SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9UK23

- NAGPA_HUMAN

UniProt

Q9UK23 - NAGPA_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
Gene
NAGPA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step. Also hydrolyzes UDP-GlcNAc, a sugar donor for Golgi N-acetylglucosaminyltransferases.1 Publication

Catalytic activityi

Glycoprotein N-acetyl-D-glucosaminyl-phospho-D-mannose + H2O = N-acetyl-D-glucosamine + glycoprotein phospho-D-mannose.

Pathwayi

GO - Molecular functioni

  1. N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase activity Source: ProtInc

GO - Biological processi

  1. carbohydrate metabolic process Source: ProtInc
  2. cellular protein modification process Source: ProtInc
  3. lysosome organization Source: ProtInc
  4. protein glycosylation Source: UniProtKB-UniPathway
  5. protein targeting to lysosome Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase (EC:3.1.4.45)
Alternative name(s):
Mannose 6-phosphate-uncovering enzyme
Phosphodiester alpha-GlcNAcase
Gene namesi
Name:NAGPA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:17378. NAGPA.

Subcellular locationi

Golgi apparatusGolgi stack membrane; Single-pass type I membrane protein. Golgi apparatustrans-Golgi network
Note: Cis/medial Golgi.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini50 – 448399Lumenal Reviewed prediction
Add
BLAST
Transmembranei449 – 46921Helical; Reviewed prediction
Add
BLAST
Topological domaini470 – 51546Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi cisterna membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi51 – 511C → M: 65% of wild-type of activity. 1 Publication
Mutagenesisi115 – 1151C → S: 15% of wild-type of activity, and almost no traffic to Golgi. 1 Publication
Mutagenesisi132 – 1321C → V: No traffic to Golgi. 1 Publication
Mutagenesisi137 – 1371N → A: 11% of wild-type of activity. 1 Publication
Mutagenesisi221 – 2211C → L: 10% of wild-type of activity; when associated with M-51. 1 Publication
Mutagenesisi225 – 2251Q → H: 6% of wild-type of activity. 1 Publication
Mutagenesisi227 – 2271T → R: Complete loss of activity. 1 Publication
Mutagenesisi247 – 2471R → A: 87% of wild-type of activity. 1 Publication
Mutagenesisi284 – 2841N → A: 22% of wild-type of activity. 1 Publication
Mutagenesisi286 – 2861D → A: Complete loss of activity. 1 Publication
Mutagenesisi287 – 2871G → A: 16% of wild-type of activity. 1 Publication
Mutagenesisi288 – 2881G → A: Complete loss of activity. 1 Publication
Mutagenesisi289 – 2891G → A: Complete loss of activity. 1 Publication
Mutagenesisi290 – 2901S → A: Complete loss of activity. 1 Publication
Mutagenesisi320 – 3201T → A: 43% of wild-type of activity. 1 Publication
Mutagenesisi322 – 3221V → A: 67% of wild-type of activity. 1 Publication

Organism-specific databases

PharmGKBiPA134940049.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25251 Publication
Add
BLAST
Propeptidei26 – 4924Removed in mature form
PRO_0000424659Add
BLAST
Chaini50 – 515466N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
PRO_0000021788Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi115 ↔ 148 Inferred
Disulfide bondi132 ↔ 3231 Publication
Glycosylationi208 – 2081N-linked (GlcNAc...) Reviewed prediction
Glycosylationi214 – 2141N-linked (GlcNAc...) Reviewed prediction
Glycosylationi296 – 2961N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi307 ↔ 314 Inferred
Disulfide bondi362 ↔ 373 By similarity
Glycosylationi366 – 3661N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi380 ↔ 389 By similarity
Glycosylationi388 – 3881N-linked (GlcNAc...) Reviewed prediction
Glycosylationi420 – 4201N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

The precursor is cleaved and activated in the trans-Golgi network by a furin endopeptidase.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ9UK23.
PaxDbiQ9UK23.
PRIDEiQ9UK23.

PTM databases

PhosphoSiteiQ9UK23.

Expressioni

Tissue specificityi

Isoform 2 may be brain-specific.

Gene expression databases

ArrayExpressiQ9UK23.
BgeeiQ9UK23.
CleanExiHS_NAGPA.
GenevestigatoriQ9UK23.

Interactioni

Subunit structurei

Homotetramer arranged as two disulfide-linked homodimers By similarity.1 Publication

Protein-protein interaction databases

BioGridi119351. 4 interactions.
IntActiQ9UK23. 2 interactions.
STRINGi9606.ENSP00000310998.

Structurei

3D structure databases

ProteinModelPortaliQ9UK23.
SMRiQ9UK23. Positions 314-434.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini358 – 39033EGF-like
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi488 – 4914Tyrosine-based internalization motif
Motifi511 – 5155NPF internalization motif

Domaini

The tyrosine-based internalization signal may be essential for its retrieval from the plasma membrane to the TGN.
The C-terminal NPFKD sequence is an attractive candidate for either an endocytosis signal acting at the plasma membrane or a retrieval signal acting at the TGN to return the enzyme to the cis/medial-Golgi.

Sequence similaritiesi

Contains 1 EGF-like domain.

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG126864.
HOGENOMiHOG000059612.
HOVERGENiHBG052571.
InParanoidiQ9UK23.
KOiK01125.
OMAiPSDHCQD.
OrthoDBiEOG7R2BJP.
PhylomeDBiQ9UK23.
TreeFamiTF331920.

Family and domain databases

InterProiIPR018711. DUF2233.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
[Graphical view]
PfamiPF09992. DUF2233. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UK23-1) [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

MATSTGRWLL LRLALFGFLW EASGGLDSGA SRDDDLLLPY PRARARLPRD    50
CTRVRAGNRE HESWPPPPAT PGAGGLAVRT FVSHFRDRAV AGHLTRAVEP 100
LRTFSVLEPG GPGGCAARRR ATVEETARAA DCRVAQNGGF FRMNSGECLG 150
NVVSDERRVS SSGGLQNAQF GIRRDGTLVT GYLSEEEVLD TENPFVQLLS 200
GVVWLIRNGS IYINESQATE CDETQETGSF SKFVNVISAR TAIGHDRKGQ 250
LVLFHADGQT EQRGINLWEM AEFLLKQDVV NAINLDGGGS ATFVLNGTLA 300
SYPSDHCQDN MWRCPRQVST VVCVHEPRCQ PPDCHGHGTC VDGHCQCTGH 350
FWRGPGCDEL DCGPSNCSQH GLCTETGCRC DAGWTGSNCS EECPLGWHGP 400
GCQRPCKCEH HCPCDPKTGN CSVSRVKQCL QPPEATLRAG ELSFFTRTAW 450
LALTLALAFL LLISTAANLS LLLSRAERNR RLHGDYAYHP LQEMNGEPLA 500
AEKEQPGGAH NPFKD 515
Length:515
Mass (Da):56,073
Last modified:May 18, 2010 - v2
Checksum:i9B80335E7F9DBAA9
GO
Isoform 2 (identifier: Q9UK23-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     392-425: Missing.

Show »
Length:481
Mass (Da):52,368
Checksum:i2FC910C7DB777505
GO
Isoform 3 (identifier: Q9UK23-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     307-309: CQD → WQA
     310-515: Missing.

Show »
Length:309
Mass (Da):33,577
Checksum:i270763749113C946
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti465 – 4651T → I.1 Publication
Corresponds to variant rs7188856 [ dbSNP | Ensembl ].
VAR_020609

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei307 – 3093CQD → WQA in isoform 3.
VSP_012267
Alternative sequencei310 – 515206Missing in isoform 3.
VSP_012268Add
BLAST
Alternative sequencei392 – 42534Missing in isoform 2.
VSP_012269Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti259 – 2591Q → H in AAF08273. 1 Publication
Sequence conflicti405 – 4051P → R in AAF08273. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF187072 mRNA. Translation: AAF08273.1.
AK127952 mRNA. Translation: BAG54605.1.
AK314320 mRNA. Translation: BAG36968.1.
AC026458 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85245.1.
BC012194 mRNA. Translation: AAH12194.1.
CCDSiCCDS10527.1. [Q9UK23-1]
RefSeqiNP_057340.2. NM_016256.3. [Q9UK23-1]
UniGeneiHs.21334.

Genome annotation databases

EnsembliENST00000312251; ENSP00000310998; ENSG00000103174. [Q9UK23-1]
ENST00000381955; ENSP00000371381; ENSG00000103174. [Q9UK23-2]
ENST00000562746; ENSP00000455900; ENSG00000103174. [Q9UK23-3]
GeneIDi51172.
KEGGihsa:51172.
UCSCiuc002cyg.3. human. [Q9UK23-1]

Polymorphism databases

DMDMi296439239.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF187072 mRNA. Translation: AAF08273.1 .
AK127952 mRNA. Translation: BAG54605.1 .
AK314320 mRNA. Translation: BAG36968.1 .
AC026458 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85245.1 .
BC012194 mRNA. Translation: AAH12194.1 .
CCDSi CCDS10527.1. [Q9UK23-1 ]
RefSeqi NP_057340.2. NM_016256.3. [Q9UK23-1 ]
UniGenei Hs.21334.

3D structure databases

ProteinModelPortali Q9UK23.
SMRi Q9UK23. Positions 314-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119351. 4 interactions.
IntActi Q9UK23. 2 interactions.
STRINGi 9606.ENSP00000310998.

Chemistry

ChEMBLi CHEMBL5920.
DrugBanki DB00141. N-Acetyl-D-glucosamine.

PTM databases

PhosphoSitei Q9UK23.

Polymorphism databases

DMDMi 296439239.

Proteomic databases

MaxQBi Q9UK23.
PaxDbi Q9UK23.
PRIDEi Q9UK23.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000312251 ; ENSP00000310998 ; ENSG00000103174 . [Q9UK23-1 ]
ENST00000381955 ; ENSP00000371381 ; ENSG00000103174 . [Q9UK23-2 ]
ENST00000562746 ; ENSP00000455900 ; ENSG00000103174 . [Q9UK23-3 ]
GeneIDi 51172.
KEGGi hsa:51172.
UCSCi uc002cyg.3. human. [Q9UK23-1 ]

Organism-specific databases

CTDi 51172.
GeneCardsi GC16M005014.
H-InvDB HIX0013112.
HGNCi HGNC:17378. NAGPA.
MIMi 607985. gene.
neXtProti NX_Q9UK23.
PharmGKBi PA134940049.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG126864.
HOGENOMi HOG000059612.
HOVERGENi HBG052571.
InParanoidi Q9UK23.
KOi K01125.
OMAi PSDHCQD.
OrthoDBi EOG7R2BJP.
PhylomeDBi Q9UK23.
TreeFami TF331920.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Miscellaneous databases

GeneWikii NAGPA.
GenomeRNAii 51172.
NextBioi 54121.
PROi Q9UK23.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UK23.
Bgeei Q9UK23.
CleanExi HS_NAGPA.
Genevestigatori Q9UK23.

Family and domain databases

InterProi IPR018711. DUF2233.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
[Graphical view ]
Pfami PF09992. DUF2233. 1 hit.
[Graphical view ]
SMARTi SM00181. EGF. 1 hit.
[Graphical view ]
PROSITEi PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional expression of two splice forms of human N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase."
    Kornfeld R.H., Bao M., Brewer K., Noll C., Canfield W.M.
    J. Biol. Chem. 274:32778-32785(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT ILE-465.
  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 1).
    Tissue: Mammary gland and Tongue.
  3. "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].
  4. 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 3).
    Tissue: Colon.
  6. "Human mannose 6-phosphate-uncovering enzyme is synthesized as a proenzyme that is activated by the endoprotease furin."
    Do H., Lee W.S., Ghosh P., Hollowell T., Canfield W., Kornfeld S.
    J. Biol. Chem. 277:29737-29744(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-36, SIGNAL SEQUENCE CLEAVAGE SITE, PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION.
  7. "Structure and function of the DUF2233 domain in bacteria and in the human mannose 6-phosphate uncovering enzyme."
    Das D., Lee W.S., Grant J.C., Chiu H.J., Farr C.L., Vance J., Klock H.E., Knuth M.W., Miller M.D., Elsliger M.A., Deacon A.M., Godzik A., Lesley S.A., Kornfeld S., Wilson I.A.
    J. Biol. Chem. 288:16789-16799(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-51; CYS-115; CYS-132; ASN-137; CYS-221; GLN-225; THR-227; ARG-247; ASN-284; ASP-286; GLY-287; GLY-288; GLY-289; SER-290; THR-320 AND VAL-322, 3D-STRUCTURE MODELING, DISULFIDE BONDS, FUNCTION.

Entry informationi

Entry nameiNAGPA_HUMAN
AccessioniPrimary (citable) accession number: Q9UK23
Secondary accession number(s): B2RAS1, Q96EJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 117 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, Direct protein sequencing, 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

Similar proteinsi