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Protein

Glia-derived nexin

Gene

SERPINE2

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

Functioni

Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei365 – 3662Reactive bondSequence Analysis

GO - Molecular functioni

  1. glycosaminoglycan binding Source: BHF-UCL
  2. heparin binding Source: BHF-UCL
  3. receptor binding Source: BHF-UCL
  4. serine-type endopeptidase inhibitor activity Source: BHF-UCL

GO - Biological processi

  1. blood coagulation Source: Ensembl
  2. cerebellar granular layer morphogenesis Source: Ensembl
  3. detection of mechanical stimulus involved in sensory perception Source: Ensembl
  4. innervation Source: Ensembl
  5. long-term synaptic potentiation Source: Ensembl
  6. mating plug formation Source: Ensembl
  7. negative regulation of blood coagulation Source: BHF-UCL
  8. negative regulation of cell growth Source: Ensembl
  9. negative regulation of cell proliferation Source: Ensembl
  10. negative regulation of endopeptidase activity Source: GO_Central
  11. negative regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  12. negative regulation of plasminogen activation Source: BHF-UCL
  13. negative regulation of platelet aggregation Source: BHF-UCL
  14. negative regulation of protein catabolic process Source: Ensembl
  15. negative regulation of protein processing Source: BHF-UCL
  16. negative regulation of proteolysis Source: BHF-UCL
  17. negative regulation of smoothened signaling pathway Source: Ensembl
  18. negative regulation of sodium ion transport Source: Ensembl
  19. positive regulation of astrocyte differentiation Source: BHF-UCL
  20. regulation of cell migration Source: UniProtKB
  21. regulation of synaptic transmission, glutamatergic Source: Ensembl
  22. regulation of timing of cell differentiation Source: Ensembl
  23. secretion by cell Source: Ensembl
  24. secretory granule organization Source: Ensembl
  25. seminal vesicle epithelium development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Protease inhibitor, Serine protease inhibitor

Keywords - Biological processi

Differentiation, Neurogenesis

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_1439. Common Pathway.
REACT_326. Intrinsic Pathway.
REACT_641. Dissolution of Fibrin Clot.

Protein family/group databases

MEROPSiI04.021.

Names & Taxonomyi

Protein namesi
Recommended name:
Glia-derived nexin
Short name:
GDN
Alternative name(s):
Peptidase inhibitor 7
Short name:
PI-7
Protease nexin 1
Short name:
PN-1
Protease nexin I
Serpin E2
Gene namesi
Name:SERPINE2
Synonyms:PI7, PN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:8951. SERPINE2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: BHF-UCL
  2. extracellular matrix Source: BHF-UCL
  3. extracellular region Source: BHF-UCL
  4. extracellular space Source: GO_Central
  5. extrinsic component of external side of plasma membrane Source: BHF-UCL
  6. neuromuscular junction Source: BHF-UCL
  7. platelet alpha granule Source: BHF-UCL
  8. vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA269.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19192 PublicationsAdd
BLAST
Chaini20 – 398379Glia-derived nexinPRO_0000032504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi159 – 1591N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiP07093.
PaxDbiP07093.
PeptideAtlasiP07093.
PRIDEiP07093.

PTM databases

PhosphoSiteiP07093.

Miscellaneous databases

PMAP-CutDBP07093.

Expressioni

Gene expression databases

BgeeiP07093.
CleanExiHS_SERPINE2.
ExpressionAtlasiP07093. baseline and differential.
GenevestigatoriP07093.

Organism-specific databases

HPAiHPA051263.

Interactioni

Protein-protein interaction databases

BioGridi111288. 13 interactions.
STRINGi9606.ENSP00000415786.

Structurei

Secondary structure

1
398
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 4522Combined sources
Beta strandi51 – 533Combined sources
Helixi55 – 6612Combined sources
Helixi71 – 8111Combined sources
Turni86 – 883Combined sources
Helixi89 – 10012Combined sources
Helixi102 – 1043Combined sources
Beta strandi109 – 1179Combined sources
Helixi124 – 13411Combined sources
Beta strandi136 – 1405Combined sources
Helixi146 – 16015Combined sources
Turni161 – 1633Combined sources
Helixi171 – 1733Combined sources
Turni176 – 1783Combined sources
Beta strandi181 – 1899Combined sources
Beta strandi193 – 1953Combined sources
Helixi199 – 2013Combined sources
Beta strandi203 – 2086Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi214 – 23219Combined sources
Beta strandi238 – 2469Combined sources
Beta strandi249 – 26012Combined sources
Helixi265 – 2673Combined sources
Helixi269 – 2713Combined sources
Helixi274 – 2818Combined sources
Beta strandi285 – 29410Combined sources
Beta strandi296 – 3038Combined sources
Helixi305 – 3106Combined sources
Helixi315 – 3173Combined sources
Turni319 – 3213Combined sources
Turni325 – 3273Combined sources
Beta strandi328 – 3303Combined sources
Beta strandi338 – 34710Combined sources
Beta strandi354 – 3563Combined sources
Helixi357 – 3604Combined sources
Beta strandi370 – 3723Combined sources
Beta strandi377 – 3837Combined sources
Turni384 – 3874Combined sources
Beta strandi388 – 3969Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DY0X-ray2.35A/B20-398[»]
4DY7X-ray2.80C/F20-398[»]
ProteinModelPortaliP07093.
SMRiP07093. Positions 21-398.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238519.
HOVERGENiHBG106493.
InParanoidiP07093.
KOiK16643.
OMAiIQVFNQI.
OrthoDBiEOG7327PB.
PhylomeDBiP07093.
TreeFamiTF352620.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 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: P07093-1) [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
MNWHLPLFLL ASVTLPSICS HFNPLSLEEL GSNTGIQVFN QIVKSRPHDN
60 70 80 90 100
IVISPHGIAS VLGMLQLGAD GRTKKQLAMV MRYGVNGVGK ILKKINKAIV
110 120 130 140 150
SKKNKDIVTV ANAVFVKNAS EIEVPFVTRN KDVFQCEVRN VNFEDPASAC
160 170 180 190 200
DSINAWVKNE TRDMIDNLLS PDLIDGVLTR LVLVNAVYFK GLWKSRFQPE
210 220 230 240 250
NTKKRTFVAA DGKSYQVPML AQLSVFRCGS TSAPNDLWYN FIELPYHGES
260 270 280 290 300
ISMLIALPTE SSTPLSAIIP HISTKTIDSW MSIMVPKRVQ VILPKFTAVA
310 320 330 340 350
QTDLKEPLKV LGITDMFDSS KANFAKITTG SENLHVSHIL QKAKIEVSED
360 370 380 390
GTKASAATTA ILIARSSPPW FIVDRPFLFF IRHNPTGAVL FMGQINKP
Length:398
Mass (Da):44,002
Last modified:April 1, 1988 - v1
Checksum:i2A165604E2CBE6B8
GO
Isoform 2 (identifier: P07093-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-330: TG → R

Show »
Length:397
Mass (Da):44,000
Checksum:i45A9C934A800D7EB
GO
Isoform 3 (identifier: P07093-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSDCRSSLVEGTM
     329-330: TG → R

Note: No experimental confirmation available.

Show »
Length:409
Mass (Da):45,267
Checksum:i6315691891B53A7B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591N → D in BAG35401. (PubMed:14702039)Curated
Sequence conflicti261 – 2611S → E(PubMed:2877744)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511I → M.
Corresponds to variant rs3795875 [ dbSNP | Ensembl ].
VAR_051955
Natural varianti204 – 2041K → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_036027

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MSDCRSSLVEGTM in isoform 3. 1 PublicationVSP_043668
Alternative sequencei329 – 3302TG → R in isoform 2 and isoform 3. 3 PublicationsVSP_038367

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17783 mRNA. Translation: AAA35883.1.
AK295564 mRNA. Translation: BAG58464.1.
AK312499 mRNA. Translation: BAG35401.1.
AC073641 Genomic DNA. Translation: AAY14926.1.
CH471063 Genomic DNA. Translation: EAW70821.1.
CH471063 Genomic DNA. Translation: EAW70823.1.
BC015663 mRNA. Translation: AAH15663.1.
BC042628 mRNA. Translation: AAH42628.1.
CCDSiCCDS2460.1. [P07093-1]
CCDS46525.1. [P07093-3]
CCDS46526.1. [P07093-2]
PIRiA37274.
RefSeqiNP_001130000.1. NM_001136528.1. [P07093-2]
NP_001130002.1. NM_001136530.1. [P07093-3]
NP_006207.1. NM_006216.3. [P07093-1]
XP_005246699.1. XM_005246642.1. [P07093-1]
UniGeneiHs.38449.
Hs.708453.

Genome annotation databases

EnsembliENST00000258405; ENSP00000258405; ENSG00000135919. [P07093-1]
ENST00000409304; ENSP00000386412; ENSG00000135919. [P07093-2]
ENST00000409840; ENSP00000386969; ENSG00000135919. [P07093-2]
ENST00000447280; ENSP00000415786; ENSG00000135919. [P07093-3]
GeneIDi5270.
KEGGihsa:5270.
UCSCiuc002vnu.2. human. [P07093-1]
uc002vnv.2. human. [P07093-2]
uc010zlr.1. human. [P07093-3]

Polymorphism databases

DMDMi121110.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17783 mRNA. Translation: AAA35883.1.
AK295564 mRNA. Translation: BAG58464.1.
AK312499 mRNA. Translation: BAG35401.1.
AC073641 Genomic DNA. Translation: AAY14926.1.
CH471063 Genomic DNA. Translation: EAW70821.1.
CH471063 Genomic DNA. Translation: EAW70823.1.
BC015663 mRNA. Translation: AAH15663.1.
BC042628 mRNA. Translation: AAH42628.1.
CCDSiCCDS2460.1. [P07093-1]
CCDS46525.1. [P07093-3]
CCDS46526.1. [P07093-2]
PIRiA37274.
RefSeqiNP_001130000.1. NM_001136528.1. [P07093-2]
NP_001130002.1. NM_001136530.1. [P07093-3]
NP_006207.1. NM_006216.3. [P07093-1]
XP_005246699.1. XM_005246642.1. [P07093-1]
UniGeneiHs.38449.
Hs.708453.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DY0X-ray2.35A/B20-398[»]
4DY7X-ray2.80C/F20-398[»]
ProteinModelPortaliP07093.
SMRiP07093. Positions 21-398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111288. 13 interactions.
STRINGi9606.ENSP00000415786.

Protein family/group databases

MEROPSiI04.021.

PTM databases

PhosphoSiteiP07093.

Polymorphism databases

DMDMi121110.

Proteomic databases

MaxQBiP07093.
PaxDbiP07093.
PeptideAtlasiP07093.
PRIDEiP07093.

Protocols and materials databases

DNASUi5270.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258405; ENSP00000258405; ENSG00000135919. [P07093-1]
ENST00000409304; ENSP00000386412; ENSG00000135919. [P07093-2]
ENST00000409840; ENSP00000386969; ENSG00000135919. [P07093-2]
ENST00000447280; ENSP00000415786; ENSG00000135919. [P07093-3]
GeneIDi5270.
KEGGihsa:5270.
UCSCiuc002vnu.2. human. [P07093-1]
uc002vnv.2. human. [P07093-2]
uc010zlr.1. human. [P07093-3]

Organism-specific databases

CTDi5270.
GeneCardsiGC02M224839.
HGNCiHGNC:8951. SERPINE2.
HPAiHPA051263.
MIMi177010. gene.
neXtProtiNX_P07093.
PharmGKBiPA269.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4826.
GeneTreeiENSGT00760000118839.
HOGENOMiHOG000238519.
HOVERGENiHBG106493.
InParanoidiP07093.
KOiK16643.
OMAiIQVFNQI.
OrthoDBiEOG7327PB.
PhylomeDBiP07093.
TreeFamiTF352620.

Enzyme and pathway databases

ReactomeiREACT_1439. Common Pathway.
REACT_326. Intrinsic Pathway.
REACT_641. Dissolution of Fibrin Clot.

Miscellaneous databases

ChiTaRSiSERPINE2. human.
GeneWikiiSERPINE2.
GenomeRNAii5270.
NextBioi20360.
PMAP-CutDBP07093.
PROiP07093.
SOURCEiSearch...

Gene expression databases

BgeeiP07093.
CleanExiHS_SERPINE2.
ExpressionAtlasiP07093. baseline and differential.
GenevestigatoriP07093.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence coding for a rat glia-derived nexin and its homology to members of the serpin superfamily."
    Sommer J., Gloor S.M., Rovelli G.F., Hofsteenge J., Nick H., Meier R., Monard D.
    Biochemistry 26:6407-6410(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "A glia-derived neurite promoting factor with protease inhibitory activity belongs to the protease nexins."
    Gloor S.M., Odink K., Guenther J., Nick H., Monard D.
    Cell 47:687-693(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Molecular cloning and expression of two forms of human protease nexin I."
    McGrogan M., Kennedy J., Li M.P., Hsu C., Scott R.W., Simonsen C.C., Baker J.B.
    Biotechnology (N.Y.) 6:172-177(1988)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "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] (ISOFORMS 1 AND 3).
    Tissue: Hippocampus and Thalamus.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORMS 1 AND 2).
    Tissue: Skin and Testis.
  8. "Protease nexin. Properties and a modified purification procedure."
    Scott R.W., Bergman B.L., Bajpai A., Hersh R.T., Rodriguez H., Jones B.N., Barreda C., Watts S., Baker J.B.
    J. Biol. Chem. 260:7029-7034(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-47, CHARACTERIZATION.
  9. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-34.
  10. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-204.

Entry informationi

Entry nameiGDN_HUMAN
AccessioniPrimary (citable) accession number: P07093
Secondary accession number(s): B2R6A4
, B4DIF2, Q53S15, Q5D0C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: February 4, 2015
This is version 154 of the entry and version 1 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.