Q924C0 (Q924C0_CRIGR) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
N-acetylglucoaminyltransferase I EMBL AAK61868.1

Gene names

Name:

Mgat1 EMBL AAK61868.1

Organism

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) EMBL AAK61868.1

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

Ontologies

Keywords
Molecular function	Transferase EMBL AAK61868.1
Gene Ontology (GO)
Biological process	protein N-linked glycosylation Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi membrane Inferred from electronic annotation. Source: InterPro
Molecular function	alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q924C0 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: CF803C82B0E5C8DA	FASTA	447	51,761
	10 20 30 40 50 60 MLKKQSAGLV LWGAILFVGW NALLLLFFWT RPAPGRPPSD SAIDDDPASL TREVFRLAED 70 80 90 100 110 120 AEVELERQRG LLQQIREHHA LWRQRWKVPT VAPPAWPRVP ATPSPAVIPI LVIACDRSTV 130 140 150 160 170 180 RRCLDKLLHY RPSAEHFPII VSQDCGHEET AQVIASYGSA VTHIRQPDLS NIAVPPDHRK 190 200 210 220 230 240 FQGYYKIARH YRWALGQIFN KFKFPAAVVV EDDLEVAPDF FEYFQATYPL LRTDPSLWCV 250 260 270 280 290 300 SAWNDNGKEQ MVDSSKPELL YRTDFFPGLG WLLMAELWTE LEPKWPKAFW DDWMRRPEQR 310 320 330 340 350 360 KGRACIRPEI SRTMTFGRKG VSHGQFFDQH LKFIKLNQQF VSFTQLDLSY LQREAYDRDF 370 380 390 400 410 420 LARVYSAPLL QVEKVRTNDQ KELGEVRVQY TSRDSFKAFA KALGVMDDLK SGVPRAGYRG 430 440 VVTFQFRGRR VHLAPPQTWE GYDPSWN

References

[1]	"Independent Lec1A CHO glycosylation mutants arise from point mutations in N-acetylglucosaminyltransferase I that reduce affinity for both substrates. Molecular consequences based on the crystal structure of GlcNAc-TI." Chen W., Unligil U.M., Rini J.M., Stanley P. Biochemistry 40:8765-8772(2001) [PubMed: 11467936] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF343963 mRNA. Translation: AAK61868.1.
RefSeq	NP_001230909.1. NM_001243980.1.
3D structure databases
HSSP	HSSP built from PDB template 1FO8 based on UniProtKB P27115.
ProteinModelPortal	Q924C0.
SMR	Q924C0. Positions 106-446.
ModBase	Search...
Protein family/group databases
CAZy	GT13. Glycosyltransferase Family 13.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100682529.
Phylogenomic databases
HOVERGEN	HBG052466.
Family and domain databases
InterPro	IPR004139. Glyco_trans_13. [Graphical view]
PANTHER	PTHR10468. Glyco_trans_13. 1 hit.
Pfam	PF03071. GNT-I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q924C0_CRIGR

Accession

Primary (citable) accession number: Q924C0

Entry history

Integrated into UniProtKB/TrEMBL:	December 1, 2001
Last sequence update:	December 1, 2001
Last modified:	January 25, 2012
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)