wanglab/gogpt-training-data huggingface dataset:
Protein: SCD5 protein (Stearoyl-CoA desaturase 5, isoform CRA_d) (Q9BSN4)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPGPATDAGKIPFCDAKEEIRAGLESSEGGGGPERPGARGQRQNIVWRNVVLMSLLHLGAVYSLVLIPKAKPLTLLWAYFCFLLAALGVTAGAHRLWSHRSYRAKLPLRIFLAVANSMAFQAAAEVVLTQMP
Protein: Kit ligand (Mast cell growth factor) (MGF) (Stem cell factor) (SCF) (c-Kit ligand) [Cleaved into: Soluble KIT ligand (sKITLG)] (P21583)
Organism: Homo sapiens (Human)
Function: Ligand for the receptor-type protein-tyrosine kinase KIT. Plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. KITLG/SCF binding can activate several signaling pathways. Promotes phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, and subsequent activation of the kinase AKT1. KITLG/SCF and KIT also transmit signals via GRB2 and activation of RAS, RAF1 and the MAP kinases MAPK1/ERK2 and/or MAPK3/ERK1. KITLG/SCF and KIT promote activation of STAT family members STAT1, STAT3 and STAT5. KITLG/SCF and KIT promote activation of PLCG1, leading to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. KITLG/SCF acts synergistically with other cytokines, probably interleukins.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:26522471}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:26522471}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, lamellipodium {ECO:0000269|PubMed:26522471}. Cell projection, filopodium {ECO:0000269|PubMed:26522471}.; SUBCELLULAR LOCATION: [Soluble KIT ligand]: Secreted.
Interaction partners:
- Mast/stem cell growth factor receptor Kit
- High affinity nerve growth factor receptor
- Interleukin-3
- Receptor-type tyrosine-protein kinase FLT3
- Fms-related tyrosine kinase 3 ligand
- Platelet-derived growth factor receptor alpha
- Thrombopoietin
- C-X-C chemokine receptor type 4
- Platelet-derived growth factor receptor beta
- Epidermal growth factor receptor
Sequence:
MKKTQTWILTCIYLQLLLFNPLVKTEGICRNRVTNNVKDVTKLVANLPKDYMITLKYVPGMDVLPSHCWISEMVVQLSDSLTDLLDKFSNISEGLSNYSIIDKLVNIVDDLVECVKENSSKDLKKSFKSPEPRLFTPEEFFRIFNRSIDAFKDFVVASETSDCVVSSTLSPEKDSRVSVTKPFMLPPVAASSLRNDSSSSNRKAKNPPGDSSLHWAAMALPALFSLIIGFAFGALYWKKRQPSLTRAVENIQINEEDNEISMLQEKEREFQEV
Protein: Actin-like protein 6B (53 kDa BRG1-associated factor B) (Actin-related protein Baf53b) (ArpNalpha) (BRG1-associated factor 53B) (BAF53B) (O94805)
Organism: Homo sapiens (Human)
Function: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex), as such plays a role in remodeling mononucleosomes in an ATP-dependent fashion, and is required for postmitotic neural development and dendritic outgrowth. During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. ACTL6B/BAF53B is not essential for assembly of the nBAF complex but is required for targeting the complex and CREST to the promoter of genes essential for dendritic growth (By similarity). Essential for neuronal maturation and dendrite development.
Subcellular location: Nucleus {ECO:0000303|PubMed:26601204}.
Interaction partners:
- Zinc finger protein neuro-d4
- Zinc finger protein DPF3
- PHD finger protein 10
- SWI/SNF complex subunit SMARCC2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- AT-rich interactive domain-containing protein 1A
Sequence:
MSGGVYGGDEVGALVFDIGSFSVRAGYAGEDCPKADFPTTVGLLAAEEGGGLELEGDKEKKGKIFHIDTNALHVPRDGAEVMSPLKNGMIEDWECFRAILDHTYSKHVKSEPNLHPVLMSEAPWNTRAKREKLTELMFEQYNIPAFFLCKTAVLTAFANGRSTGLVLDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFISMQCRELFQEMAIDIIPPYMIAAKEPVREGAPPNWKKKEKLPQVSKSWHNYMCNEVIQDFQASVLQVSDSPYDEQVAAQMPTVHYEMPNGYNTDYGAERLRIPEGLFDPSNVKGLSGNTMLGVGHVVTTSIGMCDIDIRPGLYGSVIVTGGNTLLQGFTDRLNRELSQKTPPSMRLKLIASNSTMERKFSPWIGGSILASLGTFQQMWISKQEYEEGGKQCVERKCP
Protein: Thioredoxin F1, chloroplastic (AtTrxf1) (Thioredoxin F2) (AtTrxf2) (Q9XFH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiol-disulfide oxidoreductase involved in the redox regulation of enzymes of both reductive pentose phosphate pathway (Calvin-Benson cycle) and oxidative pentose phosphate pathway. Under light or reducing conditions, activates in chloroplast the glyceraldehyde-3-phosphate dehydrogenase, the phosphoribulokinase and the fructose-1,6-bisphosphate phosphatase, and inhibits the glucose-6-phosphate dehydrogenase.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19259774}.
Interaction partners:
- Thioredoxin M4, chloroplastic
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Thioredoxin-like protein CITRX, chloroplastic
- NADPH-dependent thioredoxin reductase 3
- Peroxiredoxin Q, chloroplastic
- 2-Cys peroxiredoxin BAS1-like, chloroplastic
- Thioredoxin-like protein CDSP32, chloroplastic
- Rhodanese-like domain-containing protein 14, chloroplastic
- Thioredoxin M3, chloroplastic
- Malate dehydrogenase, chloroplastic
Sequence:
MPLSLRLSPSPTALSPTTGGFGPSRKQCRIPYSGVPTTKIGFCSLDSRKRGDSSVVRCSLETVNVSVGQVTEVDKDTFWPIVKAAGEKLVVLDMYTQWCGPCKVIAPKYKALSEKYDDVVFLKLDCNPDNRPLAKELGIRVVPTFKILKDNKVVKEVTGAKYDDLVAAIETARSAASG
Protein: Rabphilin-3A (Exophilin-1) (P47708)
Organism: Mus musculus (Mouse)
Function: Plays an essential role in docking and fusion steps of regulated exocytosis (By similarity). At the presynaptic level, RPH3A is recruited by RAB3A to the synaptic vesicle membrane in a GTP-dependent manner where it modulates synaptic vesicle trafficking and calcium-triggered neurotransmitter release (By similarity). In the post-synaptic compartment, forms a ternary complex with GRIN2A and DLG4 and regulates NMDA receptor stability. Also plays a role in the exocytosis of arginine vasopressin hormone (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P47709}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P47709}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P47709}. Membrane {ECO:0000250|UniProtKB:P47709}; Peripheral membrane protein {ECO:0000250|UniProtKB:P47709}.
Interaction partners:
- Ras-related protein Rab-3A
- Ras-related protein Rab-27A
- Ras-related protein Rab-8A
- Ras-related protein Rab-27B
- Ras-related protein Rab-3C
- Glutamate receptor ionotropic, NMDA 2A
Sequence:
MTDTVVNRWMYPGDGPLQSNDKEQLQAGWSVHPGAQTDRQRKQEELTDEEKEIINRVIARAEKMEAMEQERIGRLVDRLETMRKNVAGDGVNRCILCGEQLGMLGSACVVCEDCKKNVCTKCGVETSNNRPHPVWLCKICLEQREVWKRSGAWFFKGFPKQVLPQPMPIKKTKPQQPAGEPATQEQPTPESRHPARAPARGDMEDRRPPGQKPGPDLTSAPGRGSHGPPTRRASEARMSTAARDSEGWDHAHGGGTGDTSRSPAGLRRANSVQAARPAPAPVPSPAPPQPVQPGPPGGSRATPGPGRFPEQSTEAPPSDPGYPGAVAPAREERTGPAGGFQAAPHTAAPYSQAAPARQPPPAEEEEEEANSYDSDEATTLGALEFSLLYDQDNSNLQCTIIRAKGLKPMDSNGLADPYVKLHLLPGASKSNKLRTKTLRNTRNPVWNETLQYHGITEEDMQRKTLRISVCDEDKFGHNEFIGETRFSLKKLKANQRKNFNICLERVIPMKRAGTTGSARGMALYEEEQVERIGDIEERGKILVSLMYSTQQGGLIVGIIRCVHLAAMDANGYSDPFVKLWLKPDMGKKAKHKTQIKKKTLNPEFNEEFFYDIKHSDLAKKSLDISVWDYDIGKSNDYIGGCQLGISAKGERLKHWYECLKNKDKKIERWHQLQNENHVSSD
Protein: Phosphoglycerate mutase (PGAM) (EC 5.4.2.11) (BPG-dependent PGAM) (MPGM) (Phosphoglyceromutase) (P82612)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15378761}.
Interaction partners:
- Phosphoglycerate kinase
- Fructose-bisphosphate aldolase
- Enolase 1
- Glucose-6-phosphate isomerase
- Triosephosphate isomerase
- Pyruvate kinase
- Transaldolase
- Pyruvate decarboxylase
- 2-oxoglutarate reductase
- Hexokinase-2
Sequence:
MPKLVLVRHGQSEWNEKNLFTGWVDVRLSETGQKEAKRAGELLKEAGINVDVLHTSKLSRAIQTANIALDAADQLYVPVKRSWRLNERHYGALQGKDKAQTLEAYGQEKFQIWRRSFDVPPPKIDPKDEYSQVGDRRYADVDPAVVPLTESLALVIDRLLPYWQDEIAGDLLAGKVVLIAAHGNSLRALVKHLDNISDEDIAGLNIPTGIPLVYELDENLKPTKPSYYLDPEAAAAGAAAVAAQGQKK
Protein: Glutamate--cysteine ligase EgtA (EC 6.3.2.2) (Gamma-glutamylcysteine synthase) (GCS) (Gamma-ECS) (P9WPK7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the synthesis of gamma-glutamylcysteine (gamma-GC). This compound is used as substrate for the biosynthesis of the low-molecular thiol compound ergothioneine (By similarity).
Interaction partners:
- Hercynine oxygenase
- Histidine N-alpha-methyltransferase
- Gamma-glutamyl-hercynylcysteine sulfoxide hydrolase
- Probable hercynylcysteine sulfoxide lyase
- Putative glutamate--cysteine ligase 2
- Probable gamma-glutamyltranspeptidase GgtB
- Glutathione hydrolase proenzyme
- Probable cytosol aminopeptidase
- Aminopeptidase N
- Branched-chain-amino-acid aminotransferase
Sequence:
MTLAAMTAAASQLDNAAPDDVEITDSSAAAEYIADGCLVDGPLGRVGLEMEAHCFDPADPFRRPSWEEITEVLEWLSPLPGGSVVSVEPGGAVELSGPPADGVLAAIGAMTRDQAVLRSALANAGLGLVFLGADPLRSPVRVNPGARYRAMEQFFAASHSGVPGAAMMTSTAAIQVNLDAGPQEGWAERVRLAHALGPTMIAIAANSPMLGGRFSGWQSTRQRVWGQMDSARCGPILGASGDHPGIDWAKYALKAPVMMVRSPDTQDTRAVTDYVPFTDWVDGRVLLDGRRATVADLVYHLTTLFPPVRPRQWLEIRYLDSVPDEVWPAVVFTLVTLLDDPVAADLAVDAVEPVATAWDTAARIGLADRRLYLAANRCLAIAARRVPTELIGAMQRLVDHVDRGVCPADDFSDRVIAGGIASAVTGMMHGAS
Protein: Keratin, type II cytoskeletal 6C (Cytokeratin-6C) (CK-6C) (Cytokeratin-6E) (CK-6E) (Keratin K6h) (Keratin-6C) (K6C) (Type-II keratin Kb12) (P48668)
Organism: Homo sapiens (Human)
Interaction partners:
- Keratin, type II cytoskeletal 6B
- Keratin, type II cytoskeletal 5
- Keratin, type II cytoskeletal 6A
Sequence:
MASTSTTIRSHSSSRRGFSANSARLPGVSRSGFSSISVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISIGGGSCAISGGYGSRAGGSYGFGGAGSGFGFGGGAGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPAIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCASLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVNVSVVQSTISSGYGGASGVGSGLGLGGGSSYSYGSGLGIGGGFSSSSGRAIGGGLSSVGGGSSTIKYTTTSSSSRKSYKH
Protein: 4-coumarate--CoA ligase 2 (4CL 2) (Nt4CL-19) (Nt4CL-2) (EC 6.2.1.12) (4-coumaroyl-CoA synthase 2) (Caffeate--CoA ligase) (EC 6.2.1.-) (Cinnamate--CoA ligase) (EC 6.2.1.-) (Ferulate--CoA ligase) (EC 6.2.1.34) (O24146)
Organism: Nicotiana tabacum (Common tobacco)
Function: Major enzyme of the phenylpropanoid pathway that mediates the production of several precursors for numerous metabolites and regulates carbon flow. Catalyzes the formation of CoA thioesters using 4-coumarate, ferulate, caffeate, and cinnamate as substrates. Follows a two-step reaction mechanism, wherein a (hydroxy)cinnamate substrate first undergoes adenylation by ATP leading to an acyl-AMP, followed by a thioesterification in the presence of CoA to yield the final (hydroxy)cinnamoyl-CoA product. Almost inactive toward sinapate.
Interaction partners:
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
- caffeoyl-CoA O-methyltransferase 1.
- Phenylalanine ammonia-lyase.
- Phenylalanine ammonia-lyase
- Phenylalanine ammonia-lyase
- chalcone synthase
- chalcone synthase
Sequence:
MEKDTKQVDIIFRSKLPDIYIPNHLPLHSYCFENISEFSSRPCLINGANKQIYTYADVELNSRKVAAGLHKQGIQPKDTIMILLPNSPEFVFAFIGASYLGAISTMANPLFTPAEVVKQAKASSAKIIVTQACHVNKVKDYAFENDVKIICIDSAPEGCLHFSVLTQANEHDIPEVEIQPDDVVALPYSSGTTGLPKGVMLTHKGLVTSVAQQVDGENPNLYIHSEDVMLCVLPLFHIYSLNSVLLCGLRVGAAILIMQKFDIVSFLELIQRYKVTIGPFVPPIVLAIAKSPMVDDYDLSSVRTVMSGAAPLGKELEDTVRAKFPNAKLGQGYGMTEAGPVLAMCLAFAKEPFEIKSGACGTVVRNAEMKIVDPKTGNSLPRNQSGEICIRGDQIMKGYLNDPEATARTIDKEGWLYTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLLNHPNISDAAVVPMKDEQAGEVPVAFVVRSNGSTITEDEVKDFISKQVIFYKRIKRVFFVDAIPKSPSGKILRKDLRAKLAAGLPN
Protein: Kelch repeat-containing protein (Q54CD2)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Cysteine proteinase 4
Sequence:
MEWIKIQPKGLQPPKRGGHTSTIVKNKMYVFGGGSYQPPNANSLALEPNNLHVYDFTSNTWSIQSTMGTPPSIRYGHTATEVGDKIFIIGGYGTNMFYDDVSIFDTVTNTWSTPICGGQRPSARYAHTATLVGTNIFVFAGCYENKCFNELYCLDTIQYQWSLVVTSGSPPQQRSYHTTNLIGRKLYVFGGHLGNSYHNDLYVFNLDSKVWTQGITLGKFETGIAYHSSAIINNQLFIFGGNDGRVCYDTLWKLNIENMEWEKLAFKDSSHKPPSRHKHTLSVSHDLSLILYGGMEFYPNCYDDFYKLSIPMGKHPQSPNLISIYQQPLIINQQNNNNNNNNNNNNNNNNNGLIVQIPSSPSMLSLASGIGIGLSQSTPSTPTISEITDDRNKLLYEYNKLKEEQDQVKNVIDLLSCLSLTNATIGELDNLENCFLDGLKRISNAKRIYIETKTKELREENDFLKQHFGNNNNNNNNNYPQIPPLSPSSPSSPPLLLQQQYINQQQSYSIQKPFGFKHNQNIINQNNSSNYHSSKPLRRVNSTDSVIIDGRNKDLAFSMNGNNLSPQGSPHLNSNQRSYNRVLNNNFNLNSPTNQSNVNLNPNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTSTSNIISNNTTTNNNNSTGNNANSAIQNNNGINIPNFVNNNSNNNNSNNNNSNNKYMSKSNQPQFPFQNYQPPQQQ
Protein: PH and SEC7 domain-containing protein 4 (Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6 B) (Exchange factor for ARF6 B) (Pleckstrin homology and SEC7 domain-containing protein 4) (Telomeric of interleukin-1 cluster protein) (Q8NDX1)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor for ARF6 and ARL14/ARF7. Through ARL14 activation, controls the movement of MHC class II-containing vesicles along the actin cytoskeleton in dendritic cells. Involved in membrane recycling. Interacts with several phosphatidylinositol phosphate species, including phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 3,5-bisphosphate and phosphatidylinositol 4,5-bisphosphate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12082148, ECO:0000269|PubMed:23603394}. Cell projection, ruffle membrane {ECO:0000269|PubMed:12082148, ECO:0000269|PubMed:23603394}. Note=In interphase associated with the plasma membrane, in particular with membrane ruffling regions (PubMed:23603394). Accumulates in dynamic actin-rich membrane ruffles and microvilli-like structures (PubMed:12082148). Recruited to membranes via phosphatidylinositol phosphate-binding (Probable). {ECO:0000269|PubMed:12082148, ECO:0000269|PubMed:23603394, ECO:0000305|PubMed:12082148}.
Interaction partners:
- ADP-ribosylation factor-like protein 14
- ADP-ribosylation factor 6
Sequence:
MMGDYRLPDHPQPMEILNLYLGDSLEPHPGECPRETCSHEDPPEPFEEQTWATDPPEPTRQNVPPWGSGVELTHLGSWVHQDGLEPCQEQTRATDPPESTRQDAPPWGSGVELTHLGSPSAQREHRQNTASPGSPVNSHLPGSPKQNRSTSTQVVFWAGILQAQMCVLDLEEELEKTEGLKAGLKCCLPTPPVDLPGDTGLHSSPPENEDSGEDSSEPEGEGQAWLREGTPDSSPQWGAEEESMFFSNPLFLASPCSENSASGECFSWGASDSHAGVRTGPESPATLEPPLPEDTVLWELESEPDLGDGAAISGHCTPPFPVPIYKPHSICWASVAAAEGAPAAPPGHGESEGDRLGPAPSAAPCVDEALTWESGCVGSDLGPAAHPVQPWASLSPEGWQRGGPFWPQVTLNSQDRDEREGGHPQESLPCTLAPCPWRSPASSPEPSSPESESRGPGPRPSPASSQEGSPQLQHHSSGILPKWTLDASQSSLLETDGEQPSSLKKKEAGEAPKPGEEVKSEGTARPAETGDVQPDIHLTSAEHENLRTPMNSSWLPGSPMPQAQSPEEGQRPPAGDKLANGVRNNKVAWNLASRLYRLEGFRKSEVAAYLQKNNDFSRAVAEEYLSFFQFGGQSLDRALRSFLQALVLSGETQERERILYQFSRRFHHCNPGIFPSVDSVHTLTCAIMLLNTDLHGQNIGKSMSCQEFITNLNGLRDGGNFPKELLKALYWSIRSEKLEWAVDEEDTARPEKAQPSLPAGKMSKPFLQLAQDPTVPTYKQGILARKMHQDADGKKTPWGKRGWKMFHTLLRGMVLYFLKQGEDHCLEGESLVGQMVDEPVGVHHSLATPATHYTKKPHVFQLRTADWRLYLFQAPTAKEMSSWIARINLAAATHSAPPFPAAVGSQRRFVRPILPVGPAQSSLEEQHRSHENCLDAAADDLLDLQRNLPERRGRGRELEEHRLRKEYLEYEKTRYETYVQLLVARLHCPSDALDLWEEQLGREAGGTREPKLSLKKSHSSPSLHQDEAPTTAKVKRNISERRTYRKIIPKRNRNQL
Protein: Proteasome subunit alpha type (B5X9F8)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU000551}. Nucleus {ECO:0000256|RuleBase:RU000551}.
Interaction partners:
- Proteasome subunit beta
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 12
- 26S protease regulatory subunit 6A-B-like isoform X1
- Protease regulatory subunit 6A
- Proteasome subunit beta
- 26S proteasome non-ATPase regulatory subunit 12
- Proteasome subunit beta
- 26S proteasome non-ATPase regulatory subunit 1
- Proteasome subunit alpha type
Sequence:
MFLTRSEYDRGVNTFSPEGRLFQVEYAIEAIKLGSTAIGIQTSEGVCLAVEKRITSPLMEPSSIEKIVEIDTHIGCAMSGLIADAKTLIDKARVETQNHWFTYNETMTVESVTQAVSNLALQFGEEDADPGAMSRPFGVALLFGGLDEKGPQLYHMDPSGTFVQCDARAIGSASEGAQSSLQEVYHKSMTLKEAIKSSLTILKQVMEEKLNATNIELATIEPGKTFHMYSKEELEDVIKDI
Protein: Endo-beta-1,4-glucanase celB (Endoglucanase celB) (EC 3.2.1.4) (Carboxymethylcellulase celB) (Cellulase B) (Q5B7R2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Endo-beta-1,4-glucanase A
- Probable beta-glucosidase A
- Glucanase
- 1,4-beta-D-glucan cellobiohydrolase C
- Endo-beta-1,4-glucanase B
- Probable 1,4-beta-D-glucan cellobiohydrolase A
- 1,4-beta-D-glucan cellobiohydrolase B
- Extracellular endoglucanase, putative
- Xylanolytic transcriptional activator xlnR
- beta-glucosidase
Sequence:
MALLLSLSLLATTISAQQIGTPEIRPRLTTYHCTSANGCTEQNTSVVLDAATHPIHDASNPSVSCTTSNGLNPALCPDKQTCADNCVIDGITDYAAHGVETHGSRLTLTQYRNVNGALSSVSPRVYLVDESDPDEQEYRALSLLAQEFTFTVNVSALPCGMNGALYLSEMSPSGGRSALNPAGASYGTGYCDAQCYVNPWINGEGNINGYGACCNEMDIWEANSRSTGFTPHACLYEPEETEGRGVYECASEDECDSAGENDGICDKWGCGFNPYALGNTEYYGRGQGFEVDTKEPFTVVTQFLTDDGTSTGALTEIRRLYIQNGQVIENAVVSSGADSLTDSLCASTASWFDSYGGMEGMGRALGRGMVLAMSIWNDAGGYMQWLDGGDAGPCNATEGAPEFIEEHTPWTRVVFEDLKWGDIGSTFQAS
Protein: Protein phosphatase 1 regulatory subunit 3G (Q9CW07)
Organism: Mus musculus (Mouse)
Function: Glycogen-targeting subunit for protein phosphatase 1 (PP1). Involved in the regulation of hepatic glycogenesis in a manner coupled to the fasting-feeding cycle and distinct from other glycogen-targeting subunits.
Interaction partners:
- Protein phosphatase 1 regulatory subunit 3A
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
Sequence:
MDPSGEQLHRSEASSSTSSGDPQSAEELSVPEVLCVESGTSETPIPDAQLQDRPLSPQKGAALPEQEELQEYRRSRARSFSLPADPILQAAKLLQQRQQAGQPSSEGGAPAGDCCSKCKKRVQFADSLGLSLASVKHFSEAEEPQVPPAVLSRLHSFPLRAEDLQQLGGLLAVATMPDPLLVPCARLRPHFQLPELRAAEERLRRQRVCLERVQCSQPPRAEVTGSGRVISCPGPRAVAVRYTFTEWRTFLDVPAELDPESVEPLPPLQSGDSGSKAEDSEEGPGTERFHFSLCLPPGLQPKEGEDAGAWGVAIHFAVCYRCEQGEYWDNNEGANYTLRYVCSTDPL
Protein: VP16 (C8CHL4)
Organism: Thermus virus P23-77
Interaction partners:
Sequence:
MQEAFNRIKALRPGARPATILRSGPEFSVYSGTQRVKVGEFVVPAGASWVLPNPVPVILKLYDTGGNQLPHTTDVFLAKRTKGFDFPEFLAKVQYASYYDLTEAQLRDAKFYQNILQTLSPLRAPQPPQGVVLREGDVLEVYVEAPAGVTVNLNDPRTRIELPIGVDNSNPTL
Protein: Ninja-family protein AFP4 (ABI five-binding protein 4) (ABI5-binding protein 4) (Protein TWO OR MORE ABRES-CONTAINING GENE 2) (Q9S7Z2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a negative regulator of abscisic acid (ABA) and salinity responses.
Subcellular location: Nucleus {ECO:0000269|PubMed:17195036}.
Interaction partners:
- Transcription factor GTE10
Sequence:
MEMIRGRGIPNGVVQVPNLSANNLLQKFFIASNHFCQRDSEHGENQQEAKKREDEAEEDEKDVELTLGLSLNGQFGTDPRSRKRRHFELGRSSSIPEGFVFDEQRSGGGNGGDMRRIVGRGGSDMFQLDRTRSLPVVTEMDIEKERKVSEKTRAFMESPVTNRGAYLTKDKNRGQAVETEKPRAFLEFKIPPTKEGKKEKDRLVVTGPVNGKGKNGNTAKKQKNNVENSGMEKARNILEDMPCVSTRDVGADGKRVEGFLYWYGGNKEEVKIVCVCHGSFLSPAEFVRHGGGTVSDDDGGDVMINPLRHIVVKLPSSSI
Protein: Uncharacterized protein YKR005C (Q02203)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Grand meiotic recombination cluster protein 2
- Uncharacterized protein YKL050C
- Uncharacterized protein YOL131W
Sequence:
MLECLSALLVLFAGGGGSVLAAVQSKTVADPNLCPGYNSQLISPFLSSCKRNLSECVSRYFDEQYAFCRSCVTVNNETMEDLDNCKCLQCALSSLNNSCFHDYCTSKDEYDKLQIVVEQFQLTNGVLDDGEILKPRGNKFSSRKLSYFVGQNNTLFRNPLQFEKNQLISALLTSLTNNQKTISSVDMFEVVDANNEVQYLRERTISGKTLSPATGYEEENDGDCSVKDKKWEGKIEYHENKKVSSENCSKDTDDKSGSKKERNTKAPLFHTATEIHMTRWSSWRPKKIFTRYLVNEYQSPKIITTVNRFYRTKTDTETGTTLITSTKAKRRWFPRTKIVTSTATSTFLSITTTTTTNAIATKSLVAVLNPDGLNKKAGINFGLFSANGELASPDEGGTPTVVRRDKISDPGAANEQATLFSTTFSQVPHLPELDSGEFISAASQLDKRIFIFTAITVSITTLMMLGFSYRSRVSFRDHSIDDSDDDNDWSDDEVEFDEEYFYSLPVSIPEKGISLDKMAQQLGVE
Protein: Carboxyltransferase domain-containing protein (P95221)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Carboxyltransferase domain-containing protein
- Aminoglycoside 2'-N-acetyltransferase
- Probable periplasmic iron-transport lipoprotein
- Proline-rich antigen homolog
- Possible membrane protein
- Probable conserved Mce associated protein
- Possible conserved transmembrane protein
- Probable transport accessory protein MmpS1
- Probable 5-oxoprolinase OplA
- Three-Cys-motif partner protein TcmP
Sequence:
MDAALACTVLDYGDHALMLQCDSTADAMAWTDALRAAALPGVVDIVAASRTVLVKLDAPRYQGVTRQRLRRLRVTPEAVAAADHRCDLVIDVVYDGPDLAEVARCTGLTTAAVINAHTATGWRAGFSGSAPGFAYLIDGDPSLRVPRRPERRTSMPPGSVALADGFSAIYPSQAPSDWQIIGHTDAVLWDVDRPQPALLTPGMWVQFRAA
Protein: Death domain-containing protein CRADD (Caspase and RIP adapter with death domain) (RIP-associated protein with a death domain) (P78560)
Organism: Homo sapiens (Human)
Function: Adapter protein that associates with PIDD1 and the caspase CASP2 to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis. Also recruits CASP2 to the TNFR-1 signaling complex through its interaction with RIPK1 and TRADD and may play a role in the tumor necrosis factor-mediated signaling pathway.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O88843}. Nucleus {ECO:0000250|UniProtKB:O88843}.
Interaction partners:
- p53-induced death domain-containing protein 1
- Caspase-2
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- FAS-associated death domain protein
- Cytoplasmic FMR1-interacting protein 2
- Receptor-interacting serine/threonine-protein kinase 1
- Apoptotic protease-activating factor 1
- Ubiquitin carboxyl-terminal hydrolase MINDY-3
Sequence:
MEARDKQVLRSLRLELGAEVLVEGLVLQYLYQEGILTENHIQEINAQTTGLRKTMLLLDILPSRGPKAFDTFLDSLQEFPWVREKLKKAREEAMTDLPAGDRLTGIPSHILNSSPSDRQINQLAQRLGPEWEPMVLSLGLSQTDIYRCKANHPHNVQSQVVEAFIRWRQRFGKQATFQSLHNGLRAVEVDPSLLLHMLE