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Protein

Acetylcholine receptor subunit gamma

Gene

CHRNG

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

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
Complete GO annotation...

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 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:1967. CHRNG.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 240218ExtracellularSequence AnalysisAdd
BLAST
Transmembranei241 – 26525HelicalSequence AnalysisAdd
BLAST
Transmembranei275 – 29319HelicalSequence AnalysisAdd
BLAST
Transmembranei309 – 33022HelicalSequence AnalysisAdd
BLAST
Topological domaini331 – 474144CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei475 – 49521HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Multiple pterygium syndrome, lethal type (LMPS)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionMultiple 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.

See also OMIM:253290
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)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionNon-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.

See also OMIM:265000
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.

Chemistry

DrugBankiDB00674. Galantamine.

Polymorphism and mutation databases

BioMutaiCHRNG.
DMDMi126302510.

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

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
KRT31Q153233EBI-9008836,EBI-948001
KRTAP10-7P604093EBI-9008836,EBI-10172290
KRTAP10-8P604103EBI-9008836,EBI-10171774
KRTAP10-9P604113EBI-9008836,EBI-10172052
NOTCH2NLQ7Z3S93EBI-9008836,EBI-945833

Protein-protein interaction databases

BioGridi107568. 8 interactions.
IntActiP07510. 5 interactions.
STRINGi9606.ENSP00000374145.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG291810.
GeneTreeiENSGT00770000120477.
HOGENOMiHOG000006757.
HOVERGENiHBG003756.
InParanoidiP07510.
KOiK04818.
OMAiPSTMVWR.
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. AlignAdd to basket

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

        10         20         30         40         50
MHGGQGPLLL LLLLAVCLGA QGRNQEERLL ADLMQNYDPN LRPAERDSDV
60 70 80 90 100
VNVSLKLTLT NLISLNEREE ALTTNVWIEM QWCDYRLRWD PRDYEGLWVL
110 120 130 140 150
RVPSTMVWRP DIVLENNVDG VFEVALYCNV LVSPDGCIYW LPPAIFRSAC
160 170 180 190 200
SISVTYFPFD WQNCSLIFQS QTYSTNEIDL QLSQEDGQTI EWIFIDPEAF
210 220 230 240 250
TENGEWAIQH RPAKMLLDPA APAQEAGHQK VVFYLLIQRK PLFYVINIIA
260 270 280 290 300
PCVLISSVAI LIHFLPAKAG GQKCTVAINV LLAQTVFLFL VAKKVPETSQ
310 320 330 340 350
AVPLISKYLT FLLVVTILIV VNAVVVLNVS LRSPHTHSMA RGVRKVFLRL
360 370 380 390 400
LPQLLRMHVR PLAPAAVQDT QSRLQNGSSG WSITTGEEVA LCLPRSELLF
410 420 430 440 450
QQWQRQGLVA AALEKLEKGP ELGLSQFCGS LKQAAPAIQA CVEACNLIAC
460 470 480 490 500
ARHQQSHFDN GNEEWFLVGR VLDRVCFLAM LSLFICGTAG IFLMAHYNRV
510
PALPFPGDPR PYLPSPD
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. Curated
The sequence CAA25861.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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. [P07510-1]
PIRiA23261.
RefSeqiNP_005190.4. NM_005199.4. [P07510-1]
UniGeneiHs.248101.

Genome annotation databases

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

Polymorphism and mutation databases

BioMutaiCHRNG.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P07510-1]
PIRiA23261.
RefSeqiNP_005190.4. NM_005199.4. [P07510-1]
UniGeneiHs.248101.

3D structure databases

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

Protein-protein interaction databases

BioGridi107568. 8 interactions.
IntActiP07510. 5 interactions.
STRINGi9606.ENSP00000374145.

Chemistry

BindingDBiP07510.
ChEMBLiCHEMBL1907588.
DrugBankiDB00674. Galantamine.
GuidetoPHARMACOLOGYi475.

Protein family/group databases

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

PTM databases

PhosphoSiteiP07510.

Polymorphism and mutation databases

BioMutaiCHRNG.
DMDMi126302510.

Proteomic databases

PaxDbiP07510.
PRIDEiP07510.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1146.
GeneCardsiGC02P233404.
HGNCiHGNC:1967. CHRNG.
MIMi100730. gene.
253290. phenotype.
265000. phenotype.
neXtProtiNX_P07510.
Orphaneti2990. Autosomal recessive multiple pterygium syndrome.
33108. Lethal multiple pterygium syndrome.
PharmGKBiPA26499.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG291810.
GeneTreeiENSGT00770000120477.
HOGENOMiHOG000006757.
HOVERGENiHBG003756.
InParanoidiP07510.
KOiK04818.
OMAiPSTMVWR.
OrthoDBiEOG7H7925.
PhylomeDBiP07510.
TreeFamiTF315605.

Enzyme and pathway databases

ReactomeiREACT_22223. Highly sodium permeable acetylcholine nicotinic receptors.

Miscellaneous databases

GeneWikiiCHRNG.
GenomeRNAii1146.
NextBioi4768.
PROiP07510.
SOURCEiSearch...

Gene expression databases

BgeeiP07510.
CleanExiHS_CHRNG.
GenevestigatoriP07510.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 151 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.