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P08487

- PLCG1_BOVIN

UniProt

P08487 - PLCG1_BOVIN

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Protein

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

Gene

PLCG1

Organism
Bos taurus (Bovine)
Status
Reviewed - 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 By similarity.By similarity

Catalytic activityi

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

Cofactori

Calcium.

Enzyme regulationi

Activated by phosphorylation on tyrosine residues.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei335 – 3351PROSITE-ProRule annotation
Active sitei380 – 3801PROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi165 – 17612PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. phosphatidylinositol phospholipase C activity Source: UniProtKB-EC
  3. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. cellular response to epidermal growth factor stimulus Source: UniProtKB
  2. intracellular signal transduction Source: InterPro
  3. in utero embryonic development Source: AgBase
  4. phospholipid catabolic process Source: InterPro
  5. positive regulation of epithelial cell migration Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Keywords - Ligandi

Calcium, Metal-binding

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity
Note: Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment.By similarity

GO - Cellular componenti

  1. COP9 signalosome Source: UniProtKB
  2. lamellipodium Source: UniProtKB
  3. ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 129112901-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1PRO_0000088497Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei506 – 5061PhosphotyrosineBy similarity
Modified residuei771 – 7711Phosphotyrosine; by SYK2 Publications
Modified residuei775 – 7751PhosphotyrosineBy similarity
Modified residuei783 – 7831Phosphotyrosine; alternate3 Publications
Modified residuei783 – 7831Phosphotyrosine; by ITK, SYK and TXK; alternateBy similarity
Modified residuei977 – 9771PhosphotyrosineBy similarity
Modified residuei1222 – 12221PhosphoserineBy similarity
Modified residuei1249 – 12491PhosphoserineBy similarity
Modified residuei1254 – 12541Phosphotyrosine3 Publications

Post-translational modificationi

May be dephosphorylated by PTPRJ By similarity. Tyrosine phosphorylated by activated FGFR1, FGFR2, FGFR3 and FGFR4. 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. Tyrosine phosphorylated in response to signaling via activated FLT1, FLT3, PDGFRA, PDGFRB and KIT. Phosphorylated by ITK and TXK on Tyr-783 upon TCR activation in T-cells By similarity.By similarity
Ubiquitinated by CBLB in activated T-cells.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP08487.

Interactioni

Subunit structurei

Interacts (via SH2 domain) with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated). Interacts (via SH3 domain) with AGAP2. 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 RALGPS1. Interacts (via SH2 domain) with PDGFRB (tyrosine phosphorylated) By similarity. Interacts (via SH3 domain) with HEV ORF3 protein. Interacts (via the SH2 domains) with VIL1 (phosphorylated at C-terminus tyrosine phosphorylation sites). Interacts with FLT1 (tyrosine-phosphorylated). Interacts with AXL, FLT4 and KIT By similarity. Interacts (via SH2 domain) with RET. Interacts (via SH2 domain) with PDGFRA (tyrosine phosphorylated). Interacts with PIP5K1C By similarity. Interacts with NTRK1 and NTRK2 (phosphorylated upon ligand-binding) By similarity. Interacts with SYK; activates PLCG1 By similarity. Interacts with TESPA1 By similarity. Interacts with GRB2, LAT and THEMIS upon TCR activation in thymocytes By similarity.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CBLP226813EBI-8013886,EBI-518228From a different organism.
LATO43561-24EBI-8013886,EBI-8070286From a different organism.
LCP2Q130945EBI-8013886,EBI-346946From a different organism.
PDGFRBP096193EBI-8013886,EBI-641237From a different organism.
SykP480254EBI-8013886,EBI-300116From a different organism.
VAV1P154984EBI-8013886,EBI-625518From a different organism.

Protein-protein interaction databases

DIPiDIP-42760N.
IntActiP08487. 8 interactions.
MINTiMINT-2837008.
STRINGi9913.ENSBTAP00000023383.

Structurei

Secondary structure

1
1291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi664 – 6663
Beta strandi667 – 6704
Beta strandi671 – 6733
Helixi676 – 6849
Beta strandi685 – 6884
Beta strandi691 – 6955
Beta strandi697 – 7004
Beta strandi702 – 7087
Beta strandi711 – 7133
Beta strandi716 – 7183
Beta strandi721 – 7255
Beta strandi727 – 7326
Helixi735 – 7439
Beta strandi746 – 7494

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FCINMR-A663-759[»]
2PLDNMR-A663-759[»]
2PLENMR-A663-759[»]
ProteinModelPortaliP08487.
SMRiP08487. Positions 489-658, 663-759, 790-933.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08487.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 142116PH 1PROSITE-ProRule annotationAdd
BLAST
Domaini152 – 18736EF-handPROSITE-ProRule annotationAdd
BLAST
Domaini320 – 464145PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini489 – 52335PH 2; first partPROSITE-ProRule annotationAdd
BLAST
Domaini550 – 657108SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini668 – 75689SH2 2PROSITE-ProRule annotationAdd
BLAST
Domaini791 – 85161SH3PROSITE-ProRule annotationAdd
BLAST
Domaini895 – 93137PH 2; second partPROSITE-ProRule annotationAdd
BLAST
Domaini953 – 1070118PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini1075 – 1177103C2PROSITE-ProRule annotationAdd
BLAST

Domaini

The SH3 domain mediates interaction with CLNK and RALGPS1.By similarity

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 EF-hand domain.PROSITE-ProRule annotation
Contains 2 PH domains.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation
Contains 2 SH2 domains.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiNOG268751.
HOGENOMiHOG000230864.
HOVERGENiHBG053611.
InParanoidiP08487.
KOiK01116.

Family and domain databases

Gene3Di2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProiIPR000008. C2_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028380. PLC-gamma1.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF52. PTHR10336:SF52. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000952. PLC-gamma. 1 hit.
PRINTSiPR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 3 hits.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50004. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08487-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGAASPCAN GCGPSAPSDA EVVHLCRSLE VGTVMTLFYS KKSQRPERKT
60 70 80 90 100
FQVKLETRQI TWSRGADKIE GAIDIREIKE IRPGKTSRDF DRYQEDPAFR
110 120 130 140 150
PDQSHCFVIL YGMEFRLKTL SLQATSEDEV NMWIRGLTWL MEDTLQAATP
160 170 180 190 200
LQIERWLRKQ FYSVDRNRED RISAKDLKNM LSQVNYRVPN MRFLRERLTD
210 220 230 240 250
LEQRTSDITY GQFAQLYRSL MYSAQKTMDL PFLEASALRA GERPELCRVS
260 270 280 290 300
LPEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDEFVT
310 320 330 340 350
FLFSKENSIW NSQLDEVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL
360 370 380 390 400
EAYARCLRMG CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH
410 420 430 440 450
AFVASEYPVI LSIEDHCSIA QQRNMAQYFK KVLGDTLLTK PVDIAADGLP
460 470 480 490 500
SPNQLKRKIL IKHKKLAEGS AYEEVPTSVM YSENDISNSI KNGILYLEDP
510 520 530 540 550
VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASG 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 TFTKSAIIQN VEKQEGGWWR GDYGGKKQLW FPSNYVEEMV
860 870 880 890 900
SPAALEPERE HLDENSPLGD LLRGVLDVPA CQIAVRPEGK NNRLFVFSIS
910 920 930 940 950
MASVAHWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA
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
QALFLAGGHC GYVLQPSVMR DEAFDPFDKS SLRGLEPCAI CIEVLGARHL
1110 1120 1130 1140 1150
PKNGRGIVCP FVEIEVAGAE YDSIKQKTEF VVDNGLNPVW PAKPFHFQIS
1160 1170 1180 1190 1200
NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEGL
1210 1220 1230 1240 1250
ELASLLVKID VFPAKQENGD LSPFGGASLR ERSCDASGPL FHGRAREGSF
1260 1270 1280 1290
EARYQQPFED FRISQEHLAD HFDGRDRRTP RRTRVNGDNR L
Length:1,291
Mass (Da):148,313
Last modified:August 1, 1988 - v1
Checksum:i9F31C7DAA3F8EA77
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00301 mRNA. Translation: CAA68406.1.
PIRiS00666.
RefSeqiNP_776850.1. NM_174425.3.
UniGeneiBt.307.

Genome annotation databases

GeneIDi281987.
KEGGibta:281987.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y00301 mRNA. Translation: CAA68406.1 .
PIRi S00666.
RefSeqi NP_776850.1. NM_174425.3.
UniGenei Bt.307.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2FCI NMR - A 663-759 [» ]
2PLD NMR - A 663-759 [» ]
2PLE NMR - A 663-759 [» ]
ProteinModelPortali P08487.
SMRi P08487. Positions 489-658, 663-759, 790-933.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-42760N.
IntActi P08487. 8 interactions.
MINTi MINT-2837008.
STRINGi 9913.ENSBTAP00000023383.

Chemistry

BindingDBi P08487.
ChEMBLi CHEMBL5566.

Proteomic databases

PRIDEi P08487.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 281987.
KEGGi bta:281987.

Organism-specific databases

CTDi 5335.

Phylogenomic databases

eggNOGi NOG268751.
HOGENOMi HOG000230864.
HOVERGENi HBG053611.
InParanoidi P08487.
KOi K01116.

Miscellaneous databases

EvolutionaryTracei P08487.
NextBioi 20805855.

Family and domain databases

Gene3Di 2.30.29.30. 3 hits.
2.60.40.150. 1 hit.
3.20.20.190. 2 hits.
3.30.505.10. 2 hits.
InterProi IPR000008. C2_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001192. PI-PLC_fam.
IPR016279. PLC-gamma.
IPR028380. PLC-gamma1.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000980. SH2.
IPR001452. SH3_domain.
[Graphical view ]
PANTHERi PTHR10336. PTHR10336. 1 hit.
PTHR10336:SF52. PTHR10336:SF52. 1 hit.
Pfami PF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF00017. SH2. 2 hits.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF000952. PLC-gamma. 1 hit.
PRINTSi PR00390. PHPHLIPASEC.
PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
SMARTi SM00239. C2. 1 hit.
SM00233. PH. 3 hits.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00252. SH2. 2 hits.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF51695. SSF51695. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence similarity of phospholipase C with the non-catalytic region of src."
    Stahl M.L., Ferenz C.R., Kelleher K.L., Kriz R.W., Knopf J.L.
    Nature 332:269-272(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Tyrosine residues in bovine phospholipase C-gamma phosphorylated by the epidermal growth factor receptor in vitro."
    Kim J.W., Sim S.S., Kim U.H., Nishibe S., Whal M.I., Carpenter G., Rhee S.G.
    J. Biol. Chem. 265:3940-3943(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-771; TYR-783 AND TYR-1254.
  3. "Identification of two epidermal growth factor-sensitive tyrosine phosphorylation sites of phospholipase C-gamma in intact HSC-1 cells."
    Whal M.I., Nishibe S., Kim J.W., Kim H.K., Rhee S.G., Carpenter G.
    J. Biol. Chem. 265:3944-3948(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-771; TYR-783 AND TYR-1254.
  4. "Binding of SH2 domains of phospholipase C gamma 1, GAP, and Src to activated growth factor receptors."
    Anderson D., Koch C.A., Grey L., Ellis C., Moran M.F., Pawson T.
    Science 250:979-982(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDGFRA.
  5. "PDGF stimulation of inositol phospholipid hydrolysis requires PLC-gamma 1 phosphorylation on tyrosine residues 783 and 1254."
    Kim H.K., Kim J.W., Zilberstein A., Margolis B., Kim J.G., Schlessinger J., Rhee S.G.
    Cell 65:435-441(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-783 AND TYR-1254.
  6. "Direct association between the Ret receptor tyrosine kinase and the Src homology 2-containing adapter protein Grb7."
    Pandey A., Liu X., Dixon J.E., Di Fiore P.P., Dixit V.M.
    J. Biol. Chem. 271:10607-10610(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RET.
  7. "Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide."
    Pascal S.M., Singer A.U., Gish G., Yamazaki T., Shoelson S.E., Pawson T., Kay L.E., Forman-Kay J.D.
    Cell 77:461-472(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 663-759.

Entry informationi

Entry nameiPLCG1_BOVIN
AccessioniPrimary (citable) accession number: P08487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: October 29, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

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

External Data

Dasty 3