P29120 (NEC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neuroendocrine convertase 1
Short name=NEC 1
EC=3.4.21.93

Alternative name(s):
Prohormone convertase 1
Proprotein convertase 1
Short name=PC1

Gene names

Name:	PCSK1
Synonyms:	NEC1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	753 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Substrates include POMC, renin, enkephalin, dynorphin, somatostatin and insulin.
Catalytic activity	Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds.
Cofactor	Calcium.
Subcellular location	Cytoplasmic vesicle › secretory vesicle. Note: Localized in the secretion granules.
Post-translational modification	O-glycosylated. Ref.7
Polymorphism	Genetic variations in PCSK1 define the body mass index quantitative trait locus 12 (BMIQ12) [MIM:612362]. Variance in body mass index is a susceptibility factor for obesity.
Involvement in disease	Proprotein convertase 1 deficiency (PC1 deficiency) [MIM:600955]: Characterized by obesity, hypogonadism, hypoadrenalism, reactive hypoglycemia as well as marked small-intestinal absorptive dysfunction It is due to impaired processing of prohormones. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the peptidase S8 family. Furin subfamily.

Ontologies

Keywords
Cellular component	Cytoplasmic vesicle
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Obesity
Domain	Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell-cell signaling Traceable author statement Ref.8. Source: ProtInc energy reserve metabolic process Traceable author statement. Source: Reactome peptide biosynthetic process Inferred from sequence or structural similarity. Source: BHF-UCL peptide hormone processing Traceable author statement. Source: Reactome proteolysis Traceable author statement Ref.8. Source: ProtInc regulation of insulin secretion Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	Golgi apparatus Inferred from Biological aspect of Ancestor. Source: RefGenome extracellular space Inferred from direct assay PubMed 8397508. Source: BHF-UCL secretory granule Traceable author statement. Source: Reactome transport vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	serine-type endopeptidase activity Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P29120-1)

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.

Isoform 2 (identifier: P29120-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-59: MERRAWSLQCTAFVLFCAWCALNSAKAKRQFVNEWAAEIPGGPEAASAIAEELGYDLLG → MGKGSISFLFFS

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Propeptide	28 – 110	83	Potential		PRO_0000027057
	Chain	111 – 753	643	Neuroendocrine convertase 1		PRO_0000027058
Regions
	Region	122 – 410	289	Catalytic
	Region	739 – 751	13	Amphipathic Potential
Sites
	Active site	167	1	Charge relay system By similarity
	Active site	208	1	Charge relay system By similarity
	Active site	382	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	173	1	N-linked (GlcNAc...) Potential
	Glycosylation	401	1	N-linked (GlcNAc...) Potential
	Glycosylation	632	1	O-linked (GalNAc...) Ref.7
	Disulfide bond	225 ↔ 374		By similarity
	Disulfide bond	317 ↔ 347		By similarity
	Disulfide bond	467 ↔ 494		By similarity
Natural variations
	Alternative sequence	1 – 59	59	MERRA…YDLLG → MGKGSISFLFFS in isoform 2.		VSP_046100
	Natural variant	80	1	R → Q. Ref.3 Corresponds to variant rs1799904 [ dbSNP | Ensembl ].		VAR_013906
	Natural variant	213	1	Missing in PC1 deficiency. Ref.11		VAR_022777
	Natural variant	221	1	N → D Associated with susceptibility to obesity; induces a 10.4% reduction of activity (P = 0.03) when compared to the wild-type enzyme. Ref.9 Ref.13 Corresponds to variant rs6232 [ dbSNP | Ensembl ].		VAR_013907
	Natural variant	307	1	S → L in PC1 deficiency; in vitro the mutation markedly impairs the catalytic activity of the enzyme; however intracellular trafficking of this mutant enzyme appears normal; retains some autocatalytic activity even though it is completely inactive on other substrates. Ref.12		VAR_055002
	Natural variant	483	1	G → R in PC1 deficiency; prevents processing of pro-PCSK1 and leads to its retention in the endoplasmic reticulum. Ref.8		VAR_022778
	Natural variant	665	1	Q → E. Ref.3 Ref.9 Ref.12 Corresponds to variant rs6234 [ dbSNP | Ensembl ].		VAR_013908
	Natural variant	690	1	S → T. Ref.9 Ref.12 Corresponds to variant rs6235 [ dbSNP | Ensembl ].		VAR_013909
Experimental info
	Sequence conflict	357	1	S → G in CAA46031. Ref.1
	Sequence conflict	370 – 371	2	LH → VD in BAA11133. Ref.3
	Sequence conflict	617	1	R → G in BAH14073. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: D3CBD1B92093A208	FASTA	753	84,152
	10 20 30 40 50 60 MERRAWSLQC TAFVLFCAWC ALNSAKAKRQ FVNEWAAEIP GGPEAASAIA EELGYDLLGQ 70 80 90 100 110 120 IGSLENHYLF KHKNHPRRSR RSAFHITKRL SDDDRVIWAE QQYEKERSKR SALRDSALNL 130 140 150 160 170 180 FNDPMWNQQW YLQDTRMTAA LPKLDLHVIP VWQKGITGKG VVITVLDDGL EWNHTDIYAN 190 200 210 220 230 240 YDPEASYDFN DNDHDPFPRY DPTNENKHGT RCAGEIAMQA NNHKCGVGVA YNSKVGGIRM 250 260 270 280 290 300 LDGIVTDAIE ASSIGFNPGH VDIYSASWGP NDDGKTVEGP GRLAQKAFEY GVKQGRQGKG 310 320 330 340 350 360 SIFVWASGNG GRQGDNCDCD GYTDSIYTIS ISSASQQGLS PWYAEKCSST LATSYSSGDY 370 380 390 400 410 420 TDQRITSADL HNDCTETHTG TSASAPLAAG IFALALEANP NLTWRDMQHL VVWTSEYDPL 430 440 450 460 470 480 ANNPGWKKNG AGLMVNSRFG FGLLNAKALV DLADPRTWRS VPEKKECVVK DNDFEPRALK 490 500 510 520 530 540 ANGEVIIEIP TRACEGQENA IKSLEHVQFE ATIEYSRRGD LHVTLTSAAG TSTVLLAERE 550 560 570 580 590 600 RDTSPNGFKN WDFMSVHTWG ENPIGTWTLR ITDMSGRIQN EGRIVNWKLI LHGTSSQPEH 610 620 630 640 650 660 MKQPRVYTSY NTVQNDRRGV EKMVDPGEEQ PTQENPKENT LVSKSPSSSS VGGRRDELEE 670 680 690 700 710 720 GAPSQAMLRL LQSAFSKNSP PKQSPKKSPS AKLNIPYENF YEALEKLNKP SQLKDSEDSL 730 740 750 YNDYVDVFYN TKPYKHRDDR LLQALVDILN EEN
	Isoform 2 [UniParc]. Checksum: F082971DADE9EAAC	FASTA	706	79,010
	10 20 30 40 50 60 MGKGSISFLF FSQIGSLENH YLFKHKNHPR RSRRSAFHIT KRLSDDDRVI WAEQQYEKER 70 80 90 100 110 120 SKRSALRDSA LNLFNDPMWN QQWYLQDTRM TAALPKLDLH VIPVWQKGIT GKGVVITVLD 130 140 150 160 170 180 DGLEWNHTDI YANYDPEASY DFNDNDHDPF PRYDPTNENK HGTRCAGEIA MQANNHKCGV 190 200 210 220 230 240 GVAYNSKVGG IRMLDGIVTD AIEASSIGFN PGHVDIYSAS WGPNDDGKTV EGPGRLAQKA 250 260 270 280 290 300 FEYGVKQGRQ GKGSIFVWAS GNGGRQGDNC DCDGYTDSIY TISISSASQQ GLSPWYAEKC 310 320 330 340 350 360 SSTLATSYSS GDYTDQRITS ADLHNDCTET HTGTSASAPL AAGIFALALE ANPNLTWRDM 370 380 390 400 410 420 QHLVVWTSEY DPLANNPGWK KNGAGLMVNS RFGFGLLNAK ALVDLADPRT WRSVPEKKEC 430 440 450 460 470 480 VVKDNDFEPR ALKANGEVII EIPTRACEGQ ENAIKSLEHV QFEATIEYSR RGDLHVTLTS 490 500 510 520 530 540 AAGTSTVLLA ERERDTSPNG FKNWDFMSVH TWGENPIGTW TLRITDMSGR IQNEGRIVNW 550 560 570 580 590 600 KLILHGTSSQ PEHMKQPRVY TSYNTVQNDR RGVEKMVDPG EEQPTQENPK ENTLVSKSPS 610 620 630 640 650 660 SSSVGGRRDE LEEGAPSQAM LRLLQSAFSK NSPPKQSPKK SPSAKLNIPY ENFYEALEKL 670 680 690 700 NKPSQLKDSE DSLYNDYVDV FYNTKPYKHR DDRLLQALVD ILNEEN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression in human lung tumor cells of the proprotein processing enzyme PC1/PC3. Cloning and primary sequence of a 5 kb cDNA." Creemers J.W.M., Roebroek A.J.M., van de Ven W.J.M. FEBS Lett. 300:82-88(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"The cDNA sequence of the human pro-hormone and pro-protein convertase PC1." Seidah N.G., Hamelin J., Gaspar A.M., Day R., Chretien M. DNA Cell Biol. 11:283-289(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Human prohormone convertase 3 gene: exon-intron organization and molecular scanning for mutations in Japanese subjects with NIDDM." Ohagi S., Sakaguchi H., Sanke T., Tatsuta H., Hanabusa T., Nanjo K. Diabetes 45:897-901(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-80 AND GLU-665.
[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] (ISOFORM 2). Tissue: Trachea.
[5]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"Neuroendocrine-specific expression of the human prohormone convertase 1 gene. Hormonal regulation of transcription through distinct cAMP response elements." Jansen E. J. Biol. Chem. 270:15391-15397(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60.
[7]	"LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins." Halim A., Ruetschi U., Larson G., Nilsson J. J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT THR-632, MASS SPECTROMETRY.
[8]	"Obesity and impaired prohormone processing associated with mutations in the human prohormone convertase 1 gene." Jackson R.S., Creemers J.W., Ohagi S., Raffin-Sanson M.-L., Sanders L., Montague C.T., Hutton J.C., O'Rahilly S. Nat. Genet. 16:303-306(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PC1 DEFICIENCY ARG-483.
[9]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ASP-221; GLU-665 AND THR-690.
[10]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
[11]	"Small-intestinal dysfunction accompanies the complex endocrinopathy of human proprotein convertase 1 deficiency." Jackson R.S., Creemers J.W., Farooqi I.S., Raffin-Sanson M.-L., Varro A., Dockray G.J., Holst J.J., Brubaker P.L., Corvol P., Polonsky K.S., Ostrega D., Becker K.L., Bertagna X., Hutton J.C., White A., Dattani M.T., Hussain K., Middleton S.J. , Nicole T.M., Milla P.J., Lindley K.J., O'Rahilly S. J. Clin. Invest. 112:1550-1560(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PC1 DEFICIENCY ALA-213 DEL.
[12]	"Hyperphagia and early-onset obesity due to a novel homozygous missense mutation in prohormone convertase 1/3." Farooqi I.S., Volders K., Stanhope R., Heuschkel R., White A., Lank E., Keogh J., O'Rahilly S., Creemers J.W.M. J. Clin. Endocrinol. Metab. 92:3369-3373(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PC1 DEFICIENCY LEU-307, CHARACTERIZATION OF VARIANT PC1 DEFICIENCY LEU-307, VARIANTS GLU-665 AND THR-690.
[13]	"Common nonsynonymous variants in PCSK1 confer risk of obesity." Benzinou M., Creemers J.W.M., Choquet H., Lobbens S., Dina C., Durand E., Guerardel A., Boutin P., Jouret B., Heude B., Balkau B., Tichet J., Marre M., Potoczna N., Horber F., Le Stunff C., Czernichow S., Sandbaek A. , Lauritzen T., Borch-Johnsen K., Andersen G., Kiess W., Koerner A., Kovacs P., Jacobson P., Carlsson L.M.S., Walley A.J., Joergensen T., Hansen T., Pedersen O., Meyre D., Froguel P. Nat. Genet. 40:943-945(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ASP-221, CHARACTERIZATION OF VARIANT ASP-221, ASSOCIATION WITH SUSCEPTIBILITY TO OBESITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X64810 mRNA. Translation: CAA46031.1. M90753 mRNA. Translation: AAA59918.1. D73407 Genomic DNA. Translation: BAA11133.1. AK303888 mRNA. Translation: BAH14073.1. AC008951 Genomic DNA. No translation available. AC108107 Genomic DNA. No translation available. U24128 Genomic DNA. Translation: AAA73788.1.
IPI	IPI00301961. IPI00967321.
PIR	KXHUC1. S21106.
RefSeq	NP_000430.3. NM_000439.4. NP_001171346.1. NM_001177875.1.
UniGene	Hs.78977.
3D structure databases
ProteinModelPortal	P29120.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000308024.
Protein family/group databases
MEROPS	S08.072.
PTM databases
PhosphoSite	P29120.
Polymorphism databases
DMDM	116242674.
Proteomic databases
PaxDb	P29120.
PRIDE	P29120.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000311106; ENSP00000308024; ENSG00000175426. ENST00000508626; ENSP00000421600; ENSG00000175426.
GeneID	5122.
KEGG	hsa:5122.
UCSC	uc003kls.2. human.
Organism-specific databases
CTD	5122.
GeneCards	GC05M095751.
HGNC	HGNC:8743. PCSK1.
HPA	HPA048564.
MIM	162150. gene. 600955. phenotype. 612362. phenotype.
neXtProt	NX_P29120.
Orphanet	71528. Obesity due to prohormone convertase-I deficiency.
PharmGKB	PA33089.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4935.
HOGENOM	HOG000192536.
HOVERGEN	HBG008705.
InParanoid	P29120.
KO	K01359.
OMA	NNPGWKK.
OrthoDB	EOG4K3KVR.
PhylomeDB	P29120.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
ArrayExpress	P29120.
Bgee	P29120.
CleanEx	HS_PCSK1.
Genevestigator	P29120.
GermOnline	ENSG00000175426. Homo sapiens.
Family and domain databases
Gene3D	3.40.50.200. 1 hit.
InterPro	IPR008979. Galactose-bd-like. IPR000209. Peptidase_S8/S53_dom. IPR023827. Peptidase_S8_Asp-AS. IPR022398. Peptidase_S8_His-AS. IPR023828. Peptidase_S8_Ser-AS. IPR015500. Peptidase_S8_subtilisin-rel. IPR022005. Proho_convert. IPR009020. Prot_inh_propept. IPR002884. PrprotnconvertsP. [Graphical view]
PANTHER	PTHR10795. PTHR10795. 1 hit.
Pfam	PF01483. P_proprotein. 1 hit. PF00082. Peptidase_S8. 1 hit. PF12177. Proho_convert. 1 hit. [Graphical view]
PRINTS	PR00723. SUBTILISIN.
SUPFAM	SSF49785. Gal_bind_like. 1 hit. SSF52743. Pept_S8_S53. 1 hit. SSF54897. Prot_inh_propept. 1 hit.
PROSITE	PS00136. SUBTILASE_ASP. 1 hit. PS00137. SUBTILASE_HIS. 1 hit. PS00138. SUBTILASE_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P29120.
ChEMBL	CHEMBL3182.
ChiTaRS	PCSK1. human.
DrugBank	DB00047. Insulin Glargine recombinant. DB00046. Insulin Lyspro recombinant. DB00030. Insulin recombinant. DB00071. Insulin, porcine.
GenomeRNAi	5122.
NextBio	19750.
PMAP-CutDB	P29120.
SOURCE	Search...

Entry information

Entry name

NEC1_HUMAN

Accession

Primary (citable) accession number: P29120
Secondary accession number(s): B7Z8T7 , E9PHA1, P78478, Q92532

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.