Skip Header

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

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1

Gene

PLCG1

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

Functioni

Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration.1 Publication

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.

Cofactori

Enzyme regulationi

Activated by phosphorylation on tyrosine residues.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei335PROSITE-ProRule annotation1
Active sitei380PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi165 – 176PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • glutamate receptor binding Source: Ensembl
  • neurotrophin TRKA receptor binding Source: UniProtKB
  • phosphatidylinositol phospholipase C activity Source: UniProtKB
  • phospholipase C activity Source: Reactome
  • protein kinase binding Source: BHF-UCL
  • receptor tyrosine kinase binding Source: Ensembl
  • signal transducer activity, downstream of receptor Source: UniProtKB

GO - Biological processi

  • activation of MAPKK activity Source: Reactome
  • axon guidance Source: Reactome
  • calcium-mediated signaling Source: BHF-UCL
  • cell migration Source: BHF-UCL
  • cellular response to epidermal growth factor stimulus Source: UniProtKB
  • epidermal growth factor receptor signaling pathway Source: BHF-UCL
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • inositol phosphate metabolic process Source: Reactome
  • in utero embryonic development Source: Ensembl
  • leukocyte migration Source: Reactome
  • phospholipid catabolic process Source: InterPro
  • positive regulation of angiogenesis Source: DFLAT
  • positive regulation of blood vessel endothelial cell migration Source: DFLAT
  • positive regulation of epithelial cell migration Source: UniProtKB
  • positive regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
  • signal transduction Source: Reactome
  • T cell receptor signaling pathway Source: Reactome
  • viral process Source: UniProtKB-KW

Keywordsi

Molecular functionHydrolase, Transducer
Biological processHost-virus interaction, Lipid degradation, Lipid metabolism
LigandCalcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.4.11. 2681.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-1236382. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
R-HSA-1251932. PLCG1 events in ERBB2 signaling.
R-HSA-1489509. DAG and IP3 signaling.
R-HSA-167021. PLC-gamma1 signalling.
R-HSA-170968. Frs2-mediated activation.
R-HSA-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-HSA-186763. Downstream signal transduction.
R-HSA-202433. Generation of second messenger molecules.
R-HSA-2029485. Role of phospholipids in phagocytosis.
R-HSA-210990. PECAM1 interactions.
R-HSA-212718. EGFR interacts with phospholipase C-gamma.
R-HSA-2424491. DAP12 signaling.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-2871809. FCERI mediated Ca+2 mobilization.
R-HSA-418890. Role of second messengers in netrin-1 signaling.
R-HSA-5218921. VEGFR2 mediated cell proliferation.
R-HSA-5637810. Constitutive Signaling by EGFRvIII.
R-HSA-5654219. Phospholipase C-mediated cascade: FGFR1.
R-HSA-5654221. Phospholipase C-mediated cascade, FGFR2.
R-HSA-5654227. Phospholipase C-mediated cascade, FGFR3.
R-HSA-5654228. Phospholipase C-mediated cascade, FGFR4.
R-HSA-5655253. Signaling by FGFR2 in disease.
R-HSA-5655291. Signaling by FGFR4 in disease.
R-HSA-5655302. Signaling by FGFR1 in disease.
R-HSA-8853338. Signaling by FGFR3 point mutants in cancer.
R-HSA-8853659. RET signaling.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiP19174.
SIGNORiP19174.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC:3.1.4.11)
Alternative name(s):
PLC-148
Phosphoinositide phospholipase C-gamma-1
Phospholipase C-II
Short name:
PLC-II
Phospholipase C-gamma-1
Short name:
PLC-gamma-1
Gene namesi
Name:PLCG1
Synonyms:PLC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:9065. PLCG1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: Ensembl
  • cell projection Source: BHF-UCL
  • COP9 signalosome Source: UniProtKB
  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • ruffle Source: UniProtKB

Keywords - Cellular componenti

Cell projection

Pathology & Biotechi

Organism-specific databases

DisGeNETi5335.
OpenTargetsiENSG00000124181.
PharmGKBiPA33392.

Chemistry databases

ChEMBLiCHEMBL3964.

Polymorphism and mutation databases

BioMutaiPLCG1.
DMDMi130225.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000884982 – 12901-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1Add BLAST1289

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei506PhosphotyrosineBy similarity1
Modified residuei771Phosphotyrosine; by SYKCombined sources2 Publications1
Modified residuei775PhosphotyrosineCombined sources1
Modified residuei783Phosphotyrosine; by ITK, SYK and TXKCombined sources3 Publications1
Modified residuei977PhosphotyrosineBy similarity1
Modified residuei1221PhosphoserineCombined sources1
Modified residuei1227PhosphoserineCombined sources1
Modified residuei1233PhosphoserineCombined sources1
Modified residuei1248Phosphoserine1 Publication1
Modified residuei1253PhosphotyrosineCombined sources1
Modified residuei1263PhosphoserineCombined sources1
Isoform 2 (identifier: P19174-2)
Modified residuei1222PhosphoserineCombined sources1

Post-translational modificationi

Tyrosine phosphorylated in response to signaling via activated FLT3, KIT and PDGFRA (By similarity). Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated by activated FLT1 and KDR. Tyrosine phosphorylated by activated PDGFRB. The receptor-mediated activation of PLCG1 involves its phosphorylation by tyrosine kinases, in response to ligation of a variety of growth factor receptors and immune system receptors. For instance, SYK phosphorylates and activates PLCG1 in response to ligation of the B-cell receptor. May be dephosphorylated by PTPRJ. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells.By similarity11 Publications
Ubiquitinated by CBLB in activated T-cells.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP19174.
MaxQBiP19174.
PaxDbiP19174.
PeptideAtlasiP19174.
PRIDEiP19174.

PTM databases

iPTMnetiP19174.
PhosphoSitePlusiP19174.

Expressioni

Gene expression databases

BgeeiENSG00000124181.
CleanExiHS_PLCG1.
ExpressionAtlasiP19174. baseline and differential.
GenevisibleiP19174. HS.

Organism-specific databases

HPAiCAB004277.
HPA036681.
HPA036682.

Interactioni

Subunit structurei

Interacts with AGAP2 via its SH3 domain. Interacts (via SH2 domain) with RET. Interacts with FLT1 (tyrosine-phosphorylated) (By similarity). Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts with LAT (phosphorylated) upon TCR activation. Interacts (via SH3 domain) with the Pro-rich domain of TNK1. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB in activated T-cells; which inhibits phosphorylation. Interacts with SHB. Interacts (via SH3 domain) with the Arg/Gly-rich-flanked Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively regulated by arginine methylation of KHDRBS1/SAM68. Interacts with INPP5D/SHIP1, THEMIS and CLNK (By similarity). Interacts with AXL, FLT4 and KIT. Interacts with RALGPS1. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts (via SH2 domain) with PDGFRA and PDGFRB (tyrosine phosphorylated). Interacts with PIP5K1C (By similarity). Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding). Interacts with SYK; activates PLCG1. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes (By similarity). Interacts with TESPA1; the association is increased with prolonged stimulation of the TCR and may facilitate the assembly of the LAT signalosome.By similarity20 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • glutamate receptor binding Source: Ensembl
  • neurotrophin TRKA receptor binding Source: UniProtKB
  • protein kinase binding Source: BHF-UCL
  • receptor tyrosine kinase binding Source: Ensembl

Protein-protein interaction databases

BioGridi111351. 124 interactors.
DIPiDIP-100N.
IntActiP19174. 114 interactors.
MINTiMINT-102915.
STRINGi9606.ENSP00000244007.

Chemistry databases

BindingDBiP19174.

Structurei

Secondary structure

11290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi551 – 554Combined sources4
Beta strandi556 – 558Combined sources3
Helixi561 – 576Combined sources16
Beta strandi583 – 587Combined sources5
Beta strandi589 – 591Combined sources3
Beta strandi595 – 601Combined sources7
Beta strandi604 – 613Combined sources10
Helixi615 – 617Combined sources3
Beta strandi620 – 624Combined sources5
Beta strandi627 – 631Combined sources5
Helixi632 – 641Combined sources10
Beta strandi644 – 646Combined sources3
Beta strandi649 – 651Combined sources3
Helixi662 – 665Combined sources4
Beta strandi669 – 672Combined sources4
Helixi675 – 683Combined sources9
Beta strandi690 – 695Combined sources6
Beta strandi701 – 708Combined sources8
Beta strandi711 – 720Combined sources10
Beta strandi723 – 726Combined sources4
Beta strandi729 – 732Combined sources4
Helixi734 – 743Combined sources10
Helixi758 – 763Combined sources6
Beta strandi792 – 794Combined sources3
Beta strandi805 – 809Combined sources5
Beta strandi817 – 820Combined sources4
Turni825 – 827Combined sources3
Beta strandi834 – 836Combined sources3
Turni843 – 845Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HSQNMR-A790-851[»]
2HSPNMR-A790-851[»]
4EY0X-ray2.80A/B/C/D545-790[»]
4FBNX-ray2.40A545-790[»]
ProteinModelPortaliP19174.
SMRiP19174.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19174.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini27 – 142PH 1PROSITE-ProRule annotationAdd BLAST116
Domaini152 – 187EF-handPROSITE-ProRule annotationAdd BLAST36
Domaini320 – 464PI-PLC X-boxPROSITE-ProRule annotationAdd BLAST145
Domaini489 – 523PH 2; first partPROSITE-ProRule annotationAdd BLAST35
Domaini550 – 657SH2 1PROSITE-ProRule annotationAdd BLAST108
Domaini668 – 756SH2 2PROSITE-ProRule annotationAdd BLAST89
Domaini791 – 851SH3PROSITE-ProRule annotationAdd BLAST61
Domaini895 – 931PH 2; second partPROSITE-ProRule annotationAdd BLAST37
Domaini953 – 1070PI-PLC Y-boxPROSITE-ProRule annotationAdd BLAST118
Domaini1075 – 1177C2PROSITE-ProRule annotationAdd BLAST103

Domaini

The SH3 domain mediates interaction with CLNK (By similarity). The SH3 domain also mediates interaction with RALGPS1.By similarity

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiKOG1264. Eukaryota.
ENOG410XPXE. LUCA.
GeneTreeiENSGT00730000110782.
HOVERGENiHBG053611.
InParanoidiP19174.
KOiK01116.
OMAiPMPTFKC.
OrthoDBiEOG091G07R3.
PhylomeDBiP19174.
TreeFamiTF313216.

Family and domain databases

CDDicd09932. SH2_C-SH2_PLC_gamma_like. 1 hit.
cd10341. SH2_N-SH2_PLC_gamma_like. 1 hit.
Gene3Di2.30.29.30. 2 hits.
2.60.40.150. 1 hit.
3.20.20.190. 1 hit.
3.30.505.10. 2 hits.
InterProiView protein in InterPro
IPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028380. PLC-gamma1.
IPR035023. PLC-gamma_C-SH2.
IPR035024. PLC-gamma_N-SH2.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000980. SH2.
IPR001452. SH3_domain.
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF121. PTHR10336:SF121. 1 hit.
PfamiView protein in Pfam
PF00168. C2. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
PIRSFiPIRSF000952. PLC-gamma. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
SMARTiView protein in SMART
SM00239. C2. 1 hit.
SM00233. PH. 3 hits.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF50729. SSF50729. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiView protein in PROSITE
PS50004. C2. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS50003. PH_DOMAIN. 2 hits.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50001. SH2. 2 hits.
PS50002. SH3. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P19174-1) [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
MAGAASPCAN GCGPGAPSDA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT
60 70 80 90 100
FQVKLETRQI TWSRGADKIE GAIDIREIKE IRPGKTSRDF DRYQEDPAFR
110 120 130 140 150
PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIKGLTWL MEDTLQAPTP
160 170 180 190 200
LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD
210 220 230 240 250
LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLEASTLRA GERPELCRVS
260 270 280 290 300
LPEFQQFLLD YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDEFVT
310 320 330 340 350
FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL
360 370 380 390 400
EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH
410 420 430 440 450
AFVASEYPVI LSIEDHCSIA QQRNMAQYFK KVLGDTLLTK PVEISADGLP
460 470 480 490 500
SPNQLKRKIL IKHKKLAEGS AYEEVPTSMM YSENDISNSI KNGILYLEDP
510 520 530 540 550
VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEVSS STELHSNEKW
560 570 580 590 600
FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW
610 620 630 640 650
RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE
660 670 680 690 700
MRLSEPVPQT NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN
710 720 730 740 750
SYAISFRAEG KIKHCRVQQE GQTVMLGNSE FDSLVDLISY YEKHPLYRKM
760 770 780 790 800
KLRYPINEEA LEKIGTAEPD YGALYEGRNP GFYVEANPMP TFKCAVKALF
810 820 830 840 850
DYKAQREDEL TFIKSAIIQN VEKQEGGWWR GDYGGKKQLW FPSNYVEEMV
860 870 880 890 900
NPVALEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS
910 920 930 940 950
MASVAHWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KIMERRKKIA
960 970 980 990 1000
LELSELVVYC RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF
1010 1020 1030 1040 1050
LQYNRLQLSR IYPKGQRLDS SNYDPLPMWI CGSQLVALNF QTPDKPMQMN
1060 1070 1080 1090 1100
QALFMTGRHC GYVLQPSTMR DEAFDPFDKS SLRGLEPCAI SIEVLGARHL
1110 1120 1130 1140 1150
PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW PAKPFHFQIS
1160 1170 1180 1190 1200
NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL
1210 1220 1230 1240 1250
ELASLLIKID IFPAKENGDL SPFSGTSLRE RGSDASGQLF HGRAREGSFE
1260 1270 1280 1290
SRYQQPFEDF RISQEHLADH FDSRERRAPR RTRVNGDNRL
Length:1,290
Mass (Da):148,532
Last modified:November 1, 1990 - v1
Checksum:iAE05ABE2A18EDDAC
GO
Isoform 2 (identifier: P19174-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1215-1215: K → KQ

Show »
Length:1,291
Mass (Da):148,660
Checksum:iEDDBB8D4E49B2F3E
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025213209T → N1 PublicationCorresponds to variant dbSNP:rs2229348Ensembl.1
Natural variantiVAR_022130279S → G1 PublicationCorresponds to variant dbSNP:rs2228246Ensembl.1
Natural variantiVAR_025214739S → T1 PublicationCorresponds to variant dbSNP:rs34203315Ensembl.1
Natural variantiVAR_011908813I → T2 PublicationsCorresponds to variant dbSNP:rs753381Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0386921215K → KQ in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34667 mRNA. Translation: AAA36452.1.
DQ297143 Genomic DNA. Translation: ABB84466.1.
AL022394 Genomic DNA. Translation: CAA18537.1.
CH471077 Genomic DNA. Translation: EAW75991.1.
CH471077 Genomic DNA. Translation: EAW75992.1.
BC136466 mRNA. Translation: AAI36467.1.
BC144136 mRNA. Translation: AAI44137.1.
CCDSiCCDS13313.1. [P19174-2]
CCDS13314.1. [P19174-1]
PIRiA36466.
RefSeqiNP_002651.2. NM_002660.2. [P19174-2]
NP_877963.1. NM_182811.1. [P19174-1]
UniGeneiHs.268177.

Genome annotation databases

EnsembliENST00000244007; ENSP00000244007; ENSG00000124181. [P19174-2]
ENST00000373271; ENSP00000362368; ENSG00000124181. [P19174-1]
GeneIDi5335.
KEGGihsa:5335.
UCSCiuc002xjo.2. human. [P19174-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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 one 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.

Entry informationi

Entry nameiPLCG1_HUMAN
AccessioniPrimary (citable) accession number: P19174
Secondary accession number(s): B7ZLY7
, B9EGH4, E1P5W4, Q2V575
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: July 5, 2017
This is version 218 of the entry and version 1 of the sequence. See 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, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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