wanglab/gogpt-training-data huggingface dataset:
Protein: F-box only protein 38 (Q6PIJ6)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of PDCD1/PD-1, thereby regulating T-cells-mediated immunity. Required for anti-tumor activity of T-cells by promoting the degradation of PDCD1/PD-1; the PDCD1-mediated inhibitory pathway being exploited by tumors to attenuate anti-tumor immunity and facilitate tumor survival. May indirectly stimulate the activity of transcription factor KLF7, a regulator of neuronal differentiation, without promoting KLF7 ubiquitination (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8BMI0}. Nucleus {ECO:0000250|UniProtKB:Q8BMI0}. Note=Accumulates predominantly in the cytosol. Exported from the nucleus in a XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:Q8BMI0}.
Interaction partners:
- Krueppel-like factor 7
- Ribonuclease inhibitor
- Cullin-1
- Trafficking protein particle complex subunit 11
- Protein MON2 homolog
- Ubiquitin carboxyl-terminal hydrolase 7
Sequence:
MGPRKKSVKTCIMNNEIPEEMTADETKDYMNQLSHEVLCHIFRYLPLQDIMCMECLSRKLKEAVTLYLRVVRVVDLCAGRWWEYMPSGFTDASFLTLLKKMPDVEQLYGLHPRYLERRRVRGHEAFSIPGVLEALQACPNLVGVETSHLELVESIWTYMPHVHILGKFRNRNGAFPIPPENKLKIPIGAKIQTLHLVGVNVPEIPCIPMLRHLYMKWVRLTKPQPFKDFLCISLRTFVMRNCAGPTNSLKYVPLVTGLASARNLEHLEMVRVPFLGGLIQHVVEDSWRSGGFRNLHTIVLGACKNALEVDLGYLIITAARRLHEVRIQPSLTKDGVFSALKMAELEFPQFETLHLGYVDEFLLQSRMANADLVKYGLADVVENPGIITDIGMKAVNEVFSCIKYLAIYNCPHLHNPYNWISDHSRWTRLVDINLVRCHALKLDSFGQFIELLPSLEFISLDQMFREPPKGCARVGLSAGTGIGVSSALVSNQNSNNDDNNAQNNNANIHDNNHHHPDDSDEENDFRQDLQPGEQQFAADALNEMEDIVQEDGEVVAESGNNTPAHSQAIIPVDVDEEQAGPSGLQRVVKPTSITVHDSESDDEEDSLELQEVWIPKNGTRRYSEREEKTGESVQSRELSVSGKGKTPLRKRYNSHQMGQSKQFPLEESSCEKGCQVTSEQIKADMKAARDIPEKKKNKDVYPSCSSTTASTVGNSSSHNTASQSPDFVRTVNSGGSSEPSPTEVDVSRQCACSPGGSEDSEAMEEGDAESSVCPRCCCHRPQESQRRTSRCSDEERPSTSRACVVNGPDGTRSAFSFRTLPQGGSSGPAHDERTNGSGSGATGEDRRGSSQPESCDVQSNEDYPRRPLTRARSRLSHVLLVSESEVAKTKPRHAMKRKRTADKSTSTSDPVIEDDHVQVLVLKSKNLVGVTMTNCGITDLVLKDCPKMMFIHATRCRVLKHLKVENAPIVNRFDYAQCKKLNMDQVLDQILRMPPERNRIIYLRPMQQVDTLTLEQKLFSGPYPYHICIIHEFSNPPNVRNKVRIRSWMDTIANINQELIKYEFFPEATRSEEDLKKYPKYPWGREIYTLEGVVDGAPYSMISDFPWLRSLRAAEPNSFARYDFEDDEESTIYAPRRKGQLSADICMETIGEEISEMRQMKKGVFQRVVAIFIHYCDVNGEPVEDDYI
Protein: Protein OXIDATIVE STRESS 3 LIKE 3 (AtO3L3) (Q29PZ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Promotes slightly the tolerance to oxidizing chemicals (e.g. diamide).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9LVB9}.
Interaction partners:
- Putative RRM-containing protein family protein)
- Ternary complex factor MIP1 leucine-zipper protein
- AAA-ATPase At5g17760
- Protein RALF-like 31
- Nuclear polyadenylated RNA-binding protein
- LIMR family protein At5g01460
- ADP-ribosylation factor-like protein 8c
- CASP-like protein 5A2
- Small ribosomal subunit protein uS19w
- UDP-glycosyltransferase 76E4
Sequence:
MHYQEQMESLMLGEERRRGNYTRDVDADADEGVNSPSSFPNSPDDSDRRSSSSSSRRGLSKHYKGKSQSFTTLAEALTVEDLAKPENPFNAKLKQRRESPHCRRLSGCGGASERNLSVHDVFLAGNDRPPRLSGNRPPPRAQTLSAAHISALLTRT
Protein: Glycylpeptide N-tetradecanoyltransferase 1 (EC 2.3.1.97) (Myristoyl-CoA:protein N-myristoyltransferase 1) (HsNMT1) (NMT 1) (Type I N-myristoyltransferase) (Peptide N-myristoyltransferase 1) (Protein-lysine myristoyltransferase NMT1) (EC 2.3.1.-) (P30419)
Organism: Homo sapiens (Human)
Function: Adds a myristoyl group to the N-terminal glycine residue of certain cellular and viral proteins. Also able to mediate N-terminal lysine myristoylation of proteins: catalyzes myristoylation of ARF6 on both 'Gly-2' and 'Lys-3'. Lysine myristoylation is required to maintain ARF6 on membranes during the GTPase cycle.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9353336, ECO:0000269|PubMed:9506952}. Cytoplasm, cytosol {ECO:0000269|PubMed:9353336}. Membrane {ECO:0000269|PubMed:9506952}; Peripheral membrane protein {ECO:0000269|PubMed:9506952}. Note=Copurifies with ribosomes. {ECO:0000269|PubMed:9353336}.
Interaction partners:
- Acyl-CoA-binding domain-containing protein 6
- Guanine nucleotide-binding protein G
- BH3-interacting domain death agonist
Sequence:
MADESETAVKPPAPPLPQMMEGNGNGHEHCSDCENEEDNSYNRGGLSPANDTGAKKKKKKQKKKKEKGSETDSAQDQPVKMNSLPAERIQEIQKAIELFSVGQGPAKTMEEASKRSYQFWDTQPVPKLGEVVNTHGPVEPDKDNIRQEPYTLPQGFTWDALDLGDRGVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLPQWHCGVRVVSSRKLVGFISAIPANIHIYDTEKKMVEINFLCVHKKLRSKRVAPVLIREITRRVHLEGIFQAVYTAGVVLPKPVGTCRYWHRSLNPRKLIEVKFSHLSRNMTMQRTMKLYRLPETPKTAGLRPMETKDIPVVHQLLTRYLKQFHLTPVMSQEEVEHWFYPQENIIDTFVVENANGEVTDFLSFYTLPSTIMNHPTHKSLKAAYSFYNVHTQTPLLDLMSDALVLAKMKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWKCPSMGAEKVGLVLQ
Protein: Dimethylsulfoniopropionate demethylase DmdA (EC 2.1.1.269) (Q5LS57)
Organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi)
Function: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating demethylation of dimethylsulfonioproprionate (DMSP) to methyl-mercaptopropionate (MMPA). The intracellular concentration of DMSP is estimated to be 70 mM.
Interaction partners:
- 3-methylmercaptopropionyl-CoA ligase
- Glycine cleavage system H protein
- DMSP lyase
- Acrylyl-CoA reductase AcuI
Sequence:
MASIFPSRRVRRTPFSAGVEAAGVKGYTVYNHMLLPTVFDSLQADCAHLKEHVQVWDVACERQVSIQGPDALRLMKLISPRDMDRMADDQCYYVPTVDHRGGMLNDPVAVKLAADHYWLSLADGDLLQFGLGIAIARGFDVEIVEPDVSPLAVQGPRADDLMARVFGEAVRDIRFFRYKRLAFQGVELVVARSGWSKQGGFEIYVEGSELGMPLWNALFAAGADLNVRAGCPNNIERVESGLLSYGNDMTRENTPYECGLGKFCNSPEDYIGKAALAEQAKNGPARQIRALVIGGEIPPCQDAWPLLADGRQVGQVGSAIHSPEFGVNVAIGMVDRSHWAPGTGMEVETPDGMRPVTVREGFWR
Protein: Vacuolar protein sorting-associated protein 45 homolog (AtVPS45) (Protein BFA-VISUALIZED ENDOCYTIC TRAFFICKING DEFECTIVE 2) (O49048)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the protein transport to the vacuole, probably at the level of vesicle fusion at the trans-Golgi network (TGN) and not in transport from the TGN to the prevacuolar compartment, by promoting the recycling of vacuolar sorting receptors back to the TGN. Involved in early endosomal vesicle trafficking, particularly at the trans-Golgi-network/early endosome (TGN/EE) thus residing in early endocytic route. Together with BIG5/BEN1 required for polar PIN-FORMED (PIN) proteins localization, for their dynamic repolarization, and consequently for auxin activity gradient formation and auxin-related developmental processes (e.g. embryonic patterning, organogenesis and vasculature venation patterning). Necessary for pollen germination and for cell expansion. Binds syntaxins.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:10888666}; Peripheral membrane protein {ECO:0000269|PubMed:10888666}. Early endosome {ECO:0000269|PubMed:23737757}. Note=Binds to trans-Golgi network membranes through interaction with other proteins. {ECO:0000269|PubMed:10888666}.
Interaction partners:
- Tlg2p-like protein a
- Vesicle transport v-SNARE 12
- Syntaxin-42
- Syntaxin-61
- Syntaxin-43
- Vesicle transport v-SNARE 11
- Syntaxin-51
- Conserved oligomeric Golgi complex subunit 6
- Vesicle transport v-SNARE 13
- VAMP-like protein YKT62
Sequence:
MVLVTSVRDYINRMLQDISGMKVLILDSETVSNVSIVYSQSELLQKEVFLVEMIDSISVSKESMSHLKAVYFIRPTSDNIQKLRYQLANPRFGEYHLFFSNLLKDTQIHILADSDEQEVVQQVQEYYADFVSGDPYHFTLNMASNHLYMIPAVVDPSGLQRFSDRVVDGIAAVFLALKRRPVIRYQRTSDTAKRIAHETAKLMYQHESALFDFRRTESSPLLLVIDRRDDPVTPLLNQWTYQAMVHELIGLQDNKVDLKSIGSLPKDQQVEVVLSSEQDAFFKSNMYENFGDIGMNIKRMVDDFQQVAKSNQNIQTVEDMARFVDNYPEYKKMQGNVSKHVTLVTEMSKLVEARKLMTVSQTEQDLACNGGQGAAYEAVTDLLNNESVSDIDRLRLVMLYALRYEKENPVQLMQLFNKLASRSPKYKPGLVQFLLKQAGVEKRTGDLFGNRDLLNIARNMARGLKGVENVYTQHQPLLFQTMESITRGRLRDVDYPFVGDHFQQGRPQEVVIFMVGGTTYEESRSVALQNATNSGVRFILGGTAVLNSKRFLKDLEEAQRISRSGSHMV
Protein: UBX domain-containing protein 2A (UBX domain-containing protein 4) (Q99KJ0)
Organism: Mus musculus (Mouse)
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:26265139}. Endoplasmic reticulum {ECO:0000269|PubMed:26265139}. Perikaryon {ECO:0000269|PubMed:26265139}. Cell projection, dendrite {ECO:0000269|PubMed:26265139}. Nucleus {ECO:0000250|UniProtKB:P68543}. Cytoplasm {ECO:0000250|UniProtKB:P68543}. Note=Expressed at the axon initial segment. {ECO:0000269|PubMed:26265139}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- NSFL1 cofactor p47
- UBX domain-containing protein 10
- UBX domain-containing protein 6
- UBX domain-containing protein 8
- UBX domain-containing protein 1
- Tether containing UBX domain for GLUT4
- UBX domain-containing protein 4
- Small VCP/p97-interacting protein
- UBX domain-containing protein 7
Sequence:
MKEVDNLDSIKEEWACETGPPDSQPLNDNQQKDCEYFVDSLFEEAGKAGAKCLSPTEQKKQVDVNIKLWKNGFTVNDDFRSYSDGASQQFLNSIKKGELPSELWGIFDKEEVDVKVEDKKNEVCMSTKPVFQPFSGQGHRLGSATPRIVSKAKSVEVDNKSTLSAVSLNNLEPITRIQIWLANGERTVQRFNVSHRVSHIKDFIEKYQGSQRSPPFALATALPFLRFLDETLTLEEADLKNAVIIQRLQKTAEPFRKL
Protein: Probable calcium-binding protein CML26 (Calmodulin-like protein 26) (Q9C9U8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Potential calcium sensor.
Interaction partners:
- Probable calcium-binding protein CML48
- Probable calcium-binding protein CML49
- At2g03740
- GDSL esterase/lipase EXL6
- MLO-like protein 13
Sequence:
MANTNLESTNKSTTPSTDMELKKVFDKFDANGDGKISVSELGNVFKSMGTSYTEEELNRVLDEIDIDCDGFINQEEFATICRSSSSAVEIREAFDLYDQNKNGLISSSEIHKVLNRLGMTCSVEDCVRMIGHVDTDGDGNVNFEEFQKMMSSPELVKGTVANS
Protein: Antitoxin VapB27 (O07779)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Cognate toxin is VapC27. Upon expression in E.coli partially counteracts the ribonuclease activity of non-cognate toxins MazF6 and MazF9.
Interaction partners:
- Ribonuclease VapC27
- Putative antitoxin VapB1
Sequence:
MKAVVDAAGRIVVPKPLREALGLQPGSTVEISRYGAGLHLIPTGRTARLEEENGVLVATGETTIDDEVVFGLIDSGRK
Protein: Ion_trans_2 domain-containing protein (Q565B7)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVGMCPPTPERPIRRNYARMQYGEKKNIKHKLQQWFIENPSISARIRSCNVLIKLLTCILYCIRVVNDERSYPDDFPFSEEEAGKQDVTLYKYLLWVDFDFKIWFLQTMFACISMVYTILVFYLSYSGSVVRLLINIHFLLELITSFPFIISIFIPSLTYLYVPVFLNCWLAKGALQAMMNDLNRKSFISSSALFRQLLLLFSVLACLIFTGMCSIEHLQRARGKRIDLFTSFYFVMVTFSTVGYGDWYPDYWASQLCVVILICVALGLIPKQLDELGQTWSERQKSGTDFSSWNGVESHVVVTITTLEVEFIRDFLEEFYAHPENQRIQIVLLSPAELDNQTRMLLKIPLWNNRVHYVRGSSLRDEDLERANVATSKACFILSARHVNRKVATDEHTILRSWAIKDFAPNVKQYVQIFRAETKMHIEHAEVLICEDEFKYALLANNCICPGISTFITLLMHTSRGEEGQKSTEPWHKVYGFHSGNEMYQIKVQDSKFFCEYVGKSFSSTSFHAHKEYGIGLIAVSPDGDTSRMKLNPGSSHIIQPTDTVYYMGLTNEESLTDFRKGIRSQQKRANVASTIANIGTVAVDVPRSDKTELVGRKKKKRKEKAADEIHLIEVGEHVQSSRRPSIAMVTEGKIDSSSDSDQEEICDKCRGPCIQHKLQRTYPQVRTYIGTSNTVCHMMKERRSLCCLKLDEKCAHKSATSAHEYQWRNRPIILAADRTSSGMYNLVIPLRAYYRPVHDLHPIIILLELEEQDSLNDAFLDAISYFPDVYWMKGKVGNLDCLLRAGVSSAEHVVVVKETAVMAEEHTADCNTIITVQKIHRMFPRLRMITELTHATNMRFVQFNPHNAYSLAQSRFEKKERKRGSHMPFMFRLPFAQGGVFSANMLDRLLYQAIIKPFVVDLVRLLLGIDQHSDGGYLTSFVITSDDLWIRNYGRLYQKLCSSVADIPIGIFRTKKMDTKTVSLDLQEQCKDFENTEMGRNKDMYDHVKNRMRLLNIKDTHTLLEGSDEKSQISYVIINPAQDLELESGDIVYVIRSPIRKDATNARINPRRGLRRSKNVSETIDSTNQVPTIVIDENNL
Protein: Epoxyqueuosine reductase QueH (EC 1.17.99.6) (Queuosine biosynthesis protein QueH) (O24926)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Catalyzes the conversion of epoxyqueuosine (oQ) to queuosine (Q), which is a hypermodified base found in the wobble positions of tRNA(Asp), tRNA(Asn), tRNA(His) and tRNA(Tyr).
Interaction partners:
- S-adenosylmethionine:tRNA ribosyltransferase-isomerase
- Methyl-accepting chemotaxis protein
- Uncharacterized protein
Sequence:
MLIHICCSVDNLYFLKKAKEAFAGEKIVGFFYNPNIHPYSEYLLRLEDVKRTCEMLGIELLEGDYELEKFLDKAKGKELLGEKSERCFECFDLRLEASALKAFELGEEKFTTTLLTSPKKDPNQLIAKGQSIAQRHNLEFVVFRNDNFEHFKSELDLNLQALARENELYRQNYCGCQFALKIQKESQNRSPFELYSPLKRQILPASIEERTQVFRTLDMAKKDANKPFLAQKTIATYRLLNGGVWLSKNSNPLNCCILARSKSKAKVRINDLRWVFSQRLSVLVGYSQRDETLFLTLEGLNTLMAKNYDNLKELNLNPLNYEEELSLRALVSGSESINPIIVLEERTEKTLFVEIKSVFQEEKVFYLL
Protein: Aquaporin TIP1-1 (Aquaporin TIP) (Gamma-tonoplast intrinsic protein) (Gamma-TIP) (Tonoplast intrinsic protein 1-1) (AtTIP1;1) (Tonoplast intrinsic protein, root-specific RB7) (P25818)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Water channel required to facilitate the transport of water, diffusion of amino acids and/or peptides from the vacuolar compartment to the cytoplasm. Does not promote glycerol permeability. May play a role in the control of cell turgor and cell expansion. Its function is impaired by Hg(2+). May be involved in a vesicle-based metabolite routing through or between pre-vacuolar compartments and the central vacuole. Transports urea in yeast cells in a pH-independent manner. Transports H(2)O(2) in yeast cells.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:15584951}; Multi-pass membrane protein {ECO:0000269|PubMed:15584951}. Note=Tonoplast. Specifically located in the tonoplast of lytic or degradative vacuoles (LV) (By similarity). {ECO:0000250}.
Interaction partners:
- Protein S-acyltransferase 24
- NAC domain-containing protein 91
- Aquaporin SIP1-1
- Probable aquaporin SIP2-1
- Probable aquaporin SIP1-2
- PAMP-induced secreted peptide 1
Sequence:
MPIRNIAIGRPDEATRPDALKAALAEFISTLIFVVAGSGSGMAFNKLTENGATTPSGLVAAAVAHAFGLFVAVSVGANISGGHVNPAVTFGAFIGGNITLLRGILYWIAQLLGSVVACLILKFATGGLAVPAFGLSAGVGVLNAFVFEIVMTFGLVYTVYATAIDPKNGSLGTIAPIAIGFIVGANILAGGAFSGASMNPAVAFGPAVVSWTWTNHWVYWAGPLVGGGIAGLIYEVFFINTTHEQLPTTDY
Protein: Protein phosphatase 2C homolog 2 (PP2C-2) (EC 3.1.3.16) (Q09172)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has an important role in osmotic stability and cell shape control. It may negatively regulate the osmosensing signal transmitted through wis1 map kinase.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P39966}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P39966}.
Interaction partners:
- Putative serine/threonine-protein phosphatase C26H8.05c
- Uncharacterized N-acetyltransferase C9.02c
- Mitogen-activated protein kinase sty1
Sequence:
MGQTLSEPVLDKHSSSGGDRWLHFGVSHMQGWRISMEDAHCALLNFTDSNSSNPPTSFFGVFDGHGGDRVAKYCRQHLPDIIKSQPSFWKGNYDEALKSGFLAADNALMQDRDMQEDPSGCTATTALIVDHQVIYCANAGDSRTVLGRKGTAEPLSFDHKPNNDVEKARITAAGGFIDFGRVNGSLALSRAIGDFEYKKDSSLPPEKQIVTAFPDVVIHNIDPDDEFLILACDGIWDCKSSQQVVEFVRRGIVARQSLEVICENLMDRCIASNSESCGIGCDNMTICIVAFLHGRGLEDWYNWITQRVNSGEGPCAPPSYAELRGPNTIADARNLQLEYDHIASHEYGSGDTYDSDSDDETIAYDRYYLH
Protein: Gap3 (A1C3L7)
Organism: Streptococcus parasanguinis
Interaction partners:
Sequence:
MTKQLISEIYWNEIRKGENYLYGSQIKFQEDLVNFYNPQLASGKPIVTFKSRTNYQGDRHSPDLPILIQGNRYLLEYQIDAVPANSFFLQLDFFNRQAEQIESIVLRNSGESFIFPKDTFTYTLTLMSAGCQSVTYQKFMIYDINDEEKKNHIVENRYLRELLPKDLDLVKNLIEYI
Protein: Phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 1 (A0A8I6GLR6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MEAPGSGSGDGGGDPGGDGAHPDARGPSSGPCAAARDSERQLRLRLCVLNEILATERDYVGTLRFLQSAFLQRIRQNVADSVDKGLTEENVKILFSNIEDILEVHKDFLAALEYCLHPEPQSQHELGNVFLKFKDKFCVYEEYCSNHEKALRLLVELNKVPAARAFLLNCMLLGGRKTTDIPLEGYLLSPIQRICKYPLLLKELSKRTPGKHPDHSAVQSALQAMKTVCSNINETKRQMEKLEALEQLQSHIEGWEGSNLTDICTQLLLQGTLLKISAGNIQERAFFLFDNLLVYCKRKSRVTGSKKSTKRTKSINGSLYIFRGRINTEVMEVENVEDGTADYHSNGYTVTNGWKIHNTAKNKWFVCMAKTAEEKQKWLDALIREREQRESLKLGMERDAYVMIAEKGEKLYHMMMSKKVNLIKDRRRKLSTVPKCFLGNEFVAWLLEIGEISKTEEGVNLGQALLENGIIHHVSDKHQFKNEQVMYRFRYDDGTYKARSELEDIMSKGVRLYCRLHSLYAPVIKDRDYHLKTYKSVVPGSKLVDWLLAQGDCQTREEAVALGVGLCNNGFMHHVLEKSEFKDESQYFRFHADEEMEGTSSKNKQLRNDFKLVENILAKRLLIPPQEDDYGFDLEEKNKAVVVKSVQRGSLAEMAGLQAGRKIYSINEDLVFLRPFSEVETILNQSFCSRRPLRLLVATKAKETIKIPDHPEALSFQIRGTAPPCVFAVGRGSEAVAAGLCAGQCILKVNGNSVANDGALEVLEHFQAFRSRREEALGLYQWVYHSHEDAQQARASQGAPDEDPQEDDSVLPLLSLGPQLSLHEDSAVVSLTLDNVHLEHGVVYEYVSTAGAKCHVLEKIVEPRGCFRLAAKILEAFAEDDSLFVQNCGRLMAMGSAIITMSHYEFHNICDTKLESIGQRIACYQEFAAQLKSRVSPPFKQAPLEDHPLCGLDFCPTNCHINFMEVSYPKTTPSVGRSFSIRFGRKPSLIGLDPEQGHLNPMAYTQHCITTMAAPSWKCAPAVDGDSQSQGLIDSIFVSASGALSQQERGLSFLLKQEDREIQDAYLQLFTKLDVALKEMKQYVTQINRLLSTITEPTSAAPCDPPLVEETSSSPPASEESEVDRTDHGGIKKVCFKVSEDEQEDSGHDTMSYRDSYSECNSNRDSVLSYTSVRSNSSYLGSDETGSGDELPCDIRIPSDKQDKLHGCLEHLFNQVDSIHALLKGPVMSRAFEETRHFPMEHSWQEFKQKEECTVRGRNLIQISIQEDPWNLPSSIRTLVDNIQRYVEDGKNQLLLALLKCTDTELQLRRDAVFCQALVAAVCTFSEQLLAALDYRYNNNGEYEESSRDASRKWLEQVAATGVLLHWQSLLAPATVKEERTMLEDIWVTLSELDNVTFSFKQLDENSVANTNVFYHIEGSRQALKVVFYLDGFHFSRLPSRLEGGASLRLHTVLFTKALENVEGPSPPGSQAAEDLQQEINAQSLEKVQQYYRRLRAFYLERSNLPTDATTTAVKIDQLIRPINALDELYRLMKSFVHPKAGAGGSLGAGLVPVSSELCYRLGACQITMCGTGMQRSTLSVSLEQAAILARSHGLLPKCVMQATDIMRKQGPRVEILAKNLRIKDPMPQGAPRLYRLCQPPVDGDL
Protein: Germacrene A synthase 1 (EC 4.2.3.23) (Terpene synthase 1A) (HaTPS1A) (Q4U3F7)
Organism: Helianthus annuus (Common sunflower)
Function: Sesquiterpene synthase involved in germacrene A biosynthesis. Germacrene A is a precursor of several sesquiterpene lactones.
Interaction partners:
Sequence:
MAAVGASATPLTNTKSTAEPVRPVANFPPSVWGDLFLSFSLDKSIMEEYAEAMEEPKEQVRRLILDPTMDSNKKLSLIYTVHRLGLTYMFLKEIEAQLDRLFKEFNLEDYVELDLYTISINFQAFRHLGYKLPCDVFNKFKNDDSTTFKESITGDVRGMLGLYESAQLRLKGENILDEASAFAETKLKSLVNTLEGSLAQQVKQSLRRPFHQGMPMVEARLYFSNYQEECSAHDSILKLAKLHFNYLQLQQKEELRIVSQWWKDMRFQETTPYIRDRVPEIYLWILGLYFEPRYSLARIIATKITLFLVVLDDTYDAYATIEEIRLLTDAINRWDISAMNQIPEYIRPFYKILLDEYAELEKQLAKEGRANSVIASKEAFQDIARGYLEEAEWTNSGYVASFPEYMKNGLITSAYNVISKSALVGMGEIVSEDALVWYESHPQILQASELISRLQDDVMTYQFERERGQSATGVDSYIKTYGVSEKVAIDELKKMIENAWKEINEGCLKPREVSMDLLAPILNLARMIDVVYRYDDGFTFPGKTLKEYITLLFVGSSPM
Protein: Hsc70-interacting protein (Hip) (Protein FAM10A1) (Protein ST13 homolog) (P50503)
Organism: Rattus norvegicus (Rat)
Function: One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins.
Subcellular location: Cytoplasm.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 4
- Heat shock cognate 71 kDa protein
- BAG family molecular chaperone regulator 1
- DnaJ heat shock protein family
- Suppressor of tumorigenicity 14 protein homolog
- Prostaglandin E synthase 3
- Heat shock protein HSP 90-beta
Sequence:
MDPRKVSELRAFVKMCRQDPSVLHTEEMRFLREWVESMGGKVPPATHKAKSEENTKEEKRDKTTEDNIKTEEPSSEESDLEIDNEGVIEADTDAPQEMGDENAEITEAMMDEANEKKGAAIDALNDGELQKAIDLFTDAIKLNPRLAILYAKRASVFVKLQKPNAAIRDCDRAIEINPDSAQPYKWRGKAHRLLGHWEEAARDLALACKLDYDEDASAMLREVQPRAQKIAEHRRKYERKREEREIKERIERVKKAREEHEKAQREEEARRQSGSQFGSFPGGFPGGMPGNFPGGMPGMGGAMPGMAGMPGLNEILSDPEVLAAMQDPEVMVAFQDVAQNPSNMSKYQNNPKVMNLISKLSAKFGGHS
Protein: DNA polymerase epsilon subunit D (DNA polymerase II subunit D) (P87174)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: As accessory component of the DNA polymerase epsilon (DNA polymerase II) participates in chromosomal DNA replication. It is required during synthesis of the leading and lagging DNA strands at the replication fork and binds at/or near replication origins and moves along DNA with the replication fork. It has 3'-5' proofreading exonuclease activity that correct errors arising during DNA replication. It is also involved in DNA synthesis during DNA repair (By similarity). The dpb3-dpb4 dimer associates with histone deacetylases, chromatin remodelers, and histones and plays a crucial role in the inheritance of histone hypoacetylation and H3K9 methylation in heterochromatin. The dpb3-dpb4 dimer is also required for the recruitment of sir2 to heterochromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:15388803}.
Interaction partners:
- DNA polymerase epsilon subunit B
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase epsilon subunit C
- DNA polymerase alpha catalytic subunit
- DNA polymerase delta catalytic subunit
- Cell division control protein 45 homolog
- DNA polymerase zeta catalytic subunit
- DNA polymerase alpha subunit B
- DNA primase large subunit
- Negative cofactor 2 complex subunit beta
Sequence:
MNQDKSKETSELDDLALPRSIIMRLVKGVLPEKSLVQKEALKAMINSATLFVSFLTSASGEIATNNNRKILMPQDVLNALDEIEYPEFSKTLKKHLEAYELALKEKRLKLPNVSDVDNRKKAKIDAHDTTPLDEEKDELEEERIAEDIAQNEVEQNIDDVEDLEEVNDTLDANAESPQIETIHLTDATGNPIEDSSESDSEESLQLNDSS
Protein: Acyl-coenzyme A amino acid N-acyltransferase 1 (EC 2.3.1.-) (A2AKK5)
Organism: Mus musculus (Mouse)
Function: Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine. Shows no conjugation activity in the presence of glycine.
Subcellular location: Peroxisome {ECO:0000269|PubMed:17116739}.
Interaction partners:
- Long-chain fatty acid transport protein 5
- Sterol carrier protein 2
- Cysteine sulfinic acid decarboxylase
- Acyl-coenzyme A thioesterase 8
- Bile acid-CoA:amino acid N-acyltransferase
- Acyl-coenzyme A amino acid N-acyltransferase 2
- Glutamate decarboxylase 1
- Glutamate decarboxylase 2
- Glutathione hydrolase 1 proenzyme
- Glutathione hydrolase 6
Sequence:
MMIKLIATPSNALVDEPVSIRATGLPPSQIVTIKATVKDENDNVFQSQAFYKTNEAGEVDLEKTPALGGDYVGVHPMGLFFSLKPKKAFHRLMKKDVMNSPFCICLDLYDSVNWLETVRIPSKASQRVQRWFVGPGVKREQIQEGRVRGALFLPPGKGPFPGIIDLFGVIGGLVEFRASLLASHGFAVLALAYFAYKDLPEKLQEVDLEYFEEAANFLLSHPKIQQPGIGVISTSKGAEIGLAMACYLKQVIATVCINGATTTTAVPLRYQDLVVTPIQQALERMEVHVSGAVCFRHTTQYLQNKNILPVEKAQGKILFIVGENDELLDSKLHAQRAMDRLRRHGRSSGRMLAYPGAGHLIEPPYSPLCFASWQPVLGRPMCFGGDLMAHAAAQEHSWREIQKFFRKHLLQSGSKL
Protein: MEI-218 (Q24137)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSTNKLEKKDPRRHIPLQLNVFLRNDDDGEVREVTQNANTSSIGTIPSNGLVESDVTPIMTPTPKAGVYKPNVNVWRLSKEVTKPDRSFVVSAEEYPDLGQRPKRFKQRTPRVRNQDDGGTVSCLASRFSRVKDPPVLGNFLPDFMLPKSSNSNHQSVTTWLSSVRPSDSQKSLSDQARCSSSTNITLLSKDSVQPLTPKSSAQSSPGEKNIQQEQNTPAKSQQEETSPANSVEHQQKTPNSPKEQQKSSVGLTNMQQKASANSLQQQNSSASSLQQQNSSVHSLQKRKSWVNSSQQQRSSVNFIQKQRSWVNSSHHQKSSASSLQQKSSENSPSKFQQQQQKSPANNERSQNNQKSPGIQHSWKQQQQQKPKILQNCPKTSVQQQMNPVNHTQSQSERPTELIYLHSRSPAKRASVTNNSSAPIRIAPRQQTTQSSGPSVVHNEDEDVMPPTPNQSERRQRRFPRRNHNPRMVRSLQAVSREFTESLLEGSSGKTPEKEVVPYQQQEKPRQVKSSPEIHASSHMRKLAMGSVLNSNAKEFHPTGESHLTHKVSRLSQRRCRQRFTRSLHAKKNNPREQLPNPDSAPEPILEYTSEIDDQPCPPRQTVDTPIEAIVPPAMIEVSATGNLPPVFYFDQQSGIIWSNSSPQIPVEIQSNSVSQSVFRLASLPCTGVGTTNMDIFTSSPPPIQHMSSSRLPSSISGPTQLSHTLSSPPVENQHQQHLWESCIHQDEDLMYSRPLLDMDQEETQPEQQDQEWQWESEIEPPSFQSENQVVADEHGEENAYLAKDAGPPLERHMIFRAPSQHGQEYPKPDLNCVPSSIKKLHHLISSQYSDYSFVYALSAQISQDCVPMDCFVYLKMILLASIVSIESDEVRAPISLCIIATDSLMANRLLNKVGQLAPRFLGPHEYGLQPTFNALPTRFNWIVASPLLLAQQGVYYAGDWNRLSKDQGCQLEKCIENGAVPVPQLHIDQPLKAAVWTYWQPNNSTNQTLALAKLCPIFGLPIYMGAQASNSLWNSIIQKHNAEGQIVVNDGLSIPEDDMRMLIHLLHQRKTTLTDGAQHMLQKYYVISRKERPNVFSSKTYIVLKQLAECFANVALRLEVLESDVCVAIFHCEHFVQGIFGAKENQAPPAVFNFNVISCIDPYMNKFTRWLLQYLNSYEDEELGMHADKRRRTDSWDMP
Protein: DUNC-115s (Q95V19)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MYILIYISIPKHPQTDKTRPIYPSTLGTELRTELGKTGQGKQKIYCAKCTKKCSGEVLRVADNHFHKACFQCCQCKKSLATGGFFTKDNAYYCIPDYQRLYGTKCANCQQYVEGEVVSTMGKTYHQKCFTCSKCKQPFKSGSKVTNTGKEVLCEQCVTGAPVSPSRQATGGGVSSPAPPAESPTRATAHQQHGSVISHKAHLKEDYDPNDCAGCGELLKEGQALVALDRQWHVSCFRCKACQAVLNGEYMGKDAVPYCEKCYQKGFWVKCAYCSRFISGKVLQAGDNHHFHPTCARCTKCGDPFGDGEEMYLQGSAIWHPRCGPGPSESGIILNGGGGTSSVVGGASNGNFTDTECDRMSSSALSEMHYRTVSPGLILREYGRPNAEDISRIYTYSYLTDAPHYLRKPIDPYDKTPLSPHFHRPSSYATTASNAGSVAGSRPPSRPHSRTRSAMKVLVDAIRSETPRPKSPGMNNEEPIELSHYPAAKKPPPGEQPKIERDDFPAPPYPYTDPERRRRYSDTYKGVPASDDEDENVENGKPNGKVKNGEEQQRLQREAEQLEKLNSGIGSAIAKDLKEHAKYRKWKQNNLDPRNASRTPSASKEPLYKLRYESPIGASPSRNLDHQKPFYEDEMFDRSTSYRGSLGKSLGNAPSYNAIHSYRSPPKPGYGFKTTTLPYIRNGFSSDFSYGGLGDKTHSTDLSCGKSEASVDSITEGDRRALMGGDLPASSTYSGALSYHYPQAGLIRRSLPNMSHSIISCANAKL