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P23109

- AMPD1_HUMAN

UniProt

P23109 - AMPD1_HUMAN

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Protein

AMP deaminase 1

Gene

AMPD1

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

Functioni

AMP deaminase plays a critical role in energy metabolism.

Catalytic activityi

AMP + H2O = IMP + NH3.

Cofactori

Binds 1 zinc ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi336 – 3361Zinc; catalyticBy similarity
Metal bindingi338 – 3381Zinc; catalyticBy similarity
Binding sitei338 – 3381SubstrateBy similarity
Metal bindingi605 – 6051Zinc; catalyticBy similarity
Binding sitei608 – 6081SubstrateBy similarity
Active sitei627 – 6271Proton acceptorPROSITE-ProRule annotation
Metal bindingi682 – 6821Zinc; catalyticBy similarity

GO - Molecular functioni

  1. AMP deaminase activity Source: ProtInc
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. IMP salvage Source: UniProtKB-UniPathway
  2. nucleobase-containing small molecule metabolic process Source: Reactome
  3. purine-containing compound salvage Source: Reactome
  4. purine nucleobase metabolic process Source: Reactome
  5. response to organic substance Source: Ensembl
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1923. Purine salvage.
SABIO-RKP23109.
UniPathwayiUPA00591; UER00663.

Names & Taxonomyi

Protein namesi
Recommended name:
AMP deaminase 1 (EC:3.5.4.6)
Alternative name(s):
AMP deaminase isoform M
Myoadenylate deaminase
Gene namesi
Name:AMPD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:468. AMPD1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Myopathy due to myoadenylate deaminase deficiency (MMDD) [MIM:615511]: A metabolic disorder resulting in exercise-related myopathy. It is characterized by exercise-induced muscle aches, cramps, and early fatigue.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti421 – 4211R → W in MMDD; loss of activity. 1 Publication
Corresponds to variant rs35859650 [ dbSNP | Ensembl ].
VAR_013271
Natural varianti458 – 4581R → H in MMDD; loss of activity. 1 Publication
VAR_013272

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615511. phenotype.
Orphaneti45. Adenosine monophosphate deaminase deficiency.
PharmGKBiPA24776.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 780780AMP deaminase 1PRO_0000194403Add
BLAST

Proteomic databases

PaxDbiP23109.
PRIDEiP23109.

PTM databases

PhosphoSiteiP23109.

Expressioni

Tissue specificityi

Three isoforms are present in mammals: AMP deaminase 1 is the predominant form in skeletal muscle; AMP deaminase 2 predominates in smooth muscle, non-muscle tissue, embryonic muscle and undifferentiated myoblasts; AMP deaminase 3 is found in erythrocytes.

Gene expression databases

BgeeiP23109.
CleanExiHS_AMPD1.
ExpressionAtlasiP23109. baseline and differential.
GenevestigatoriP23109.

Organism-specific databases

HPAiHPA026478.
HPA028080.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi106767. 5 interactions.
IntActiP23109. 5 interactions.
STRINGi9606.ENSP00000316520.

Structurei

3D structure databases

ProteinModelPortaliP23109.
SMRiP23109. Positions 225-775.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni407 – 4126Substrate bindingBy similarity
Regioni683 – 6864Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1816.
GeneTreeiENSGT00390000008190.
HOGENOMiHOG000092200.
HOVERGENiHBG050494.
InParanoidiP23109.
KOiK01490.
OMAiNMTWMIQ.
OrthoDBiEOG70ZZMQ.
PhylomeDBiP23109.
TreeFamiTF300439.

Family and domain databases

InterProiIPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029770. AMPD1.
[Graphical view]
PANTHERiPTHR11359. PTHR11359. 1 hit.
PTHR11359:SF1. PTHR11359:SF1. 1 hit.
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
PIRSFiPIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsiTIGR01429. AMP_deaminase. 1 hit.
PROSITEiPS00485. A_DEAMINASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P23109) [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
MNVRIFYSVS QSPHSLLSLL FYCAILESRI SATMPLFKLP AEEKQIDDAM
60 70 80 90 100
RNFAEKVFAS EVKDEGGRQE ISPFDVDEIC PISHHEMQAH IFHLETLSTS
110 120 130 140 150
TEARRKKRFQ GRKTVNLSIP LSETSSTKLS HIDEYISSSP TYQTVPDFQR
160 170 180 190 200
VQITGDYASG VTVEDFEIVC KGLYRALCIR EKYMQKSFQR FPKTPSKYLR
210 220 230 240 250
NIDGEAWVAN ESFYPVFTPP VKKGEDPFRT DNLPENLGYH LKMKDGVVYV
260 270 280 290 300
YPNEAAVSKD EPKPLPYPNL DTFLDDMNFL LALIAQGPVK TYTHRRLKFL
310 320 330 340 350
SSKFQVHQML NEMDELKELK NNPHRDFYNC RKVDTHIHAA ACMNQKHLLR
360 370 380 390 400
FIKKSYQIDA DRVVYSTKEK NLTLKELFAK LKMHPYDLTV DSLDVHAGRQ
410 420 430 440 450
TFQRFDKFND KYNPVGASEL RDLYLKTDNY INGEYFATII KEVGADLVEA
460 470 480 490 500
KYQHAEPRLS IYGRSPDEWS KLSSWFVCNR IHCPNMTWMI QVPRIYDVFR
510 520 530 540 550
SKNFLPHFGK MLENIFMPVF EATINPQADP ELSVFLKHIT GFDSVDDESK
560 570 580 590 600
HSGHMFSSKS PKPQEWTLEK NPSYTYYAYY MYANIMVLNS LRKERGMNTF
610 620 630 640 650
LFRPHCGEAG ALTHLMTAFM IADDISHGLN LKKSPVLQYL FFLAQIPIAM
660 670 680 690 700
SPLSNNSLFL EYAKNPFLDF LQKGLMISLS TDDPMQFHFT KEPLMEEYAI
710 720 730 740 750
AAQVFKLSTC DMCEVARNSV LQCGISHEEK VKFLGDNYLE EGPAGNDIRR
760 770 780
TNVAQIRMAY RYETWCYELN LIAEGLKSTE
Length:780
Mass (Da):90,219
Last modified:April 18, 2012 - v2
Checksum:i2449E96D00312629
GO
Isoform 2 (identifier: P23109-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     41-45: AEEKQ → E

Show »
Length:776
Mass (Da):89,763
Checksum:iB831F57E1D7AA491
GO

Sequence cautioni

The sequence AAA57281.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAG24258.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAF84038.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAG36918.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence CAI18828.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2341P → S in BAF84038. (PubMed:14702039)Curated
Sequence conflicti306 – 3061V → A in BAF84038. (PubMed:14702039)Curated
Sequence conflicti467 – 4671D → G in BAG36918. (PubMed:14702039)Curated
Sequence conflicti475 – 4751W → R in BAF84038. (PubMed:14702039)Curated
Sequence conflicti659 – 6591F → S in BAF84038. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti55 – 551E → K.
Corresponds to variant rs2273268 [ dbSNP | Ensembl ].
VAR_048860
Natural varianti81 – 811P → L Polymorphism; activity comparable to wild-type. 1 Publication
Corresponds to variant rs61752479 [ dbSNP | Ensembl ].
VAR_013270
Natural varianti421 – 4211R → W in MMDD; loss of activity. 1 Publication
Corresponds to variant rs35859650 [ dbSNP | Ensembl ].
VAR_013271
Natural varianti458 – 4581R → H in MMDD; loss of activity. 1 Publication
VAR_013272
Natural varianti666 – 6661P → H in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035801

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei41 – 455AEEKQ → E in isoform 2. CuratedVSP_042638

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37931
, M37920, M37921, M37922, M37923, M37924, M37927, M37928, M37929, M37930 Genomic DNA. Translation: AAG24258.1. Different initiation.
AL096773 Genomic DNA. Translation: CAI18828.1. Different initiation.
AL096773 Genomic DNA. Translation: CAI18830.1.
CH471122 Genomic DNA. Translation: EAW56607.1.
M60092 mRNA. Translation: AAA57281.1. Different initiation.
AK314252 mRNA. Translation: BAG36918.1. Different initiation.
AK291349 mRNA. Translation: BAF84038.1. Different initiation.
CCDSiCCDS53349.1. [P23109-2]
CCDS876.2. [P23109-1]
PIRiI39444.
RefSeqiNP_000027.2. NM_000036.2. [P23109-1]
NP_001166097.1. NM_001172626.1. [P23109-2]
UniGeneiHs.89570.

Genome annotation databases

EnsembliENST00000369538; ENSP00000358551; ENSG00000116748. [P23109-2]
ENST00000520113; ENSP00000430075; ENSG00000116748. [P23109-1]
GeneIDi270.
KEGGihsa:270.
UCSCiuc001efe.2. human. [P23109-1]
uc001eff.2. human. [P23109-2]

Polymorphism databases

DMDMi384872309.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M37931
, M37920 , M37921 , M37922 , M37923 , M37924 , M37927 , M37928 , M37929 , M37930 Genomic DNA. Translation: AAG24258.1 . Different initiation.
AL096773 Genomic DNA. Translation: CAI18828.1 . Different initiation.
AL096773 Genomic DNA. Translation: CAI18830.1 .
CH471122 Genomic DNA. Translation: EAW56607.1 .
M60092 mRNA. Translation: AAA57281.1 . Different initiation.
AK314252 mRNA. Translation: BAG36918.1 . Different initiation.
AK291349 mRNA. Translation: BAF84038.1 . Different initiation.
CCDSi CCDS53349.1. [P23109-2 ]
CCDS876.2. [P23109-1 ]
PIRi I39444.
RefSeqi NP_000027.2. NM_000036.2. [P23109-1 ]
NP_001166097.1. NM_001172626.1. [P23109-2 ]
UniGenei Hs.89570.

3D structure databases

ProteinModelPortali P23109.
SMRi P23109. Positions 225-775.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106767. 5 interactions.
IntActi P23109. 5 interactions.
STRINGi 9606.ENSP00000316520.

Chemistry

BindingDBi P23109.
ChEMBLi CHEMBL2869.
DrugBanki DB00131. Adenosine monophosphate.

PTM databases

PhosphoSitei P23109.

Polymorphism databases

DMDMi 384872309.

Proteomic databases

PaxDbi P23109.
PRIDEi P23109.

Protocols and materials databases

DNASUi 270.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000369538 ; ENSP00000358551 ; ENSG00000116748 . [P23109-2 ]
ENST00000520113 ; ENSP00000430075 ; ENSG00000116748 . [P23109-1 ]
GeneIDi 270.
KEGGi hsa:270.
UCSCi uc001efe.2. human. [P23109-1 ]
uc001eff.2. human. [P23109-2 ]

Organism-specific databases

CTDi 270.
GeneCardsi GC01M115215.
H-InvDB HIX0199913.
HGNCi HGNC:468. AMPD1.
HPAi HPA026478.
HPA028080.
MIMi 102770. gene.
615511. phenotype.
neXtProti NX_P23109.
Orphaneti 45. Adenosine monophosphate deaminase deficiency.
PharmGKBi PA24776.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1816.
GeneTreei ENSGT00390000008190.
HOGENOMi HOG000092200.
HOVERGENi HBG050494.
InParanoidi P23109.
KOi K01490.
OMAi NMTWMIQ.
OrthoDBi EOG70ZZMQ.
PhylomeDBi P23109.
TreeFami TF300439.

Enzyme and pathway databases

UniPathwayi UPA00591 ; UER00663 .
Reactomei REACT_1923. Purine salvage.
SABIO-RK P23109.

Miscellaneous databases

ChiTaRSi AMPD1. human.
GeneWikii AMP_deaminase.
GenomeRNAii 270.
NextBioi 1061.
PROi P23109.
SOURCEi Search...

Gene expression databases

Bgeei P23109.
CleanExi HS_AMPD1.
ExpressionAtlasi P23109. baseline and differential.
Genevestigatori P23109.

Family and domain databases

InterProi IPR006650. A/AMP_deam_AS.
IPR001365. A/AMP_deaminase_dom.
IPR006329. AMPD.
IPR029770. AMPD1.
[Graphical view ]
PANTHERi PTHR11359. PTHR11359. 1 hit.
PTHR11359:SF1. PTHR11359:SF1. 1 hit.
Pfami PF00962. A_deaminase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001251. AMP_deaminase_met. 1 hit.
TIGRFAMsi TIGR01429. AMP_deaminase. 1 hit.
PROSITEi PS00485. A_DEAMINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of the human and rat myoadenylate deaminase genes."
    Sabina R.L., Morisaki T., Clarke P., Eddy R., Shows T.B., Morton C.C., Holmes E.W.
    J. Biol. Chem. 265:9423-9433(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Molecular analysis of the myoadenylate deaminase deficiencies."
    Sabina R.L., Fishbein W.N., Pezeshkpour G., Clarke P.R., Holmes E.W.
    Neurology 42:170-179(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-780 (ISOFORM 1).
  5. "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] OF 15-780 (ISOFORM 1).
    Tissue: Pericardium and Tongue.
  6. Cited for: VARIANT LEU-81.
  7. "First missense mutations (R388W and R425H) of AMPD1 accompanied with myopathy found in a Japanese patient."
    Morisaki H., Higuchi I., Abe M., Osame M., Morisaki T.
    Hum. Mutat. 16:467-472(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MMDD TRP-421 AND HIS-458.
  8. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-666.

Entry informationi

Entry nameiAMPD1_HUMAN
AccessioniPrimary (citable) accession number: P23109
Secondary accession number(s): A8K5N4
, B2RAM1, F2Z3B3, Q5TF00, Q5TF02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 18, 2012
Last modified: October 29, 2014
This is version 138 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

Caution

It is uncertain whether Met-1 or Met-34 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3