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Q9NPC4

- A4GAT_HUMAN

UniProt

Q9NPC4 - A4GAT_HUMAN

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Protein

Lactosylceramide 4-alpha-galactosyltransferase

Gene

A4GALT

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

Functioni

Necessary for the biosynthesis of the Pk antigen of blood histogroup P. Catalyzes the transfer of galactose to lactosylceramide and galactosylceramide. Necessary for the synthesis of the receptor for bacterial verotoxins.

Catalytic activityi

UDP-alpha-D-galactose + beta-D-galactosyl-(1->4)-D-glucosyl-(1<->1)-ceramide = UDP + alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-D-glucosyl-(1<->1)-ceramide.

Pathwayi

GO - Molecular functioni

  1. galactosyltransferase activity Source: UniProtKB
  2. lactosylceramide 4-alpha-galactosyltransferase activity Source: UniProtKB-EC
  3. toxic substance binding Source: Ensembl

GO - Biological processi

  1. globoside biosynthetic process Source: Ensembl
  2. glycosphingolipid biosynthetic process Source: UniProtKB
  3. plasma membrane organization Source: MGI
  4. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

BRENDAi2.4.1.228. 2681.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT32. Glycosyltransferase Family 32.

Names & Taxonomyi

Protein namesi
Recommended name:
Lactosylceramide 4-alpha-galactosyltransferase (EC:2.4.1.228)
Alternative name(s):
Alpha-1,4-N-acetylglucosaminyltransferase
Alpha-1,4-galactosyltransferase
Alpha4Gal-T1
CD77 synthase
Globotriaosylceramide synthase
Short name:
Gb3 synthase
P1/Pk synthase
UDP-galactose:beta-D-galactosyl-beta1-R 4-alpha-D-galactosyltransferase
Gene namesi
Name:A4GALT
Synonyms:A14GALT, A4GALT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:18149. A4GALT.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2222CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei23 – 4321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini44 – 353310LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. integral component of Golgi membrane Source: UniProtKB
  3. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

MIMi111400. phenotype.
PharmGKBiPA24359.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353Lactosylceramide 4-alpha-galactosyltransferasePRO_0000080578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi121 – 1211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi203 – 2031N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9NPC4.
PRIDEiQ9NPC4.

PTM databases

PhosphoSiteiQ9NPC4.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in kidney, heart, spleen, liver, testis and placenta.

Gene expression databases

BgeeiQ9NPC4.
CleanExiHS_A4GALT.
ExpressionAtlasiQ9NPC4. baseline.
GenevestigatoriQ9NPC4.

Organism-specific databases

HPAiHPA001141.

Interactioni

Protein-protein interaction databases

BioGridi119825. 6 interactions.
IntActiQ9NPC4. 2 interactions.
MINTiMINT-5210812.
STRINGi9606.ENSP00000249005.

Structurei

3D structure databases

ProteinModelPortaliQ9NPC4.
SMRiQ9NPC4. Positions 150-197.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi192 – 1943DXD motifBy similarity

Domaini

The conserved DXD motif is involved in enzyme activity.By similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 32 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG251623.
GeneTreeiENSGT00510000047981.
HOVERGENiHBG050427.
InParanoidiQ9NPC4.
KOiK01988.
OMAiISFKFTF.
OrthoDBiEOG75MVW8.
PhylomeDBiQ9NPC4.
TreeFamiTF324053.

Family and domain databases

InterProiIPR007652. A1-4-GlycosylTfrase_dom.
IPR007577. GlycoTrfase_DXD_sugar-bd_CS.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF04572. Gb3_synth. 1 hit.
PF04488. Gly_transf_sug. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9NPC4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKPPDLLLR LLRGAPRQRV CTLFIIGFKF TFFVSIMIYW HVVGEPKEKG
60 70 80 90 100
QLYNLPAEIP CPTLTPPTPP SHGPTPGNIF FLETSDRTNP NFLFMCSVES
110 120 130 140 150
AARTHPESHV LVLMKGLPGG NASLPRHLGI SLLSCFPNVQ MLPLDLRELF
160 170 180 190 200
RDTPLADWYA AVQGRWEPYL LPVLSDASRI ALMWKFGGIY LDTDFIVLKN
210 220 230 240 250
LRNLTNVLGT QSRYVLNGAF LAFERRHEFM ALCMRDFVDH YNGWIWGHQG
260 270 280 290 300
PQLLTRVFKK WCSIRSLAES RACRGVTTLP PEAFYPIPWQ DWKKYFEDIN
310 320 330 340 350
PEELPRLLSA TYAVHVWNKK SQGTRFEATS RALLAQLHAR YCPTTHEAMK

MYL
Length:353
Mass (Da):40,499
Last modified:October 1, 2000 - v1
Checksum:i8755865BDA5DA205
GO

Polymorphismi

Genetic variation in A4GALT is responsible for the P system blood group phenotypes [MIMi:111400]. Different combinations or absence of the P blood group system antigens define 5 different phenotypes: P1, P2, P1(k), P2(k), and p. Genetic variation in A4GALT determines the p phenotype, which is rare and does not express any antigens. It is also known as null phenotype; p individuals have antibodies against P, P1 and Pk antigens in their sera. These antibodies are clinically important because they can cause severe transfusion reactions and miscarriage.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti37 – 371M → V.3 Publications
Corresponds to variant rs11541159 [ dbSNP | Ensembl ].
VAR_014296
Natural varianti80 – 801Missing in p individuals. 1 Publication
VAR_017507
Natural varianti163 – 1631Q → R.1 Publication
Corresponds to variant rs28915383 [ dbSNP | Ensembl ].
VAR_022320
Natural varianti183 – 1831M → K in p individuals; complete loss of activity. 2 Publications
VAR_014297
Natural varianti187 – 1871G → D in p individuals; partial loss of activity. 1 Publication
Corresponds to variant rs28940572 [ dbSNP | Ensembl ].
VAR_017508
Natural varianti251 – 2511P → L in p individuals; complete loss of activity. 1 Publication
Corresponds to variant rs28940571 [ dbSNP | Ensembl ].
VAR_017509

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037883 mRNA. Translation: BAA95915.1.
AJ245581 mRNA. Translation: CAB93532.1.
AB041418 Genomic DNA. Translation: BAA94503.1.
AY941797 Genomic DNA. Translation: AAX20109.1.
AK312927 mRNA. Translation: BAG35771.1.
Z82176 Genomic DNA. Translation: CAI18757.1.
CH471138 Genomic DNA. Translation: EAW73274.1.
BC017068 mRNA. Translation: AAH17068.1.
CCDSiCCDS14041.1.
RefSeqiNP_059132.1. NM_017436.4.
XP_005261700.1. XM_005261643.1.
XP_005261701.1. XM_005261644.1.
XP_005261703.1. XM_005261646.2.
XP_005261704.1. XM_005261647.1.
XP_005261705.1. XM_005261648.1.
XP_006724328.1. XM_006724265.1.
XP_006724329.1. XM_006724266.1.
XP_006724330.1. XM_006724267.1.
UniGeneiHs.105956.

Genome annotation databases

EnsembliENST00000249005; ENSP00000249005; ENSG00000128274.
ENST00000381278; ENSP00000370678; ENSG00000128274.
ENST00000401850; ENSP00000384794; ENSG00000128274.
GeneIDi53947.
KEGGihsa:53947.
UCSCiuc003bdb.3. human.

Polymorphism databases

DMDMi25452796.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

SeattleSNPs
Functional Glycomics Gateway - GTase

Lactosylceramide 4-alpha-galactosyltransferase

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037883 mRNA. Translation: BAA95915.1 .
AJ245581 mRNA. Translation: CAB93532.1 .
AB041418 Genomic DNA. Translation: BAA94503.1 .
AY941797 Genomic DNA. Translation: AAX20109.1 .
AK312927 mRNA. Translation: BAG35771.1 .
Z82176 Genomic DNA. Translation: CAI18757.1 .
CH471138 Genomic DNA. Translation: EAW73274.1 .
BC017068 mRNA. Translation: AAH17068.1 .
CCDSi CCDS14041.1.
RefSeqi NP_059132.1. NM_017436.4.
XP_005261700.1. XM_005261643.1.
XP_005261701.1. XM_005261644.1.
XP_005261703.1. XM_005261646.2.
XP_005261704.1. XM_005261647.1.
XP_005261705.1. XM_005261648.1.
XP_006724328.1. XM_006724265.1.
XP_006724329.1. XM_006724266.1.
XP_006724330.1. XM_006724267.1.
UniGenei Hs.105956.

3D structure databases

ProteinModelPortali Q9NPC4.
SMRi Q9NPC4. Positions 150-197.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119825. 6 interactions.
IntActi Q9NPC4. 2 interactions.
MINTi MINT-5210812.
STRINGi 9606.ENSP00000249005.

Protein family/group databases

CAZyi GT32. Glycosyltransferase Family 32.

PTM databases

PhosphoSitei Q9NPC4.

Polymorphism databases

DMDMi 25452796.

Proteomic databases

PaxDbi Q9NPC4.
PRIDEi Q9NPC4.

Protocols and materials databases

DNASUi 53947.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000249005 ; ENSP00000249005 ; ENSG00000128274 .
ENST00000381278 ; ENSP00000370678 ; ENSG00000128274 .
ENST00000401850 ; ENSP00000384794 ; ENSG00000128274 .
GeneIDi 53947.
KEGGi hsa:53947.
UCSCi uc003bdb.3. human.

Organism-specific databases

CTDi 53947.
GeneCardsi GC22M043088.
HGNCi HGNC:18149. A4GALT.
HPAi HPA001141.
MIMi 111400. phenotype.
607922. gene.
neXtProti NX_Q9NPC4.
PharmGKBi PA24359.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG251623.
GeneTreei ENSGT00510000047981.
HOVERGENi HBG050427.
InParanoidi Q9NPC4.
KOi K01988.
OMAi ISFKFTF.
OrthoDBi EOG75MVW8.
PhylomeDBi Q9NPC4.
TreeFami TF324053.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.228. 2681.

Miscellaneous databases

GeneWikii A4GALT.
GenomeRNAii 53947.
NextBioi 56264.
PROi Q9NPC4.
SOURCEi Search...

Gene expression databases

Bgeei Q9NPC4.
CleanExi HS_A4GALT.
ExpressionAtlasi Q9NPC4. baseline.
Genevestigatori Q9NPC4.

Family and domain databases

InterProi IPR007652. A1-4-GlycosylTfrase_dom.
IPR007577. GlycoTrfase_DXD_sugar-bd_CS.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
Pfami PF04572. Gb3_synth. 1 hit.
PF04488. Gly_transf_sug. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of globotriaosylceramide/CD77 synthase, a glycosyltransferase that initiates the synthesis of globo series glycosphingolipids."
    Kojima Y., Fukumoto S., Furukawa K., Okajima T., Wiels J., Yokoyama K., Suzuki Y., Urano T., Ohta M., Furukawa K.
    J. Biol. Chem. 275:15152-15156(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Melanoma.
  2. "Cloning and expression of the histo-blood group Pk UDP-galactose:Galbeta1-4Glcbeta1-Cer alpha1,4-galactosyltransferase. Molecular genetic basis of the p phenotype."
    Steffensen R., Carlier K., Wiels J., Levery S.B., Stroud M., Cedergren B., Nilsson Sojka B., Bennett E.P., Jersild C., Clausen H.
    J. Biol. Chem. 275:16723-16729(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-37 AND LYS-183.
  3. "Human-specific amino acid changes found in 103 protein-coding genes."
    Kitano T., Liu Y.-H., Ueda S., Saitou N.
    Mol. Biol. Evol. 21:936-944(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. SeattleSNPs variation discovery resource
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-37 AND ARG-163.
  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].
    Tissue: Tongue.
  6. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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].
    Tissue: Uterus.
  9. "Molecular basis for the p phenotype. Identification of distinct and multiple mutations in the alpha 1,4-galactosyltransferase gene in Swedish and Japanese individuals."
    Furukawa K., Iwamura K., Uchikawa M., Sojka B.N., Wiels J., Okajima T., Urano T., Furukawa K.
    J. Biol. Chem. 275:37752-37756(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS VAL-37; LYS-183; ASP-187 AND LEU-251.
  10. "Three-base deletion and one-base insertion of the alpha(1,4)galactosyltransferase gene responsible for the P phenotype."
    Koda Y., Soejima M., Sato H., Maeda Y., Kimura H.
    Transfusion 42:48-51(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PHE-80 DEL.

Entry informationi

Entry nameiA4GAT_HUMAN
AccessioniPrimary (citable) accession number: Q9NPC4
Secondary accession number(s): B2R7C4, Q9P1X5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2002
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 124 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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