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Q9UBM8

- MGT4C_HUMAN

UniProt

Q9UBM8 - MGT4C_HUMAN

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Protein

Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C

Gene

MGAT4C

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

Functioni

Glycosyltransferase that participates in the transfer of N-acetylglucosamine (GlcNAc) to the core mannose residues of N-linked glycans. Catalyzes the formation of the GlcNAcbeta1-4 branch on the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans. Essential for the production of tri- and tetra-antennary N-linked sugar chains (By similarity). Does not catalyze the transfer of GlcNAc to the Manalpha1-6 arm to form GlcNAcBeta1-4Manalpha1-6 linkage ('GnT-VI' activity).By similarity1 Publication

Catalytic activityi

UDP-N-acetyl-D-glucosamine + 3-(2-(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2,4-bis(N-acetyl-beta-D-glucosaminyl)-alpha-D-mannosyl)-beta-D-mannosyl-R.

Cofactori

a divalent metal cationBy similarityNote: Divalent metal cations.By similarity

Pathwayi

GO - Molecular functioni

  1. alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. post-translational protein modification Source: Reactome
  3. protein N-linked glycosylation via asparagine Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS00017-MONOMER.
ReactomeiREACT_25085. N-Glycan antennae elongation.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT54. Glycosyltransferase Family 54.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase C (EC:2.4.1.145)
Alternative name(s):
N-acetylglucosaminyltransferase IV homolog
Short name:
hGnT-IV-H
N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVc
Short name:
GlcNAc-T IVc
Short name:
GnT-IVc
Short name:
N-acetylglucosaminyltransferase IVc
UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVc
Gene namesi
Name:MGAT4C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:30871. MGAT4C.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2323CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei24 – 4421Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini45 – 478434LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485535.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase CPRO_0000288596Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9UBM8.
PRIDEiQ9UBM8.

PTM databases

PhosphoSiteiQ9UBM8.

Expressioni

Tissue specificityi

Expressed in heart, adrenal gland, testis, liver, brain and fetal brain. Not expressed in pancreas.1 Publication

Gene expression databases

BgeeiQ9UBM8.
CleanExiHS_MGAT4C.
ExpressionAtlasiQ9UBM8. baseline and differential.
GenevestigatoriQ9UBM8.

Organism-specific databases

HPAiHPA016418.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000331664.

Structurei

3D structure databases

ProteinModelPortaliQ9UBM8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 54 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG69242.
GeneTreeiENSGT00550000074578.
HOGENOMiHOG000070065.
HOVERGENiHBG103174.
InParanoidiQ9UBM8.
KOiK13748.
OrthoDBiEOG7F24TD.
PhylomeDBiQ9UBM8.
TreeFamiTF324570.

Family and domain databases

InterProiIPR006759. Glyco_transf_54.
[Graphical view]
PANTHERiPTHR12062. PTHR12062. 1 hit.
PfamiPF04666. Glyco_transf_54. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UBM8-1) [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
MFKFHQMKHI FEILDKMRCL RKRSTVSFLG VLVIFLLFMN LYIEDSYVLE
60 70 80 90 100
GDKQLIRETS THQLNSERYV HTFKDLSNFS GAINVTYRYL AATPLQRKRY
110 120 130 140 150
LTIGLSSVKR KKGNYLLETI KSIFEQSSYE ELKEISVVVH LADFNSSWRD
160 170 180 190 200
AMVQDITQKF AHHIIAGRLM VIHAPEEYYP ILDGLKRNYN DPEDRVKFRS
210 220 230 240 250
KQNVDYAFLL NFCANTSDYY VMLEDDVRCS KNFLTAIKKV IASLEGTYWV
260 270 280 290 300
TLEFSKLGYI GKLYHSHDLP RLAHFLLMFY QEMPCDWLLT HFRGLLAQKN
310 320 330 340 350
VIRFKPSLFQ HMGYYSSYKG TENKLKDDDF EEESFDIPDN PPASLYTNMN
360 370 380 390 400
VFENYEASKA YSSVDEYFWG KPPSTGDVFV IVFENPIIIK KIKVNTGTED
410 420 430 440 450
RQNDILHHGA LDVGENVMPS KQRRQCSTYL RLGEFKNGNF EMSGVNQKIP
460 470
FDIHCMRIYV TKTQKEWLII RSISIWTS
Length:478
Mass (Da):56,061
Last modified:May 18, 2010 - v2
Checksum:i7D09A1BB6B6800C6
GO
Isoform 2 (identifier: Q9UBM8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLGKDMVRFVVRKTVQRSVAKGSRRCKKRM

Note: No experimental confirmation available.

Show »
Length:507
Mass (Da):59,465
Checksum:iA73FDA660E5A71C3
GO

Sequence cautioni

The sequence AAH26068.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti428 – 4281T → S.2 Publications
Corresponds to variant rs17855890 [ dbSNP | Ensembl ].
VAR_032447

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLGKDMVRFVVRKTVQRSVA KGSRRCKKRM in isoform 2. 1 PublicationVSP_056096

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024729 mRNA. Translation: BAA83074.1.
AB024730 mRNA. Translation: BAA83075.1.
AB024911 Genomic DNA. Translation: BAA83087.1.
AK299253 mRNA. Translation: BAG61284.1.
AC010196 Genomic DNA. No translation available.
AC016993 Genomic DNA. No translation available.
AC025157 Genomic DNA. No translation available.
AC079596 Genomic DNA. No translation available.
AC079865 Genomic DNA. No translation available.
AC087887 Genomic DNA. No translation available.
AC093122 Genomic DNA. No translation available.
AC128681 Genomic DNA. No translation available.
AC139663 Genomic DNA. No translation available.
AC139697 Genomic DNA. No translation available.
BC026068 mRNA. Translation: AAH26068.1. Sequence problems.
BC064141 mRNA. Translation: AAH64141.1.
CCDSiCCDS9030.1. [Q9UBM8-1]
RefSeqiNP_037376.2. NM_013244.3. [Q9UBM8-1]
XP_005268833.1. XM_005268776.2. [Q9UBM8-2]
XP_005268834.1. XM_005268777.2. [Q9UBM8-2]
XP_005268836.1. XM_005268779.2. [Q9UBM8-1]
XP_005268838.1. XM_005268781.2. [Q9UBM8-1]
UniGeneiHs.589093.

Genome annotation databases

EnsembliENST00000548651; ENSP00000447253; ENSG00000182050. [Q9UBM8-1]
ENST00000552808; ENSP00000446647; ENSG00000182050. [Q9UBM8-1]
ENST00000611864; ENSP00000481096; ENSG00000182050. [Q9UBM8-1]
ENST00000620241; ENSP00000477650; ENSG00000182050. [Q9UBM8-1]
ENST00000621808; ENSP00000478300; ENSG00000182050. [Q9UBM8-1]
GeneIDi25834.
KEGGihsa:25834.
UCSCiuc001tah.4. human. [Q9UBM8-1]

Polymorphism databases

DMDMi296437368.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024729 mRNA. Translation: BAA83074.1 .
AB024730 mRNA. Translation: BAA83075.1 .
AB024911 Genomic DNA. Translation: BAA83087.1 .
AK299253 mRNA. Translation: BAG61284.1 .
AC010196 Genomic DNA. No translation available.
AC016993 Genomic DNA. No translation available.
AC025157 Genomic DNA. No translation available.
AC079596 Genomic DNA. No translation available.
AC079865 Genomic DNA. No translation available.
AC087887 Genomic DNA. No translation available.
AC093122 Genomic DNA. No translation available.
AC128681 Genomic DNA. No translation available.
AC139663 Genomic DNA. No translation available.
AC139697 Genomic DNA. No translation available.
BC026068 mRNA. Translation: AAH26068.1 . Sequence problems.
BC064141 mRNA. Translation: AAH64141.1 .
CCDSi CCDS9030.1. [Q9UBM8-1 ]
RefSeqi NP_037376.2. NM_013244.3. [Q9UBM8-1 ]
XP_005268833.1. XM_005268776.2. [Q9UBM8-2 ]
XP_005268834.1. XM_005268777.2. [Q9UBM8-2 ]
XP_005268836.1. XM_005268779.2. [Q9UBM8-1 ]
XP_005268838.1. XM_005268781.2. [Q9UBM8-1 ]
UniGenei Hs.589093.

3D structure databases

ProteinModelPortali Q9UBM8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000331664.

Protein family/group databases

CAZyi GT54. Glycosyltransferase Family 54.

PTM databases

PhosphoSitei Q9UBM8.

Polymorphism databases

DMDMi 296437368.

Proteomic databases

PaxDbi Q9UBM8.
PRIDEi Q9UBM8.

Protocols and materials databases

DNASUi 25834.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000548651 ; ENSP00000447253 ; ENSG00000182050 . [Q9UBM8-1 ]
ENST00000552808 ; ENSP00000446647 ; ENSG00000182050 . [Q9UBM8-1 ]
ENST00000611864 ; ENSP00000481096 ; ENSG00000182050 . [Q9UBM8-1 ]
ENST00000620241 ; ENSP00000477650 ; ENSG00000182050 . [Q9UBM8-1 ]
ENST00000621808 ; ENSP00000478300 ; ENSG00000182050 . [Q9UBM8-1 ]
GeneIDi 25834.
KEGGi hsa:25834.
UCSCi uc001tah.4. human. [Q9UBM8-1 ]

Organism-specific databases

CTDi 25834.
GeneCardsi GC12M086372.
H-InvDB HIX0026328.
HGNCi HGNC:30871. MGAT4C.
HPAi HPA016418.
MIMi 607385. gene.
neXtProti NX_Q9UBM8.
PharmGKBi PA143485535.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG69242.
GeneTreei ENSGT00550000074578.
HOGENOMi HOG000070065.
HOVERGENi HBG103174.
InParanoidi Q9UBM8.
KOi K13748.
OrthoDBi EOG7F24TD.
PhylomeDBi Q9UBM8.
TreeFami TF324570.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci MetaCyc:HS00017-MONOMER.
Reactomei REACT_25085. N-Glycan antennae elongation.

Miscellaneous databases

ChiTaRSi MGAT4C. human.
GenomeRNAii 25834.
NextBioi 35474390.
PROi Q9UBM8.
SOURCEi Search...

Gene expression databases

Bgeei Q9UBM8.
CleanExi HS_MGAT4C.
ExpressionAtlasi Q9UBM8. baseline and differential.
Genevestigatori Q9UBM8.

Family and domain databases

InterProi IPR006759. Glyco_transf_54.
[Graphical view ]
PANTHERi PTHR12062. PTHR12062. 1 hit.
Pfami PF04666. Glyco_transf_54. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the human UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IV-homologue (hGnT-IV-H) gene."
    Furukawa T., Youssef E.M., Yatsuoka T., Yokoyama T., Makino N., Inoue H., Fukushige S., Hoshi M., Hayashi Y., Sunamura M., Horii A.
    J. Hum. Genet. 44:397-401(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT SER-428.
  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. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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), VARIANT SER-428.
    Tissue: Testis.
  5. "Molecular cloning and expression of cDNA encoding chicken UDP-N-acetyl-D-glucosamine (GlcNAc): GlcNAcbeta 1-6(GlcNAcbeta 1-2)-manalpha 1-R[GlcNAc to man]beta 1,4N-acetylglucosaminyltransferase VI."
    Sakamoto Y., Taguchi T., Honke K., Korekane H., Watanabe H., Tano Y., Dohmae N., Takio K., Horii A., Taniguchi N.
    J. Biol. Chem. 275:36029-36034(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiMGT4C_HUMAN
AccessioniPrimary (citable) accession number: Q9UBM8
Secondary accession number(s): B4DRH2, Q4G199, Q9UIU5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 106 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 12
    Human chromosome 12: 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