Unreviewed, UniProtKB/TrEMBL Q924B9 (Q924B9_CRIGR)

Names and origin

Protein names

Submitted name:
    Mutant N-acetylglucoaminyltransferase I EMBL AAK61869.1

Gene names

Name:

Mgat1 EMBL AAK61869.1

Organism

Cricetulus griseus (Chinese hamster) EMBL AAK61869.1

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.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

Ontologies

Keywords
Molecular function	Transferase
Gene Ontology (GO)
Biological process	protein amino acid 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)
	Q924B9-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 7236E7ED26BCAD49	FASTA	447	51,760
	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 ENDLEVAPDF 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF343964 mRNA. Translation: AAK61869.1.
3D structure databases
HSSP	HSSP built from PDB template 1FOA based on UniProtKB P27115.
SMR	Q924B9. Positions 106-446.
ModBase	Search...
Protein family/group databases
CAZy	GT13. Glycosyltransferase Family 13.
Phylogenomic databases
HOVERGEN	Q924B9.
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

Q924B9_CRIGR

Accession

Primary (citable) accession number: Q924B9

Entry history

Integrated into UniProtKB/TrEMBL:	December 1, 2001
Last sequence update:	December 1, 2001
Last modified:	April 14, 2009
This is version 20 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)