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Q9BT22

- ALG1_HUMAN

UniProt

Q9BT22 - ALG1_HUMAN

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Protein

Chitobiosyldiphosphodolichol beta-mannosyltransferase

Gene

ALG1

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

Functioni

Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. Involved in assembling the dolichol-pyrophosphate-GlcNAc(2)-Man5 intermediate on the cytoplasmic surface of the ER.1 Publication

Catalytic activityi

GDP-mannose + chitobiosyldiphosphodolichol = GDP + beta-1,4-D-mannosylchitobiosyldiphosphodolichol.

Pathwayi

GO - Molecular functioni

  1. chitobiosyldiphosphodolichol beta-mannosyltransferase activity Source: UniProtKB-EC
  2. mannosyltransferase activity Source: ProtInc

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. dolichol-linked oligosaccharide biosynthetic process Source: Reactome
  3. lipopolysaccharide biosynthetic process Source: ProtInc
  4. mannosylation Source: GOC
  5. post-translational protein modification Source: Reactome
  6. protein glycosylation Source: ProtInc
  7. protein N-linked glycosylation via asparagine Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.142. 2681.
ReactomeiREACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT33. Glycosyltransferase Family 33.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitobiosyldiphosphodolichol beta-mannosyltransferase (EC:2.4.1.142)
Alternative name(s):
Asparagine-linked glycosylation protein 1 homolog
Beta-1,4-mannosyltransferase
GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase
GDP-mannose-dolichol diphosphochitobiose mannosyltransferase
Mannosyltransferase-1
Short name:
MT-1
Short name:
hMat-1
Gene namesi
Name:ALG1
Synonyms:HMAT1, HMT1
ORF Names:PSEC0061, UNQ861/PRO1870
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:18294. ALG1.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: ProtInc
  2. endoplasmic reticulum membrane Source: Reactome
  3. integral component of membrane Source: UniProtKB-KW
  4. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Congenital disorder of glycosylation 1K (CDG1K) [MIM:608540]: A multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti150 – 1501S → R in CDG1K; impairs activity. 1 Publication
Corresponds to variant rs121908340 [ dbSNP | Ensembl ].
VAR_023364
Natural varianti258 – 2581S → L in CDG1K; impairs activity. 3 Publications
Corresponds to variant rs28939378 [ dbSNP | Ensembl ].
VAR_023365
Natural varianti342 – 3421Q → P in CDG1K; impairs activity. 1 Publication
VAR_023366

Keywords - Diseasei

Congenital disorder of glycosylation, Disease mutation

Organism-specific databases

MIMi608540. phenotype.
Orphaneti79327. ALG1-CDG.
PharmGKBiPA134979319.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464Chitobiosyldiphosphodolichol beta-mannosyltransferasePRO_0000080249Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei242 – 2421Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BT22.
PaxDbiQ9BT22.
PRIDEiQ9BT22.

PTM databases

PhosphoSiteiQ9BT22.

Expressioni

Gene expression databases

BgeeiQ9BT22.
CleanExiHS_ALG1.
ExpressionAtlasiQ9BT22. baseline and differential.
GenevestigatoriQ9BT22.

Organism-specific databases

HPAiHPA060392.

Interactioni

Protein-protein interaction databases

BioGridi121033. 4 interactions.
IntActiQ9BT22. 1 interaction.
STRINGi9606.ENSP00000262374.

Structurei

3D structure databases

ProteinModelPortaliQ9BT22.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 22CytoplasmicSequence Analysis
Topological domaini24 – 464441LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei3 – 2321Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0438.
GeneTreeiENSGT00390000008647.
HOGENOMiHOG000216716.
HOVERGENiHBG055036.
InParanoidiQ9BT22.
KOiK03842.
OMAiIVGYKET.
OrthoDBiEOG70W3DB.
PhylomeDBiQ9BT22.
TreeFamiTF314121.

Family and domain databases

InterProiIPR026051. ALG1-like.
[Graphical view]
PANTHERiPTHR13036. PTHR13036. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BT22-1) [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
MAASCLVLLA LCLLLPLLLL GGWKRWRRGR AARHVVAVVL GDVGRSPRMQ
60 70 80 90 100
YHALSLAMHG FSVTLLGFCN SKPHDELLQN NRIQIVGLTE LQSLAVGPRV
110 120 130 140 150
FQYGVKVVLQ AMYLLWKLMW REPGAYIFLQ NPPGLPSIAV CWFVGCLCGS
160 170 180 190 200
KLVIDWHNYG YSIMGLVHGP NHPLVLLAKW YEKFFGRLSH LNLCVTNAMR
210 220 230 240 250
EDLADNWHIR AVTVYDKPAS FFKETPLDLQ HRLFMKLGSM HSPFRARSEP
260 270 280 290 300
EDPVTERSAF TERDAGSGLV TRLRERPALL VSSTSWTEDE DFSILLAALE
310 320 330 340 350
KFEQLTLDGH NLPSLVCVIT GKGPLREYYS RLIHQKHFQH IQVCTPWLEA
360 370 380 390 400
EDYPLLLGSA DLGVCLHTSS SGLDLPMKVV DMFGCCLPVC AVNFKCLHEL
410 420 430 440 450
VKHEENGLVF EDSEELAAQL QMLFSNFPDP AGKLNQFRKN LRESQQLRWD
460
ESWVQTVLPL VMDT
Length:464
Mass (Da):52,518
Last modified:August 30, 2005 - v2
Checksum:i83F55FD12CFDDBE9
GO
Isoform 2 (identifier: Q9BT22-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-111: Missing.

Note: No experimental confirmation available

Show »
Length:353
Mass (Da):40,338
Checksum:i118C424301EABD77
GO

Sequence cautioni

The sequence AAQ89432.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti150 – 1501S → R in CDG1K; impairs activity. 1 Publication
Corresponds to variant rs121908340 [ dbSNP | Ensembl ].
VAR_023364
Natural varianti258 – 2581S → L in CDG1K; impairs activity. 3 Publications
Corresponds to variant rs28939378 [ dbSNP | Ensembl ].
VAR_023365
Natural varianti267 – 2671S → N.1 Publication
Corresponds to variant rs17849848 [ dbSNP | Ensembl ].
VAR_038425
Natural varianti325 – 3251L → M.1 Publication
Corresponds to variant rs17852920 [ dbSNP | Ensembl ].
VAR_038426
Natural varianti342 – 3421Q → P in CDG1K; impairs activity. 1 Publication
VAR_023366
Natural varianti429 – 4291D → E No effect on activity. 1 Publication
Corresponds to variant rs9745522 [ dbSNP | Ensembl ].
VAR_023367
Natural varianti438 – 4381R → W.
Corresponds to variant rs16835020 [ dbSNP | Ensembl ].
VAR_049350
Natural varianti455 – 4551Q → R.1 Publication
Corresponds to variant rs17856919 [ dbSNP | Ensembl ].
VAR_038427

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 111111Missing in isoform 2. 1 PublicationVSP_056931Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB019038 mRNA. Translation: BAA90748.1.
AK298144 mRNA. Translation: BAG60420.1.
AK075373 mRNA. Translation: BAC11576.1.
AC026458 Genomic DNA. No translation available.
BC004402 mRNA. Translation: AAH04402.1.
BC031095 mRNA. Translation: AAH31095.1.
AY359073 mRNA. Translation: AAQ89432.1. Different initiation.
CCDSiCCDS10528.1.
RefSeqiNP_061982.3. NM_019109.4.
UniGeneiHs.592086.

Genome annotation databases

EnsembliENST00000262374; ENSP00000262374; ENSG00000033011.
GeneIDi56052.
KEGGihsa:56052.
UCSCiuc002cyj.3. human.

Polymorphism databases

DMDMi73921663.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB019038 mRNA. Translation: BAA90748.1 .
AK298144 mRNA. Translation: BAG60420.1 .
AK075373 mRNA. Translation: BAC11576.1 .
AC026458 Genomic DNA. No translation available.
BC004402 mRNA. Translation: AAH04402.1 .
BC031095 mRNA. Translation: AAH31095.1 .
AY359073 mRNA. Translation: AAQ89432.1 . Different initiation.
CCDSi CCDS10528.1.
RefSeqi NP_061982.3. NM_019109.4.
UniGenei Hs.592086.

3D structure databases

ProteinModelPortali Q9BT22.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121033. 4 interactions.
IntActi Q9BT22. 1 interaction.
STRINGi 9606.ENSP00000262374.

Protein family/group databases

CAZyi GT33. Glycosyltransferase Family 33.

PTM databases

PhosphoSitei Q9BT22.

Polymorphism databases

DMDMi 73921663.

Proteomic databases

MaxQBi Q9BT22.
PaxDbi Q9BT22.
PRIDEi Q9BT22.

Protocols and materials databases

DNASUi 56052.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262374 ; ENSP00000262374 ; ENSG00000033011 .
GeneIDi 56052.
KEGGi hsa:56052.
UCSCi uc002cyj.3. human.

Organism-specific databases

CTDi 56052.
GeneCardsi GC16P005121.
H-InvDB HIX0009871.
HIX0009901.
HIX0021452.
HIX0030817.
HIX0030848.
HIX0031467.
HIX0036459.
HGNCi HGNC:18294. ALG1.
HPAi HPA060392.
MIMi 605907. gene.
608540. phenotype.
neXtProti NX_Q9BT22.
Orphaneti 79327. ALG1-CDG.
PharmGKBi PA134979319.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0438.
GeneTreei ENSGT00390000008647.
HOGENOMi HOG000216716.
HOVERGENi HBG055036.
InParanoidi Q9BT22.
KOi K03842.
OMAi IVGYKET.
OrthoDBi EOG70W3DB.
PhylomeDBi Q9BT22.
TreeFami TF314121.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BRENDAi 2.4.1.142. 2681.
Reactomei REACT_22433. Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein.

Miscellaneous databases

GeneWikii ALG1.
GenomeRNAii 56052.
NextBioi 61475.
PROi Q9BT22.
SOURCEi Search...

Gene expression databases

Bgeei Q9BT22.
CleanExi HS_ALG1.
ExpressionAtlasi Q9BT22. baseline and differential.
Genevestigatori Q9BT22.

Family and domain databases

InterProi IPR026051. ALG1-like.
[Graphical view ]
PANTHERi PTHR13036. PTHR13036. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the human cDNA which can complement the defect of the yeast mannosyltransferase I-deficient mutant alg 1."
    Takahashi T., Honda R., Nishikawa Y.
    Glycobiology 10:321-327(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Fetal brain.
  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 2).
  3. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Teratocarcinoma.
  4. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [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 1), VARIANTS ASN-267; MET-325 AND ARG-455.
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-464 (ISOFORM 1).
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Deficiency of GDP-Man:GlcNAc2-PP-dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik."
    Schwarz M., Thiel C., Luebbehusen J., Dorland B., de Koning T., von Figura K., Lehle L., Koerner C.
    Am. J. Hum. Genet. 74:472-481(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CDG1K LEU-258.
  10. "Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of mannosyltransferase I."
    Kranz C., Denecke J., Lehle L., Sohlbach K., Jeske S., Meinhardt F., Rossi R., Gudowius S., Marquardt T.
    Am. J. Hum. Genet. 74:545-551(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CDG1K LEU-258 AND PRO-342.
  11. "Deficiency of the first mannosylation step in the N-glycosylation pathway causes congenital disorder of glycosylation type Ik."
    Grubenmann C.E., Frank C.G., Huelsmeier A.J., Schollen E., Matthijs G., Mayatepek E., Berger E.G., Aebi M., Hennet T.
    Hum. Mol. Genet. 13:535-542(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS CDG1K ARG-150 AND LEU-258, VARIANT GLU-429.

Entry informationi

Entry nameiALG1_HUMAN
AccessioniPrimary (citable) accession number: Q9BT22
Secondary accession number(s): B4DP08
, Q6UVZ9, Q8N5Y4, Q9P2Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: August 30, 2005
Last modified: October 29, 2014
This is version 123 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 16
    Human chromosome 16: 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