Translation: CAA25861.1 . Sequence problems.
    AK125362 mRNA. Translation: BAG54190.1 .
    AC092165 Genomic DNA. Translation: AAY24103.1 . Sequence problems.
    BC111802 mRNA. Translation: AAI11803.1 .
    CCDSi CCDS33400.1.
    PIRi A23261.
    RefSeqi NP_005190.4. NM_005199.4.
    UniGenei Hs.248101.

    3D structure databases

    ProteinModelPortali P07510.
    SMRi P07510. Positions 24-338, 436-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107568. 1 interaction.
    STRINGi 9606.ENSP00000374145.

    Chemistry

    BindingDBi P07510.
    ChEMBLi CHEMBL1907588.
    DrugBanki DB00674. Galantamine.
    GuidetoPHARMACOLOGYi 475.

    Protein family/group databases

    TCDBi 1.A.9.1.1. the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.

    PTM databases

    PhosphoSitei P07510.

    Polymorphism databases

    DMDMi 126302510.

    Proteomic databases

    PaxDbi P07510.
    PRIDEi P07510.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389492 ; ENSP00000374143 ; ENSG00000196811 . [P07510-2 ]
    ENST00000389494 ; ENSP00000374145 ; ENSG00000196811 . [P07510-1 ]
    GeneIDi 1146.
    KEGGi hsa:1146.
    UCSCi uc002vsx.1. human.

    Organism-specific databases

    CTDi 1146.
    GeneCardsi GC02P233404.
    HGNCi HGNC:1967. CHRNG.
    MIMi 100730. gene.
    253290. phenotype.
    265000. phenotype.
    neXtProti NX_P07510.
    Orphaneti 2990. Autosomal recessive multiple pterygium syndrome.
    33108. Lethal multiple pterygium syndrome.
    PharmGKBi PA26499.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291810.
    HOGENOMi HOG000006757.
    HOVERGENi HBG003756.
    InParanoidi P07510.
    KOi K04818.
    OMAi VFYLLIQ.
    OrthoDBi EOG7H7925.
    PhylomeDBi P07510.
    TreeFami TF315605.

    Enzyme and pathway databases

    Reactomei REACT_22223. Highly sodium permeable acetylcholine nicotinic receptors.

    Miscellaneous databases

    GeneWikii CHRNG.
    GenomeRNAii 1146.
    NextBioi 4768.
    PROi P07510.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07510.
    Bgeei P07510.
    CleanExi HS_CHRNG.
    Genevestigatori P07510.

    Family and domain databases

    Gene3Di 1.20.120.370. 2 hits.
    2.70.170.10. 1 hit.
    InterProi IPR027361. Acetylcholine_rcpt_TM.
    IPR006202. Neur_chan_lig-bd.
    IPR006201. Neur_channel.
    IPR006029. Neurotrans-gated_channel_TM.
    IPR018000. Neurotransmitter_ion_chnl_CS.
    IPR002394. Nicotinic_acetylcholine_rcpt.
    [Graphical view ]
    PANTHERi PTHR18945. PTHR18945. 1 hit.
    Pfami PF02931. Neur_chan_LBD. 1 hit.
    PF02932. Neur_chan_memb. 1 hit.
    [Graphical view ]
    PRINTSi PR00254. NICOTINICR.
    PR00252. NRIONCHANNEL.
    SUPFAMi SSF63712. SSF63712. 1 hit.
    SSF90112. SSF90112. 1 hit.
    PROSITEi PS00236. NEUROTR_ION_CHANNEL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and sequence analysis of human genomic DNA encoding gamma subunit precursor of muscle acetylcholine receptor."
      Shibahara S., Kubo T., Perski H.J., Takahashi H., Noda M., Numa S.
      Eur. J. Biochem. 146:15-22(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Primary structure of the human muscle acetylcholine receptor. cDNA cloning of the gamma and epsilon subunits."
      Beeson D.M.W., Brydson M., Betty M., Jeremiah S., Povey S., Vincent A., Newsom-Davis J.
      Eur. J. Biochem. 215:229-238(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Muscle fibroblast.
    3. "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 1).
      Tissue: Tongue.
    4. "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].
    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] (ISOFORM 2).
    6. Cited for: VARIANT EVMPS CYS-239, VARIANT LMPS CYS-239.
    7. "Mutations in the embryonal subunit of the acetylcholine receptor (CHRNG) cause lethal and Escobar variants of multiple pterygium syndrome."
      Morgan N.V., Brueton L.A., Cox P., Greally M.T., Tolmie J., Pasha S., Aligianis I.A., van Bokhoven H., Marton T., Al-Gazali L., Morton J.E.V., Oley C., Johnson C.A., Trembath R.C., Brunner H.G., Maher E.R.
      Am. J. Hum. Genet. 79:390-395(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EVMPS GLY-107, VARIANT LMPS GLY-107.

    Entry informationi

    Entry nameiACHG_HUMAN
    AccessioniPrimary (citable) accession number: P07510
    Secondary accession number(s): B3KWM8, Q14DU4, Q53RG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: February 20, 2007
    Last modified: October 1, 2014
    This is version 145 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 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3