wanglab/gogpt-training-data huggingface dataset:
Protein: Hormone-sensitive lipase (HSL) (EC 3.1.1.79) (Monoacylglycerol lipase LIPE) (EC 3.1.1.23) (Retinyl ester hydrolase) (REH) (P15304)
Organism: Rattus norvegicus (Rat)
Function: Lipase with broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters. Shows a preferential hydrolysis of DAGs over TAGs and MAGs and preferentially hydrolyzes the fatty acid (FA) esters at the sn-3 position of DAGs (By similarity). Preferentially hydrolyzes fatty acids at the sn-1 and sn-2 positions of TAGs. Catalyzes the hydrolysis of 2-arachidonoylglycerol, an endocannabinoid and of 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor (By similarity). In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q05469}. Membrane, caveola {ECO:0000250|UniProtKB:Q05469}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q05469}. Lipid droplet {ECO:0000269|PubMed:15878856}. Note=Found in the high-density caveolae (By similarity). Translocates to the cytoplasm from the caveolae upon insulin stimulation (By similarity). Phosphorylation by AMPK reduces its translocation towards the lipid droplets. {ECO:0000250|UniProtKB:Q05469, ECO:0000269|PubMed:15878856}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- Fatty acid-binding protein, adipocyte
- cAMP-dependent protein kinase catalytic subunit beta
- Perilipin-1
- Patatin-like phospholipase domain-containing protein 2
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- TIR domain-containing adapter molecule 1
- Perilipin
- Protein kinase AMP-activated non-catalytic subunit gamma 2
- cAMP-dependent protein kinase type II-beta regulatory subunit
Sequence:
MKPRRPISFTREITAMEPSSTSVSRPEWRPEAQQTLTDYPGSRELQEFGIPQKQSLPNEATAQQGAEFQQEQGVQQSTLLQKLLTPLAFPVPQQSFPSHKVHSDQQEATSQNGPGAGKVHTTQKELEHRDEHVGTAESGPAEPPPATEVEATSIAQAVSGPDKKLPTQTDLVSQERAEQSDPTAQQTPLVQGVKSDQGSLIESGILARLQKLAIQQPSQEWKTFLDCVTESDMEKYLNSSSKSNPPEPSGGTVIPGTLPSKQKPDCGKMSGYGGKLPHGKKGILQKHKHYWDTASAFSHSMDLRTMTQSLVALAEDNMAFFSSQGPGETARRLSNVFAGVREQALGLEPTLGQLLGVAHHFDLDTETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRASHNLAELEAYLAALTQLRALAYYAQRLLTINRPGVLFFEGDEGLSADFLQDYVTLHKGCFYGRCLGFQFTPAIRPFLQTLSIGLVSFGEHYKRNETGLSVTASSLFTGGRFAIDPELRGAEFERIIQNLDVHFWKAFWNITEIEVLSSLANMASTTVRVSRLLSLPPEAFEMPLTSDPKLTVTISPPLAHTGPGPVLARLISYDLREGQDSKMLNSLAKSEGPRLELRPRPQQAPRSRALVVHIHGGGFVAQTSKSHEPYLKNWAQELGVPIISIDYSLAPEAPFPRALEECFFAYCWAVKHCELLGSTGERICLAGDSAGGNLCITVSLRAAAYGVRVPDGIMAAYPVTTLQSSASPSRLLSLMDPLLPLSVLSKCVSAYSGTETEDHFDSDQKALGVMGLVQRDTSLFLRDLRLGASSWLNSFLELSGRKPHKTPLPATETLRPTDSGRLTESMRRSVSEAALAQPEGLLGTDSLKKLTIKDLSFKGNSEPSDSPEMSQSMETLGPSTPSDVNFFLRSGNSQEEAETRDDISPMDGIPRVRAAFPDGFHPRRSSQGVLHMPLYSSPIVKNPFMSPLLAPDVMLKTLPPVHLVACALDPMLDDSVMFARRLKDLGQPVTLKVVEDLPHGFLSLAALCRETRQAAELCVQRIRLILTPPAAPLT
Protein: High-affinity heme uptake system protein IsdE (Iron-regulated surface determinant protein E) (Staphylococcal iron-regulated protein F) (Q7AP55)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Interaction partners:
- Probable heme-iron transport system permease protein IsdF
- Lmo2182 protein
- Sortase B
- Lmo2430 protein
- FhuG protein
- FhuB protein
- Lmo2429 protein
- Hemin/hemoglobin-binding protein 1
- FhuC protein
- Lmo0365 protein
Sequence:
MRKMAVISLVLLLFLVGCGKEEAAQKPEQKTDKEPKIVATTVAITEIMDKLDLPLVGIPSSSKKLPKRYADVKETGSPMGPDLEIIRMLKPDMVLSTKTLEADLKSGFEGADLEADFLDFTSIASMQTEIKNLGAKFDRIEEATKLNKDLTSDIDQVKSNVAKKKKPTVLILMGVPGSYLVVTEHAYIGDLVKLAGGENVIKDQKVEYLASNTEYLQSANPDIILRAAHGMPAEVVKMFDEEFKTNDIWKHFDAVKNNRVYDLDENLFGMTASLNAPEALKEMEKMLYDN
Protein: Solute carrier family 12 member 9 (Cation-chloride cotransporter 6) (hCCC6) (Cation-chloride cotransporter-interacting protein 1) (CCC-interacting protein 1) (hCIP1) (Potassium-chloride transporter 9) (WO3.3) (Q9BXP2)
Organism: Homo sapiens (Human)
Function: May be an inhibitor of SLC12A1. Seems to correspond to a subunit of a multimeric transport system and thus, additional subunits may be required for its function.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10871601}; Multi-pass membrane protein {ECO:0000269|PubMed:10871601}. Lysosome membrane {ECO:0000269|PubMed:38334070}.
Interaction partners:
Sequence:
MASESSPLLAYRLLGEEGVALPANGAGGPGGASARKLSTFLGVVVPTVLSMFSIVVFLRIGFVVGHAGLLQALAMLLVAYFILALTVLSVCAIATNGAVQGGGAYFMISRTLGPEVGGSIGLMFYLANVCGCAVSLLGLVESVLDVFGADATGPSGLRVLPQGYGWNLLYGSLLLGLVGGVCTLGAGLYARASFLTFLLVSGSLASVLISFVAVGPRDIRLTPRPGPNGSSLPPRFGHFTGFNSSTLKDNLGAGYAEDYTTGAVMNFASVFAVLFNGCTGIMAGANMSGELKDPSRAIPLGTIVAVAYTFFVYVLLFFLSSFTCDRTLLQEDYGFFRAISLWPPLVLIGIYATALSASMSSLIGASRILHALARDDLFGVILAPAKVVSRGGNPWAAVLYSWGLVQLVLLAGKLNTLAAVVTVFYLVAYAAVDLSCLSLEWASAPNFRPTFSLFSWHTCLLGVASCLLMMFLISPGAAGGSLLLMGLLAALLTARGGPSSWGYVSQALLFHQVRKYLLRLDVRKDHVKFWRPQLLLLVGNPRGALPLLRLANQLKKGGLYVLGHVTLGDLDSLPSDPVQPQYGAWLSLVDRAQVKAFVDLTLSPSVRQGAQHLLRISGLGGMKPNTLVLGFYDDAPPQDHFLTDPAFSEPADSTREGSSPALSTLFPPPRAPGSPRALNPQDYVATVADALKMNKNVVLARASGALPPERLSRGSGGTSQLHHVDVWPLNLLRPRGGPGYVDVCGLFLLQMATILGMVPAWHSARLRIFLCLGPREAPGAAEGRLRALLSQLRIRAEVQEVVWGEGAGAGEPEAEEEGDFVNSGRGDAEAEALARSANALVRAQQGRGTGGGPGGPEGGDAEGPITALTFLYLPRPPADPARYPRYLALLETLTRDLGPTLLVHGVTPVTCTDL
Protein: TauD/TfdA-like domain-containing protein (A0A1D8PRK5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Aldehyde dehydrogenase domain-containing protein
- low-specificity L-threonine aldolase
- Indoleamine 2,3-dioxygenase
Sequence:
MLRQPLRQIRFHSKLALAGYNSKEVTVTINGRTCTFNNVFLRDACQSPDSVDPISSQKLFTTADAATGLQINAPPVVEDSSLKIQWSNNGKLTNSVYPVSFLENYSTNKRLGKFFDKDRKLWDKQELENNFASLNMDYDDILTNDNSFFQTLYNLNRYGLTFVNNIPTPQISDMTEDNATQWPVYKIAEKFGYIKKTFYGTLFDVKNKKEKATNIAYTNTFLPLHMDLLYYESPPGLQLLHAIQNSTLGGENIFCDSYLAAEHVRKTDPRAYTALTQTPITFHYDNNNEYYYYKRPLIVEDPEVGDGFPKIASINYAPPFQGPFEVDPHPDFIRGMQLFETFINDPANHFEIKMPEGTCVIFENRRALHSRNAFSDSNNGDRWLMGTYVDGDSFRSKLRIGYRKVHT
Protein: Lysosomal acid phosphatase (LAP) (EC 3.1.3.2) (P24638)
Organism: Mus musculus (Mouse)
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:P11117}; Single-pass membrane protein {ECO:0000255}; Lumenal side {ECO:0000250|UniProtKB:P11117}. Lysosome lumen {ECO:0000250|UniProtKB:P11117}. Note=The soluble form arises by proteolytic processing of the membrane-bound form. {ECO:0000250|UniProtKB:P11117}.
Interaction partners:
- Tartrate-resistant acid phosphatase type 5
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Riboflavin kinase
- FAD synthase
- Flavin reductase
Sequence:
MAGRQTGWSQAALLQFLLGMCLTVMPPIQARSLRFVTLLYRHGDRSPVKTYPKDPYQEEKWPQGFGQLTKEGMLQHWELGQALRQRYHGFLNTSYHRQEVYVRSTDFDRTLMSAEANLAGLFPPNEVQHFNPNISWQPIPVHTVPITEDRLLKFPLGPCPRYEQLQNETRQTPEYQNRSIQNAQFLNMVANETGLTNVTLETIWNVYDTLFCEQTHGLLLPPWASPQTVQRLSQLKDFSFLFLFGIHEQVQKARLQGGVLLAQILKNLTLMATTSQFPKLLVYSAHDTTLVALQMALNVYNGKQAPYASCHIFELYQEDNGNFSVEMYFRNDSKKAPWPLILPGCPHRCPLQDFLRLTEPVIPKDWQKECQLANDTADTEVIVALAVCGSILFLLIVLLLTILFRMQAQPPGYHHVADREDHA
Protein: Trypsin inhibitor (ClTI) (EC 3.4.21.4) (C0HK48)
Organism: Cassia leiandra (Marimari)
Function: Inhibits trypsin but not chymotrypsin, papain or porcine pancreatic alpha-amylase. Has insecticidal activity against A.aegypti. Functions by inhibiting the A.aegypti midgut proteases to reduce the survival of larva and adults.
Interaction partners:
Sequence:
SVELDSDGEPIRNGGGLYYILPVVQGKGGGLEFAKTGSQS
Protein: Inosine-5'-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) (P0ADG7)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Interaction partners:
- GMP synthase
- Adenylosuccinate synthetase
- Bifunctional purine biosynthesis protein PurH
- Xanthine-guanine phosphoribosyltransferase
- Hypoxanthine phosphoribosyltransferase
- dITP/XTP pyrophosphatase
- Guanosine-inosine kinase
- GMP reductase
- Adenylosuccinate lyase
- 5'/3'-nucleotidase SurE
Sequence:
MLRIAKEALTFDDVLLVPAHSTVLPNTADLSTQLTKTIRLNIPMLSAAMDTVTEARLAIALAQEGGIGFIHKNMSIERQAEEVRRVKKHESGVVTDPQTVLPTTTLREVKELTERNGFAGYPVVTEENELVGIITGRDVRFVTDLNQPVSVYMTPKERLVTVREGEAREVVLAKMHEKRVEKALVVDDEFHLIGMITVKDFQKAERKPNACKDEQGRLRVGAAVGAGAGNEERVDALVAAGVDVLLIDSSHGHSEGVLQRIRETRAKYPDLQIIGGNVATAAGARALAEAGCSAVKVGIGPGSICTTRIVTGVGVPQITAVADAVEALEGTGIPVIADGGIRFSGDIAKAIAAGASAVMVGSMLAGTEESPGEIELYQGRSYKSYRGMGSLGAMSKGSSDRYFQSDNAADKLVPEGIEGRVAYKGRLKEIIHQQMGGLRSCMGLTGCGTIDELRTKAEFVRISGAGIQESHVHDVTITKESPNYRLGS
Protein: Collagen type XVI alpha 1 chain (G3MXK9)
Organism: Bos taurus (Bovine)
Interaction partners:
- Collagen alpha-2
- Collagen type V alpha 2 chain.
- Collagen alpha-2
- Collagen type V alpha 1 chain
- Collagen alpha-1
- Collagen alpha-1
- Collagen type III alpha 1 chain
- Collagen alpha-2
- Collagen alpha-2
- Collagen type V alpha 3 chain
Sequence:
MWASWAPGLWLLSLYVTYSHGADAGEQCPPSQQEGLKLEHRSDLSTNVTGFNLIHRLSLMKTSAVKKIRNPKGPFILRLGAVSVTQPTRRVFPRGLPSEFALVLTLLMKKHTHRNTWYLFQVTDGDGYPQISLEVNSQEQSLELRTRGQDGDFVSCIFSVPQLFDLRWHKLVLSVAERVASVHVDCMSASSQPLGPRRSIEPVGHVFLGLDAEQGKPVSFDLQQAHIYCDPEFVLEEGCCEILPGGCPPETSKARRDTQNNELIEINPQTEGKVYTRCFCLEEPQNSKVDAQLSGRISQKPERGAKAHQETAADECPPCVHGAQESNVTIGPSGPQGGKGERGLPGPSGPKGEKGARGNDCVRISPDAPLQCAEGLKGEKGESGALGPSGLPGSTGQKGQKGEKGDGGVKGSPGKPGRDGRPGEVCVIGPKGQKGDPGFVGPEGLAGEPGPPGLPGPPGIGLPGTPGDPGGPPGPKGDKGNSGVPGKEGPGGKPGKPGVPGLKGEKGDPCEVCPTLPEGFQNFVGLPGKPGPKGEPGDPAPARESLGAVGQKGDRGDPGIQGLKGEKGESCSSCSFAVAAQHLQPSAGAKGDVGPPGLGLPGLPGKAGAPGPTGLKGEKGNFGEVGPAGNPGPPGPAGPTGIKGEKGEPCEPCRALTEHQDEDSHVVALPGPRGEKGEPGPPGFGLPGKQGKAGERGLKGQKGDAGNPGDPGTPGITGRPGLSGEPGVRGPVGPKGEKGDGCTACPSTQGALTDRAGPPGKPGPKGDPGPEGVGRPGKPGQPGLPGVQGPPGLKGIQGEPGPPGVGVQGPQGEPGAQGLPGIQGLPGPRGPPGPAGEKGAKGSPGVKGAAGPVGPPGASVSGPPGPDGQQGQAGLPGARGMPGEKGSQGEKGEPGECSCPSRGDLIFSGMPGAPGLWMGSSWQPGPQGPPGVPGPPGPPGMPGLQGVPGHNGLPGQPGLTAELGSLPIEQHLLKSICGDCIQGKMAHEVALMESGEKGDQGIPGVPGLDSCTQCFMERERPRAEEARGDNHEGDPGCAGSPGLPGPPGLPGQRGEEGLQGERGLRGLTGEKGEPGPPGQPGYPGAMGPPGLPGIKGERGYAGSPGEKGESGPPGSEGLPGPPGPAGPRGERGPQGSSGEKGDQGFQGQPGFPGPPGPPGFPGKAGAPGPPGPQAEKGSEGIRGPSGLPGPPGPPGSPGIQGPAGLDGLDGKDGKPGLRGDPGPAGPPGLMGPPGFKGKPGHPGLPGQKGDCGKPGPQGSSGRPGAEGEPGAMGPQGRPGPPGHVGPPGPPGQPGPAGISAVGPKGDRGATGERGLLGLPGQPGPPGHPGPPGEPGMDGAAGKEGPPGKQGLYGPPGPKGDPGPSGQKGQAGEKGRAGMPGGPGKSGSMGPAGPPGPAGERGHPGSPGPAGSPGLPGVPGSMGDMVNYDEIKRFIRQEIIKMFDERMAYYTSRMQFPMEMAAAPGRPGPPGKDGPPGRPGSPGSPGLPGQIGREGRQGLPGMRGLPGTKGEKGDIGVGIAGEIGLPGPPGPQGPPGYGKMGATGPMGQQGIPGIPGPPGPIGPPGKTGHCNPSDCFGAMPMEQQYPPMKNMKGPFG
Protein: Sll0169 protein (Q55559)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Hydrogenase subunit
- Sll1939 protein
- Sll0072 protein
- Sll1033 protein
- Heat shock protein
- Slr0086 protein
- Sll1632 protein
- Chaperone protein DnaK2
- Thylakoid membrane protein slr1796
- Penicillin-binding protein
Sequence:
MFIPLDFYRILGIPPQSGGETIEQAYQDRLLQLPRREFSDAAVTLRNQLLAIAYETLRDPEKRQAYDQEWWGAMDEALGEALPLTTPELECSPEQEIGALLILLDLGEYELVVKYGEPVLHDPNPPAGGLPQDYLLSVILAHWELSRERWQQQQYEFAATASLKALARLQQDNDFPALEAEIRQELYRLRPYRILELLAKEGQGEEQRQQGLALLQAMVQDRGGIEGKGEDYSGLGNDDFLKFIHQLRCHLTVAEQNALFLPESQRPSLVASYLAVHSLMAEGVKEQDPMAIVEAKSLIIQLENCQDLALEKVICELLLGQTEVVLAAIDQGDPKIVAGLESKLATGEDPLTAFYTFTEQWLEEEIVPYFRDLSPETLSPKAYFNNPSVQQYLEQLEPDSFTTDNSFASPALLSTATESETPMVHSSAALPDRPLTSTVPSRRGRSPRRSRDDVFPSADNSSGLAVTTLSPAIAYDTHSLGTNGIGGDSTSNGFSSNSAPESTSKHKSPRRRKKRVTIKPVRFGIFLLCLAGIVGGATALIINRTGDPLGGLLEDPLDVFLDQPSEFIPDEATSRNLILSQPNFNQQVGQMVVQGWLDSKKLAFGQNYDVGALQSVLAPNLLAQQRGRAQRDQAQKVYHQYEHKLQILAYQVNPQDPNRATVTARVEEISQPFTLGNQQQKGSATKDDLTVRYQLVRHQGVWKIDQIQVVNGPR
Protein: Eukaryotic translation initiation factor 4 gamma 1 (D3ZU13)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- RNA helicase
- Eukaryotic translation initiation factor 4E
- Eukaryotic initiation factor 4A-II
- Eukaryotic translation initiation factor 4B
- Polyadenylate-binding protein 1
- Eukaryotic translation initiation factor 4, gamma 2.
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 4E type 2
- Eukaryotic translation initiation factor 4 gamma, 3
- Eukaryotic translation initiation factor 3 subunit A
Sequence:
MNKAPQPTGPPPARSPGLPQPAFPPGQTAPVVFSTPQATQMNTPSQPRQGGFRSLQHFYPSRAQPPSSAASRVQSAAPARPGPAPHVYPAGSQVMMIPSQISYSASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQSVQQFPASVAPAPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGSLEPQPNGESPQVAVIIRPDDRSQGAAIGGRPGLPGPEHSPGTESQPSSPSPTPSPPPILEPGSESNLGVLSIPGDTMTTGMIPISVEESTPISCESGEPYCLSPEPTLAEPILEVEVTLSKPIPESEFSSSPLQVSTSLVPHRAETHEPNGVIPSEDLEPEVESSTEPAPPPLSACASESLVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVPSAALASIVSPTPPVAPSDTSAAQEEEIEEDEDEDGEAESEKGGEDLPLDSTPVPAQLSQNLEVAAAPQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEVDPAVPEVENQPPTGSNPSPESEGSAALPQPEEAEETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHITDVVLDKANKTPLRSLDPSRLPGINCGPDFTPSFANLGRPTLSSRGPPRGGPGGELPRGPAGLGPRRSQQGPRKETRKIISSVIMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFAKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRQSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGGDKRRGGPPGPPVNRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDTASEATRPATLNRFSALQQTLPVENTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRGRDPVKREATLPPVSPPKAALAVDEVERKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRLGIESTLERSTIAREHMGRLLHQLLCAGHLSTAQYYQGLYETLELAEDMEIDIPHVWLYLAELITPILQEDGVPMGELFREITKPLRPMGKATSLLLEILGLLCKSMGPKKVGMLWREAGLSWREFLAEGQDVGSFVAEKKVEYTLGEESEAPGQRALAFEELRRQLEKLLKDGGSNQRVFDWIEANLNEQQIASNTLVRALMTTVCYSAIIFETPLRVDVQVLKVRARLLQKYLSDEQKELQALYALQALVVTLEQPANLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFNWLREAEDEESDHN
Protein: Zinc finger protein 33B (Zinc finger protein 11B) (Zinc finger protein KOX2) (Q06732)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MNKVDQKFQGSVSFKDVTVGFTQEEWQHLDPSQRALYRDVMLENYSNLVSVGYCAHKPEVIFRLEQGEEPWRLEEEFPSQSFPEVWTADHLKERSQENQSKHLWEVVFINNEMLTKEQGNVIGIPFNMDVSSFPSRKMFCQYDSRGMSFNTVSELVISKINYLGKKSDEFNACGKLLLNIKHDETHTREKNEVLKNRNTLSHRENTLQHEKIQTLDHNFEYSICQETLLEKAVFNTRKRENAEENNCDYNEFGRTFCDSSSLLFHQIPPSKDSHYEFSDCEKFLCVKSTLSKHDGVPVKHYDCGESGNNFRRKLCLSQLQKGDKGEKHFECNECGKAFWEKSHLTRHQRVHTGEKHFQCNQCGKTFWEKSNLTKHQRSHTGEKPFECNECGKAFSHKSALTLHQRTHTGEKPYQCNACGKTFYQKSDLTKHQRTHTGQKPYECYECGKSFCMNSHLTVHQRTHTGEKPFECLECGKSFCQKSHLTQHQRTHIGDKPYECNACGKTFYHKSVLTRHQIIHTGLKPYECYECGKTFCLKSDLTIHQRTHTGEKPFACPECGKFFSHKSTLSQHYRTHTGEKPYECHECGKIFYNKSYLTKHNRTHTGEKPYECNECGKTFCQKSQLTQHQRIHIGEKPYECNECGKAFCHKSALIVHQRTHTQEKPYKCNECGKSFCVKSGLILHERKHTGEKPYECNECGKSFSHKSSLTVHHRAHTGEKSCQCNECGKIFYRKSDLAKHQRSHTGEKPYECNTCRKTFSQKSNLIVHQRTHIGEKPYE
Protein: Tubulin alpha-4A chain (EC 3.6.5.-) (Alpha-tubulin 1) (Testis-specific alpha-tubulin) (Tubulin H2-alpha) (Tubulin alpha-1 chain) (P68366)
Organism: Homo sapiens (Human)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-2A chain
- Tubulin beta chain
- Tubulin beta-3 chain
- Tubulin beta-4B chain
- Tubulin beta-4A chain
- Microtubule-associated protein tau
- Tubulin beta-6 chain
- Tubulin beta-2B chain
- Tubulin beta-1 chain
- Tubulin beta-8 chain
Sequence:
MRECISVHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFTTFFCETGAGKHVPRAVFVDLEPTVIDEIRNGPYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDPVLDRIRKLSDQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIAAIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGIDSYEDEDEGEE
Protein: Putative uncharacterized protein C13G1.15c (Q9C0X3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MASCCIFCAQFVLNRNLLEANKYKLSEITFKVYISIRRLLIVVITLYRRIVECCASLCSLIFSKYYLHYKTFRILTIIQSWSDKVSVLPNRLYCLPFCNAFIEFVKKLTET
Protein: Zinc finger protein ZAT1 (Q39092)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that may be involved in stress responses.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- At1g56200/F14G9_26
Sequence:
MEERHKCKLCWKSFANGRALGGHMRSHMLIHPLPSQPESYSSSMADPGFVLQDRESETESSKKPSRKRSRLNRRSISSLRHQQSNEEGKSETARAADIKIGVQELSESCTEQEPMSSVSDAATTEEDVALSLMLLSRDKWEKEEEESDEERWKKKRNKWFECETCEKVFKSYQALGGHRASHKKKIAETDQLGSDELKKKKKKSTSSHHECPICAKVFTSGQALGGHKRSHASANNEFTRRSGIIISLIDLNLPAPSEEEEMASSVF
Protein: Regulator of microtubule dynamics 3 (H0YNE5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRLGALGGARAGLGLLLGTAAGLGFLCLLYSQRWKRTQRHGRSQSLPNSLDYTQTSDPGRHVMLLRAVPGGAGDASVLPSLPREGQEKVLDRLDFVLTSLVALRREVEELRSSLRGLAGEIVGEVRPLMRSSSKRHPMVSRKTSWMGPNGTLRDGACFPDATWKRTREWLGGEGFRLSGRGVTPLAPALSTSRPPREPRSQMLRVKGGKEEAEAALEKGDESADCHLWYAVLCGQLAEHESIQRRIQSGF
Protein: Ras GTPase-activating protein-binding protein gtbp-1 (Q21351)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, Stress granule {ECO:0000269|PubMed:32432401, ECO:0000269|PubMed:34661238, ECO:0000269|PubMed:34807903}. Cytoplasm {ECO:0000269|PubMed:34661238}. Note=Cytoplasmic but assembles into stress granules following cellular stress (PubMed:34661238). Co-localizes with and requires pqn-59 to effectively localize to stress granules (PubMed:34807903). {ECO:0000269|PubMed:34661238, ECO:0000269|PubMed:34807903}.
Interaction partners:
- Prion-like
- RRM domain-containing protein
- RRM domain-containing protein
- Cytotoxic granule-associated RNA binding protein tiar-1
- WD_REPEATS_REGION domain-containing protein
- Ataxin-2 homolog
- NAD-dependent protein deacetylase sir-2.4
Sequence:
MQITSALTQNKMDPINGNLTSTAPVEPLSLTAAEQVGGAFCHQFYITVSENRKAITKFYGHESKFYLDDQVVTGSQEIVKLYNHLPETTHFKIQSIKGYPTPHKQGVIINVIGTVNLRPFLQSFLLGQQGQKKYYVESDAFQYIDKFFVANTEKEKTTSSTGHNGHASGANGKDSKSSKTEQPKEQSKPAPPKQQTPKKAEDRIVKQDTPKSVEKEVAKTPQKPQLAQQPPQQRAPVPEPVQEQPKVQKTWANLVGGGGKSQPPQQQSYGQGQQIHQQTQMHHMQPSMHQQQQGSHAPLYQQQRQSHPANELRQAQESSDANLNERKIYLGGITREIVPSNTAQAESEIKQVFYKYGEIEEVRMPRKVLDSPNDTSKHAFAFITMRNKAGVKAIFEAATKDEQGVWKLPLKLDAFGFDGHAQISEQRDQPQGGGFRGGRGGFQPRGGQFFRRGGSGGAPRGGMRSGFQNAGQN
Protein: Alpha/beta-Hydrolases superfamily protein (Putative phospholipase) (Q8RXN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cytochrome P450 98A3
- F5F19.5 protein
- Flavone 3'-O-methyltransferase 1
- Shikimate O-hydroxycinnamoyltransferase
- 4-coumarate--CoA ligase 4
- Cinnamoyl-CoA reductase 2
- Cinnamoyl-CoA reductase 1
- Putative caffeoyl-CoA O-methyltransferase At1g67980
- Cytochrome P450 84A1
- 4-coumarate--CoA ligase 1
Sequence:
MASETENIKYEESFIKNTRGMKLFTCKWVPAKQEPKALVFICHGYAMECSITMNSTARRLVKAGFAVYGIDYEGHGKSDGLSAYVPNFDHLVDDVSTHYTSICEKEENKGKMRFLLGESMGGAVLLLLHRKKPQFWDGAVLVAPMCKIAEEMKPSPLVISILAKLSGVIPSWKIIPGQDIIETAFKQPEIRKQVRENPYCYKGRPRLKTAYELLRVSTDLEKRLNEVSLPFIVLHGEDDKVTDKAVSRQLYEVASSSDKTFKLYPGMWHGLLYGETPENIETVFADIIGWLDKKVADESGGFESELKRKNDGIPLKG
Protein: Ras-related protein Rab-6 (EC 3.6.5.2) (Q8IHR8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Vacuolar protein sorting-associated protein 33, putative
- GDP dissociation inhibitor, putative
- Ran-specific GTPase-activating protein 1, putative
- Rab GDP dissociation inhibitor
- Vacuolar protein sorting-associated protein 3, putative
- Vacuolar protein sorting-associated protein 52, putative
- Vacuolar protein sorting-associated protein 53, putative
- Ras-related protein Rab-1A
- GTPase-activating protein, putative
Sequence:
MDEFQNSGLNKYKLVFLGEQAVGKTSIITRFMYDTFDNNYQSTIGIDFLSKTLYLDEGPVRLQLWDTAGQERFRSLIPSYIRDSAAAIVVYDITNRQSFENTTKWIQDILNERGKDVIIALVGNKTDLGDLRKVTYEEGMQKAQEYNTMFHETSAKAGHNIKVLFKKIASKLPNLDNTNNNEANVVDIQLTNNSNKNDKNMLSKCLC
Protein: R-spondin-3 (Cabriolet) (Cysteine-rich and single thrombospondin domain-containing protein 1) (Cristin-1) (Nucleopondin) (Roof plate-specific spondin-3) (Q2TJ95)
Organism: Mus musculus (Mouse)
Function: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors, which acts as a key regulator of angiogenesis. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. Acts as a key regulator of angiogenesis by controlling vascular stability and pruning: acts by activating the non-canonical Wnt signaling pathway in endothelial cells. Can also amplify Wnt signaling pathway independently of LGR4-6 receptors, possibly by acting as a direct antagonistic ligand to RNF43 and ZNRF3 (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:16543246}.
Interaction partners:
- Leucine-rich repeat-containing G-protein coupled receptor 4
- Leucine-rich repeat-containing G-protein coupled receptor 5
- E3 ubiquitin-protein ligase ZNRF3
- E3 ubiquitin-protein ligase RNF43
- Leucine-rich repeat-containing G-protein coupled receptor 6
- Syndecan-4
Sequence:
MHLRLISCFFIILNFMEYIGSQNASRGRRQRRMHPNVSQGCQGGCATCSDYNGCLSCKPRLFFVLERIGMKQIGVCLSSCPSGYYGTRYPDINKCTKCKVDCDTCFNKNFCTKCKSGFYLHLGKCLDSCPEGLEANNHTMECVSIVHCEASEWSPWSPCMKKGKTCGFKRGTETRVRDILQHPSAKGNLCPPTSETRTCIVQRKKCSKGERGKKGRERKRKKLNKEERKETSSSSDSKGLESSIETPDQQENKERQQQQKRRARDKQQKSVSVSTVH
Protein: Zinc finger protein with KRAB and SCAN domains 4 (P373c6.1) (Zinc finger protein 307) (Zinc finger protein 427) (Q969J2)
Organism: Homo sapiens (Human)
Function: May be involved in the transcriptional activation of MDM2 and EP300 genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187, ECO:0000269|PubMed:17910948}.
Interaction partners:
- Zinc finger and SCAN domain-containing protein 32
- Zinc finger protein 174
- Zinc finger protein 397
- PiggyBac transposable element-derived protein 1
- Zinc finger and SCAN domain-containing protein 21
- Zinc finger protein 396
- Zinc finger protein with KRAB and SCAN domains 3
- SCAN domain-containing protein 1
- Zinc finger and SCAN domain-containing protein 20
- Zinc finger protein 24
Sequence:
MAREPRKNAALDAQSAEDQTGLLTVKVEKEEASALTAEVRAPCSPARGPERSRQRFRGFRYPEAAGPREALSRLRELCGQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWVREQHPESGEEVVVLLEYLERQLDEPAPQVPVGDQGQELLCCKMALLTQTQGSQSSQCQPMKALFKHESLGSQPLHDRVLQVPGLAQGGCCREDAMVASRLTPGSQGLLKMEDVALTLTPGWTQLDSSQVNLYRDEKQENHSSLVSLGGEIQTKSRDLPPVKKLPEKEHGKICHLREDIAQIPTHAEAGEQEGRLQRKQKNAIGSRRHYCHECGKSFAQSSGLTKHRRIHTGEKPYECEDCGKTFIGSSALVIHQRVHTGEKPYECEECGKVFSHSSNLIKHQRTHTGEKPYECDDCGKTFSQSCSLLEHHKIHTGEKPYQCNMCGKAFRRNSHLLRHQRIHGDKNVQNPEHGESWESQGRTESQWENTEAPVSYKCNECERSFTRNRSLIEHQKIHTGEKPYQCDTCGKGFTRTSYLVQHQRSHVGKKTLSQ