wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase (EC 2.4.1.143) (Beta-1,2-N-acetylglucosaminyltransferase II) (GlcNAc-T II) (Mannoside acetylglucosaminyltransferase 2) (N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II) (O17560)
Organism: Caenorhabditis elegans
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
- Alpha-
- Alpha-mannosidase
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-1,6-mannosylglycoprotein 6-beta-N-acetylglucosaminyltransferase
- Putative alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Exostosin-like-3 homolog
- GP-PDE domain-containing protein
- Uncharacterized protein
- RING-type domain-containing protein
Sequence:
MMVYRRMHRLANAVIACCLFGFIVIFLKAPGEDQRLRDGVPVLSQNPVWSVNDWNGLNKEVVDLLKNESNRLSINEKPDLSGWNFKTKEDMSLKGSEIVESVSFLNENFDILNAAKFGDLSTVKTILVIQVHDRPVYLQYLIESMRNTKGIEDTLLVFSHDINVGIINEMIRNITFARVYQIFYPYNLQLFPTVFPGQSPSDCPEKMKRDKAQETNCSNWSSPDKYGNYRVAQLTQIKHHWWWKMNFVFDGIVEKYSMKDPWVLLLEEDHMLAPDALHVLDIIVSNRPKYCENCEIISLGFYLKSTNKYGQDIAHLGVHPWYSSKHNMGMALQKNTWQKIKGCSEMFCKWDDYNWDWSLMQISAKCLPQRFRVIFTKSPRVIHIGDCGVHTHRCEAHKALQSTQELFRQHKDLLFPTSLSVTDTSRRSLKPSKENGGWGDIRDRQLCEINKSPLVRVSSQSASVLHKLLNSKIQFSSSNKTITSTTS
Protein: Fermitin family homolog 2 (Kindlin-2) (Pleckstrin homology domain-containing family C member 1) (Q8CIB5)
Organism: Mus musculus (Mouse)
Function: Scaffolding protein that enhances integrin activation mediated by TLN1 and/or TLN2, but activates integrins only weakly by itself. Binds to membranes enriched in phosphoinositides. Enhances integrin-mediated cell adhesion onto the extracellular matrix and cell spreading; this requires both its ability to interact with integrins and with phospholipid membranes. Required for the assembly of focal adhesions. Participates in the connection between extracellular matrix adhesion sites and the actin cytoskeleton and also in the orchestration of actin assembly and cell shape modulation. Recruits FBLIM1 to focal adhesions. Plays a role in the TGFB1 and integrin signaling pathways. Stabilizes active CTNNB1 and plays a role in the regulation of transcription mediated by CTNNB1 and TCF7L2/TCF4 and in Wnt signaling.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, lamellipodium membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, myofibril, sarcomere, I band. Cell surface. Note=Colocalizes with actin stress fibers at cell-ECM focal adhesion sites. Colocalizes with ITGB3 at lamellipodia at the leading edge of spreading cells. Binds to membranes that contain phosphatidylinositides (By similarity). {ECO:0000250}.
Interaction partners:
- Filamin-binding LIM protein 1
- Scaffold protein ILK
- Integrin beta-1
- Paxillin
- LIM and senescent cell antigen-like-containing domain protein 1
- Filamin-A
- Cas scaffolding protein family member 4
- Vinculin
- Alpha-parvin
- Ras-related C3 botulinum toxin substrate 1
Sequence:
MALDGIRMPDGCYADGTWELSVHVTDLNRDVTLRVTGEVHIGGVMLKLVEKLDVKKDWSDHALWWEKKRTWLLKTHWTLDKCGIQADAKLQFTPQHKLLRLQLPNMKYVKVKVNFSDRVFKAVSDICKTFNIRHPEELSLLKKPRDPTKKKKKKLDDQSEDEALELEGPLIMPGSGSIYSSPGLYSKTMTPTYDAHDGSPLSPTSAWFGDSALSEGNPGILAVSQPVTSPEILAKMFKPQALLDKAKTNQGWLDSSRSLMEQDVKENEALLLRFKYYSFFDLNPKYDAIRINQLYEQAKWALLLEEIECTEEEMMMFAALQYHINKLSIMTSENHLNNSDKEVDEVDAALSDLEITLEGGKTSTILGDITSIPELADYIKVFKPKKLTLKGYKQYWCTFKDTSISCYKSREESSGTPAHQLNLRGCEVTPDVNISGQKFNIKLLIPVAEGMNEIWLRCDNEKQYAHWMAACRLASKGKTMADSSYNLEVQNILSFLKMQHLNPDPQLIPDQITTDVNPECLVSPRYLKKYKSKQITARILEAHQNVAQMSLIEAKMRFIQAWQSLPEFGITHFIARFQGGKREELIGIAYNRLIRMDASTGDAIKTWRFSNMKQWNVNWEIKMVTVEFADEVRLSFICTEVDCKVVHEFIGGYIFLSTRAKDQNESLDEEMFYKLTSGWV
Protein: Rapamycin-insensitive companion of Tor, isoform C (X2JFR5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MWPYYSFIKVSQDPEDFYRLDPQRSAAENAFEIYSMLCLEETRDTKRLFLLNALASLCLGARKGSHHSNIRFTTEELLYCLSASLVHTFTQVRAAALRTIRYAISTPNDIKTFNALQLQHLLCRSIDLMLKNDDERVQALKLVRKMLAIAPEDISPAVVRCLVSLADSGIEENDNLLRACLATLAEFAVLNPALLIVCGGVTSITRNVLECHNPRIAESLCGVLLYLLEWPQTRNICGVRLDCLAAPYCDFTYRQSIVDKNKDARELRYTSCRLALLSVLRSWTGTLEFCDPSKPSGLKAIVDALYLNQIEVRKAILDLLYELLTLPQPTWTDDYAVALQAVDPSDFQDTWLLSNGFVSAEGRSILPTLAARAPSVVEQHLALMLYCFLETGLLNALVEVVVSSDQFVSVQATVLIGKILQLMHTHLPPDICCTSPALPTLVSHATLGNQQANAAVAALQNYQKLLRQRPASRSLFLDSIIQGGALIQTRLFRRHLNVQEQAGPVLQLQETAEAAAFAVPPVTQFRGTLDRSRLDSVSSSDESNSQASTSSRSSFRLKRKFLPQALYDNFRAFNRLLTDSRVLSQADAHLWDWDVITTILKSNLIRKLDYTQGKFLKRLVDFYKPRNNRFSHQDLVPGQRLPTYVSAGLDLIDVLLSSNELECMRFITDYFSDISQQLAAVTTSNRAHDCLFSPQHMNNTMCQQYFLYIGRMCRTVKGIEVLKNTTVFEYLINLVRVTDHVCYVKLIVSGLNYSYEKLPRQVLEKALTSAKTRGRLYSTQFMAVLLRARLPHFEVWGIPLIINQTRDSDRSVGLAAMDVLEEACHDKYYLEEIVSRWPNLTHRGDAGRLLMARYYSLPRGLNSTMARIEDEIRYWRNGYNKRYVLLVEADTHSSLTLHIRNEDGYYSRRNCNQRPQTVPPNVAPHLYGQMAQTGQGMTALRKHGDLPQLLELLRRAKCTDDAECLELKAAIWALAHASTHSNGIEYFVELNARLYEKLIVLVTKCEVYSVRATCFSALGLIAGTQAGANILFKLNWLSVRHDKNTMWPVHQPEDWMSSQYTPVRHYYEDVPADNMTMMDDYIERFYETGSDFWHMLADQTDASGGGGGVAGTVVGMHPIVQDPNATITTTDSVRTTTDDVHPRMLVGVAAKSKTLPEGSNLRQGKHQRSLSESKTTDVISLLGSGVGTMSGAVLYPTPYQHRIRYNSCTDSNTSGVSSCESVTGRTAAAYAAAANELQQFPLSPIPSMSNLLESDELFRRNQLATSMLPSTLSPMAMKGYVQLRSLRKHSRPVFSESSAEFYDFAEILDTPEVQMRKLDWTHSHRRLKVRSLDRQLSDVYRRLSADELNVLLPTLNAPKFLPPNDLKGPCYAGICLPKNVLDLFPTRNLSRTYVSRDIQDQDIVGINLLNTMLRPQCLNDSLTNEGGDESSVISSLSDVSSASRRQTRQLQQGAKHSRSLCLHCARSPRQQRNDSGSHSNGGGGASLAPCELYSSAAAALVAAGIQAGPVLAKKSGSSAQGASAALGADISFHSPESMLSEDSLPDRLTASILYNVQRLANPVSAKQSKMALLELKQKHPHAFQDICLYSEACKTIGRSSYRMIARRFLQELFLDLNFDSFYVEPQLIIGARKFSAEEKAEATAPTAMQAMPFKQTILKPKPAAQLASVYETSWENLLMDQSPRINKSSPADQPANAQTKAKARNQLHIDDTESSLSSTDGENDSGEDVCDGSGAGTQASSVTTAHTALPTGNSNRSSIGTCTASQLVPGAATSNSAGAGTSASDNASTSLKNENRQFTRGRFYTLELDLSCTKNKFPIKNRSQRTPTPPPIESLIESKPTVQTDVNTSALPIMQRTGGSNDSSSALRYSTVTKSLSASMARPVGSLYCEKRLQSSKSEAVLDEVAKARRASGGVGLTTVRDNS
Protein: Helix-loop-helix DNA-binding domain containing protein (Q2QML8)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MAFMNRQDPEASGFFSDDDSGQTAAIAAAAAMENEDFSYMLREFDYYTSSEDLFELMWQGGGGGGASSFDQPPPPVSYHRLSPPPPAMGTTTTTLLPEQPLVDDHHLPAAAAAPPSEEEMAAWLYPIVSGHEVAGGGWRSPEAQDDRRAAPAPEKKQMEKMPAAASPTTTMNKDETSDDSGERKKKKASSAAGKSKQASPRGCRSSQPYRKSGDSIDELFTKFHRRRFKITERFRTLQRLVPGCDKSNQASTLDQTIQYMKSLQHQLKAMSVVGSPPALLYPAAVHPQSYMHPPPPPPPVTMPMHPGMVLAAPPPGAAPPPGPPAMVPFGAMLPYPPYPAVLLPPPAAATLYGRPPAPAPGVAARRHGSSGGGRISKSSSSSLCKKL
Protein: Cytochrome P450 1A (EC 1.14.14.1) (B8JKD5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368045}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368045}. Microsome membrane {ECO:0000256|RuleBase:RU368045}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368045}.
Interaction partners:
- Epoxide hydrolase
- Indoleamine 2,3-dioxygenase 1.
- Very-long-chain 3-oxoacyl-CoA reductase-A
- Estradiol 17-beta-dehydrogenase 1
- Very-long-chain 3-oxoacyl-CoA reductase-B
- FabG like.
- Transmembrane O-methyltransferase homolog
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Cytochrome P450 1A
- Catechol O-methyltransferase A
Sequence:
MMDVLLALRDLLQLSTRSVLLSLMVCLMLMFRRRQLVPGPFSWPVIGNAAQLGNTPHFYFSRMAQKYGDVFQIKLGSRNVVVLNGDAIKEALVKKATDFAGRPDFASFRFVSNGKSMAFGNYTPWWKLHRKVAQSTVRNFSTANIQTKQTFEKHIVSEIGELIRLFLNKSREQQFFQPHRYLVVSVANTMSAVCFGNRYAYDDAEFQQVVGRNDQFTKTVGAGSMVDVMPWMQYFPNPIRTLFDQFKELNKEFCAFIELKVSEHRKTISPSHVRDMTDAFIVALDKGLSGGSGVSLDKEFVPPTISDIFGASQDTLSTALQWIILLLVRYPEIQKRLQEDVDRVVDRSRLPTIADQPHLPYLMAFIYEVMRFTSFTPLTIPHSTTKDTSINGYPIPKDTVIFVNQWSLNHDPTKWDQPEVFNPQRFLDEDGSLNKDLTTNVLIFSLGKRRCIGEDVSKIQLFLFTSVLVHQCSFKAESTPNMDYEYGLTLKPKPFKVSVTARDSSDLLDSLVGTSQTPTEKRQKCD
Protein: Uncharacterized protein (Q54DL1)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPNIQDPLLGKAFQVKNNHNIVNSLLVSFGTLLIYIVYYFSSDQFNLSELTHDGIIKQYIYYGMLLTACFISPITVSLLSEKITMVLSSLVITIIFILNYFKITLFSMIIKIISIFTIEILWTAVGAFLIVLSTRSNISLNFGIFFSIFGLYLGFYSIYLNLTTDLLYFTIFSIFIGLAIILYFMLDGKNNQEIQEIEIENNNGSGILTSINIIGNARFYYVIPSLFYIGFSNFFLKLVLELISLKATTTNTQPINYYNLIEVYSISFSLISFIWGCMILYKNKTNATVNENPIIVVSIIGAFGIIASLICLVISYNQDKYIYGSNCSIYLSIILFSLVDSIFSIQIYTSLGTLFENKALSIIASIRIIQYIGSLFAYTLVTWISASFVVGFYLLASLLLLSCFTLYTHLYNNNDN
Protein: C-type lectin 35 kDa subunit (C-type lectin 30 kDa subunit) (Q9PRY2)
Organism: Petromyzon marinus (Sea lamprey)
Function: Calcium-dependent lectin involved in innate immune defense. Binds mannose residues on the surface of the Gram-negative bacterium A.salmonicida. Shows agglutinating activity towards horse erythrocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:18937980}.
Interaction partners:
Sequence:
XWSCTKGCPDAKQCEAT
Protein: Spondin-2 (Mindin) (Q8BMS2)
Organism: Mus musculus (Mouse)
Function: Cell adhesion protein that promotes adhesion and outgrowth of hippocampal embryonic neurons. Binds directly to bacteria and their components and functions as an opsonin for macrophage phagocytosis of bacteria. Binds bacterial lipopolysaccharide. Essential in the initiation of the innate immune response and represents a unique pattern-recognition molecule in the ECM for microbial pathogens.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:14691481}.
Interaction partners:
Sequence:
MENVSLALGRALWVFLLAMIGSTTSQPLGGESVCTARPLARYSITFIGKWSQTAFPKQYPLFRPPAQWSSLLGAAHSSDYSMWRKNEYVSNGLRDFAERGEAWALMKEIEAAGEKLQSVHAVFSAPAIPSGTGQTSTELEVHPRHSLVSFVVRIVPSPDWFVGIDSLDLCEGGRWKEQVVLDLYPHDAGTDSGFTFSSPNFATIPQDTVTEITASSPSHPANSFYYPRLKSLPPIAKVTFVRLQQSPRAFAPPSLDLASRGNEIVDSLSVPETPLDCEVSLWSSWGLCGGPCGKLGAKSRTRYVRVQPANNGTPCPELEEEAECAPDNCV
Protein: Large ribosomal subunit protein P2 (60S acidic ribosomal protein P2) (P22683)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Plays an important role in the elongation step of protein synthesis.
Interaction partners:
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein eS30
- Large ribosomal subunit protein P1
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS9
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein eS19
Sequence:
MKYLAAYLLASLSGNANAASVTKILQSVGVEVDAARVESVCKELDGKDVQALIAAGKSKVGSVAAAAAPAAATSAAPAAAAAAPAKKVVEEKKEESDDDMGMGLFD
Protein: Polybromo 1 (A0A8I5ZMW9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSKRRRATSPSSSVSGDFDDGHHSVPTPGPSRKRRRLSSLPTVDPIAVCHELYNTIRDYKDEQGRLLCELFIRAPKRRNQPDYYEVVSQPIDLMKIQQKLKMEEYDDINLLTADFQLLFNNAKAYYKPDSPEYKAACKLWDLYLRTRNEFVQKGEADDEDDDEDGQDNQGTMADGSSPGYLKEILEQLLEAIVVATNPSGRLISELFQKLPSKVQYPDYYAIIKEPIDLKTIAQRIQNGSYKSIHAMAKDIDLLAKNAKTYNEPGSQVFKDANSIKKIFYMKKAEIEHHEMTKSSLRIRTATNLAAARLTGPSHNKSSLDEERNPTSKCYRNKRAVQGGRLSAITMALQYGSESEEDAALAAARYEEGESEAESITSFMDVSNPFHQLYDTVRSCRNNQGQLIAEPFFHLPSKKKYPDYYQQIKMPISLQQIRTKLKNQEYETLDHLECDLNLMFENAKRYNVPNSAIYKRVLKLQQVMQAKKKELARRDDIEDGDSMISSATSDTGSAKRKRNTHDSEMLGLRRLSSKKNIRKQRMKILFNVVLEAREPGSGRRLCDLFMVKPSKKDYPDYYKIILEPMDLKIIEHNIRNDKYAGEEGMMEDMKLMFRNARHYNEEGSQVYNDAHILEKLLKDKRKELGPLPDDDDMASPKLKLSRKSGVSPKKSKYMTPMQQKLNEVYEAVKNYTDKRGRRLSAIFLRLPSRSELPDYYLTIKKPMDMEKIRSHMMANKYQDIDSMVEDFVMMFNNACTYNEPESLIYKDALVLHKVLLETRRDLEGDEDSHVPNVTLLIQELIHNLFVSVMSHQDDEGRCYSDSLAEIPAVDPNFPSRPPLTFDIIRKNVESNRYRRLDLFQEHMFEVLERARRMNRTDSEIYEDAVELQQFFIRIRDELCKNGEILLSPALSYTTKHLHNDVEKEKKEKLPKEIEEDKLKREEEKREAEKSEDSSGTTGLSGLHRTYSQDCSFKNSMYHVGDYVYVEPAEANLQPHIVCIERLWEDSAGEKWLYGCWFYRPNETFHLATRKFLEKEVFKSDYYNKVPVSKILGKCVVMFVKEYFKLCPETFRDEDVFVCESRYSAKTKSFKKIKLWTMPISSVRFVPRDVPLPVVRVASVFANADKGDEEKSTDNSDDNRAEDSFNLEKEKEDVPVEMSNGEPGCHYFEQLRYNDMWLKVGDCVFIKSHGLVRPRVGRIEKVWVRDGAAYFYGPIFIHPEETEHEPTKMFYKKEVFLSNLEETCPMSCILGKCAVLSFKDFLSCRPTEIPENDILLCESRYNESDKQMKKFKGLKRFSLSAKVVDDEIYYFRKPIIPQKEPSPLLEKKIQLLEAKFAELEGGDDDTEEMGEEDSEVIEPPSLPQLQTPLANELDLMPYTPPQSTPKSAKGSAKKESSKRKINMSGYILFSSEMRAVIKAQHPDYSFGELSRLVGTEWRNLETAKKAEYEERAAKAAEQQERERAAQQQQPSASPRAGTPVGALMGVVPPPTPMGMLNQQLTPVAGMMGGYPPGLPPLQGPVDGLVSMGSMQPLHPGGPPPHHLPPGVPGLPGIPPPGVMNQGVTPMVGTPAPGGSPYGQQVGVLGPPGQQAPPPYPGPHPTGPPVIQQPTTPMFVAPPPKTQRLLHSEAYLKYIEGLSAESNSISKWDQTLAARRRDVHLSKEQESRLPSHWLKSKGAHTTMADALWRLRDLMLRDTLNIRQAYNLENV
Protein: Salicyloyl-CoA 5-hydroxylase (EC 1.14.13.209) (Q7X281)
Organism: Streptomyces sp
Function: Involved in the degradation of salicylate via a pathway involving coenzyme A derivative. Catalyzes the aromatic hydroxylation of salicylyl-CoA to yield gentisyl-CoA.
Interaction partners:
Sequence:
MKVACIGAGPGGLFFATLLKRSRPDAEVVVFERNRPDDTFGFGVVFSDATLDAIDAADPVLSEALEKHGRHWDDIEVRVHGERERVGGMGMAAVVRKTLLSLLQERARAEGVQMRFQDEVRDPAELDDFDLVVVCDGANSRFRTLFADDFGPTAEVASAKFIWFGTTYMFDGLTFVHQDGPHGVFAAHAYPISDSLSTFIVETDADSWARAGLDAFDPATPLGMSDEKTKSYLEDLFRAQIDGHPLVGNNSRWANFATRRARSWRSGKWVLLGDAAHTAHFSVGSGTKMAMEDAVALAETLGEASRSVPEALDLYEERRRPKVERIQNSARPSLSWWEHFGRYVRSFDAPTQFAFHFLTRSIPRGKLAVRDAAYVDRVDGWWLRHHEAGPLKTPFRVGPYRLPTRRVTVGDDLLTGTDGTGIPMVPFSGQPFGAGVWIDAPDTEEGLPLALDQVRETAEAGVLLVGVRGGTALTRVLVAEEARLAHSLPAAIVGAYDDDTATTLVLSGRADLVGGTK
Protein: Acyl-coenzyme A thioesterase THEM4 (Acyl-CoA thioesterase THEM4) (EC 3.1.2.2) (Carboxyl-terminal modulator protein) (Thioesterase superfamily member 4) (Q3UUI3)
Organism: Mus musculus (Mouse)
Function: Has acyl-CoA thioesterase activity towards medium and long-chain (C14 to C18) fatty acyl-CoA substrates, and probably plays a role in mitochondrial fatty acid metabolism (By similarity). Plays a role in the apoptotic process, possibly via its regulation of AKT1 activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q5T1C6}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q5T1C6}. Cytoplasm {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion {ECO:0000269|PubMed:19421406}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5T1C6}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q5T1C6}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q5T1C6}. Note=Released from the mitochondria into the cytosol in response to apoptotic stimuli. {ECO:0000250|UniProtKB:Q5T1C6}.
Interaction partners:
- RAC-alpha serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- RAC-gamma serine/threonine-protein kinase
- Acyl-coenzyme A thioesterase 3
- Peroxisomal succinyl-coenzyme A thioesterase
- Acyl-coenzyme A thioesterase 5
- Acyl-coenzyme A thioesterase 2, mitochondrial
- Cytosolic acyl coenzyme A thioester hydrolase
- Acyl-coenzyme A thioesterase 1
- Acyl-coenzyme A thioesterase THEM5
Sequence:
MLRNCAMRLRTLGATPARRPGAARRLFSSEKVIRKDYALPNPSWTKDLRLLFDQFMKKCEDGSWKRMPSHRQNPTRAIQEFQTLFVDSKFKKEEQMSKAQQFTRSFEEGLGFEYAMFYNKVEKRTVSLFQGGLHLQGVPGFVHGGAIATIIDVTTGTCAISEGVAMTANLNITYKKPIPLLSVVVVNSQLQKIEGRKLFVSCTIQSIDEKTLYTEATALFIKLDPEKPLT
Protein: Protein EARLY RESPONSIVE TO DEHYDRATION 15 (PAM2-containing protein CID1) (Polyadenylate-binding protein-interacting protein 1) (PABP-interacting protein 1) (Poly(A)-binding protein-interacting protein 1) (Protein CTC-INTERACTING DOMAIN 1) (Protein LIGHT STRESS-REGULATED 1) (Q39096)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Central component of stress responses that interacts with poly(A)-binding proteins. Negative regulator of abscisic acid (ABA) responses, including resistance to drought and freezing as well as stomatal closure regulation. Mediates resistance to the bacterial necrotroph pathogen Erwinia carotovora subsp. carotovora and promotes the induction of marker genes for systemic acquired resistance (SAR).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:11683875}.
Interaction partners:
- Polyadenylate-binding protein-interacting protein 11
- Polyadenylate-binding protein-interacting protein 13
- Polyadenylate-binding protein-interacting protein 7
- Polyadenylate-binding protein-interacting protein 5
- Polyadenylate-binding protein-interacting protein 12
- Polyadenylate-binding protein-interacting protein 3
- Polyadenylate-binding protein-interacting protein 8
- Polyadenylate-binding protein-interacting protein 6
- Polyadenylate-binding protein-interacting protein 4
- At3g56320
Sequence:
MAMVSGRRSTLNPDAPLFIPAAVRQVEDFSPEWWQLVTTSTWYPDYWISQQQQGADGFYDNGENENGGGHIDVADLLPESFDFDDMEDFFDTDAAEFDQGFDGRMYYQAPSEFGFGKNGEMVKKSSGNRSPRSIVEPAKYAEKPAKWGNQRVAAAPRNIHQPR
Protein: Neuromodulin (Axonal membrane protein GAP-43) (Growth-associated protein 43) (Q5U058)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU368113}; Peripheral membrane protein {ECO:0000256|RuleBase:RU368113}; Cytoplasmic side {ECO:0000256|RuleBase:RU368113}. Cell projection, growth cone membrane {ECO:0000256|ARBA:ARBA00004503, ECO:0000256|RuleBase:RU368113}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004503, ECO:0000256|RuleBase:RU368113}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004503, ECO:0000256|RuleBase:RU368113}. Synapse {ECO:0000256|ARBA:ARBA00034103, ECO:0000256|RuleBase:RU368113}. Cell projection, filopodium membrane {ECO:0000256|ARBA:ARBA00004516, ECO:0000256|RuleBase:RU368113}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004516, ECO:0000256|RuleBase:RU368113}. Perikaryon {ECO:0000256|ARBA:ARBA00004484, ECO:0000256|RuleBase:RU368113}. Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279, ECO:0000256|RuleBase:RU368113}. Cell projection, axon {ECO:0000256|RuleBase:RU368113}. Cytoplasm {ECO:0000256|RuleBase:RU368113}. Note=Cytoplasmic surface of growth cone and synaptic plasma membranes. {ECO:0000256|RuleBase:RU368113}.
Interaction partners:
Sequence:
MLCCMRRTKQVEKNDDDQKIEQDGIKPEDKAHKAATKIQASFRGHITRKKLKGEKKDDVQAAEAEANKKDEAPVADGVEKKGEGTTTAEAAPATGSKPDEPGKAGETPSEEKKGEGDAATEQAAPQAPASSEEKAGSAETESATKASTDNSPSSKAEDAPAKEEPKQADVPAAVTAAAATTPAAEDAAAKATAQPPTETGESSQAEENIEAVDETKPKESARQDEGKEEEPEADQEHA
Protein: Glutathione peroxidase 1 (EC 1.11.1.9) (O02621)
Organism: Caenorhabditis elegans
Function: May constitute a glutathione peroxidase-like protective system against oxidative stresses.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Thioredoxin domain-containing protein
- Glutathione reductase, mitochondrial
- Glutathione peroxidase 3
- Thioredoxin domain-containing protein
- Glutathione peroxidase
- Thioredoxin
- Glutathione synthetase
- Glutathione peroxidase
- Thioredoxin domain-containing protein
- Glutathione peroxidase 2
Sequence:
MSSVYDFNVKNANGDDVSLSDYKGKVLIIVNVASQCGLTNKNYTQLKELLDVYKKDGLEVLAFPCNQFAGQEPSCEIDIQAFVADKFKFEPTLFQKIDVNGDKQSPLFKFLKNEKGGFMFDAIKWNFTKFLVGRDGKIIKRFGPTTDPKDMEKDIKEALGEKL
Protein: Cinnamyl alcohol dehydrogenase 5 (AtCAD5) (EC 1.1.1.195) (Cinnamyl alcohol dehydrogenase D) (O49482)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in lignin biosynthesis in the floral stem. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.
Interaction partners:
- Cinnamoyl-CoA reductase 2
- Cinnamoyl-CoA reductase 1
- Flavone 3'-O-methyltransferase 1
- Cytochrome P450 84A1
- Aldehyde dehydrogenase family 2 member C4
- F5F19.5 protein
- GLYCINE RICH PROTEIN 9
- Caffeoyl-CoA O-methyltransferase 1
- Trans-cinnamate 4-monooxygenase
- 4-coumarate--CoA ligase 1
Sequence:
MGIMEAERKTTGWAARDPSGILSPYTYTLRETGPEDVNIRIICCGICHTDLHQTKNDLGMSNYPMVPGHEVVGEVVEVGSDVSKFTVGDIVGVGCLVGCCGGCSPCERDLEQYCPKKIWSYNDVYINGQPTQGGFAKATVVHQKFVVKIPEGMAVEQAAPLLCAGVTVYSPLSHFGLKQPGLRGGILGLGGVGHMGVKIAKAMGHHVTVISSSNKKREEALQDLGADDYVIGSDQAKMSELADSLDYVIDTVPVHHALEPYLSLLKLDGKLILMGVINNPLQFLTPLLMLGRKVITGSFIGSMKETEEMLEFCKEKGLSSIIEVVKMDYVNTAFERLEKNDVRYRFVVDVEGSNLDA
Protein: Uncharacterized protein C664.13 (Q9US01)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDLEELQKIIQEEQIRCEREIAEAAEARNSSNSLIVVDEYSKESEDVLENGLEHVQSNEFTESEDYKSIERSLAVTEAVMARFEKEMGSLRDQMNFFHQILDNDNLDGFLTGSSKPC
Protein: Glycine-rich domain-containing protein 1 (AtGRDP1) (Q9ZQ47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a regulatory role in abscisic acid (ABA) signaling and tolerance to abiotic stress during germination. May be involved in the regulation of the ABI transcriptional factors.
Interaction partners:
- Protein kinase superfamily protein
- F19P19.6 protein
- AT4G01090 protein
- Protein C2-DOMAIN ABA-RELATED 2
- Protein ROOT HAIR DEFECTIVE 3 homolog 2
- Defensin-like protein 199
- UNC93-like protein 1
- Putative methylesterase 14, chloroplastic
- Tetraspanin-19
- PRA1 family protein D
Sequence:
MDKEKDHEVEWLEAQKIEISVDLLAAAKQHLLFLETVDRNRWLYDGPALEKAIYRYNACWLPLLVKYSESSSVSEGSLVPPLDCEWIWHCHRLNPVRYNSDCEQFYGRVLDNSGVLSSVDGNCKLKTEDLWKRLYPDEPYELDLDNIDLEDISEKSSALEKCTKYDLVSAVKRQSPFYYQVSRSHVNSDIFLQEAVARYKGFLYLIKMNRERSLKRFCVPTYDVDLIWHTHQLHPVSYCDDMVKLIGKVLEHDDTDSDRGKGKKLDTGFSKTTAQWEETFGTRYWKAGAMHRGKTPVPVTNSPYASDVLVKDPTAKDDFQNLIQFPEVEVVEVLLEIIGVRNLPDGHKGKVSVMFSKTQPDSLFNAERRLTILSEVGEKQVATFQCEPTGELVFKLISCSPSKIPVSREPKNLGFASLSLKEFLFPVITQLSVEKWLELTPSKGSQTDTKPISLRVAVSFTPPVRSPSVLHMVQSRPSCKGSCFFPIIGKSRLAKSSTHIVDETQTEVITLQIRNSADGGILKDDQRQVMGVTDSGETRVLAVYTGSFWSLLDSKWSLKQINASTADNPLFEILGPRVVKIFSGRKLDYEPKHCANLRSDLDFMTLVEFSKQHPYGKTVGLVDMRFGSIEAKENWLLLPGIVSAFILHTVLKKGGSEGFNVTTKDIKEESKQTKLVAATENNVNANSTNVETQTAITAPKKGSGCGGGCSGECGNMVKAANASGCGSSCSGECGDMVKSAANASGCGSGCSGECGNMVKAANASGGGYGARCKAAKASGCGGGCGGGCGGGCGDMVKSVNASGCGGGCNGECGNMVKAA
Protein: Uncharacterized protein T27F2.1 (Q22836)
Organism: Caenorhabditis elegans
Interaction partners:
- TPR_REGION domain-containing protein
- Pre-mRNA-splicing factor SYF1
- Protein BUD31 homolog
- Pre-mRNA-splicing factor RBM22
- Cell division cycle 5-like protein
- Pleiotropic regulator 1
- Spliceosome-associated protein CWC15 homolog
- Tr-type G domain-containing protein
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Cullin-1
Sequence:
MSMKLRDILPAPVAADEAASQIRRDPWFGGRDNEPSAALVSKEPPPYGKRTSFRPRGPEDFGDGGAFPEIHVAQFPLGLGLGDMRGKPENTLALQYGTDGKLQHDAIARIGHVKDKVVYSKLNDMKAKTWNEDDDDIQKPDDDAVIDATEKTRMALEKIVNSKVASALPVRHADKLAPAQYIRYTPSQQNGAAGSQQRIIRMVEEQKDPMEPPKFKINQKIPRAPPSPPAPVMHSPPRKMTAKDQNDWKIPPCISNWKNPKGFTVGLDKRLAADGRGLQQTHINENFAKLADALYIADRKAREEVETRAQLERRVAQNKKSEQEAKMAEAAAKARQERSAMRRKDDEDDEQVKVREEIRRDRLDDIRKERNIARSRPDKADKLRKERERDISEKIVLGLPDTNQKRTGEPQFDQRLFDKTQGLDSGAMDDDTYNPYDAAWRGGDSVQQHVYRPSKNLDNDVYGGDLDKIIEQKNRFVADKGFSGAEGSSRGSGPVQFEKDQDVFGLSSLFEHTKEKKRGGDGGDSRGESKRSRRD