wanglab/gogpt-training-data huggingface dataset:
Protein: Aldo-keto reductase family 1 member C2 (EC 1.-.-.-) (EC 1.1.1.112) (EC 1.1.1.209) (EC 1.1.1.53) (EC 1.1.1.62) (EC 1.3.1.20) (3-alpha-HSD3) (Chlordecone reductase homolog HAKRD) (Dihydrodiol dehydrogenase 2) (DD-2) (DD2) (Dihydrodiol dehydrogenase/bile acid-binding protein) (DD/BABP) (Type III 3-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.357) (P52895)
Organism: Homo sapiens (Human)
Function: Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids. Most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentrations of NADPH. Displays a broad positional specificity acting on positions 3, 17 and 20 of steroids and regulates the metabolism of hormones like estrogens and androgens. Works in concert with the 5-alpha/5-beta-steroid reductases to convert steroid hormones into the 3-alpha/5-alpha and 3-alpha/5-beta-tetrahydrosteroids. Catalyzes the inactivation of the most potent androgen 5-alpha-dihydrotestosterone (5-alpha-DHT) to 5-alpha-androstane-3-alpha,17-beta-diol (3-alpha-diol). Also specifically able to produce 17beta-hydroxy-5alpha-androstan-3-one/5alphaDHT. May also reduce conjugated steroids such as 5alpha-dihydrotestosterone sulfate. Displays affinity for bile acids.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:8486699}.
Interaction partners:
- Aldo-keto reductase family 1 member C1
- Aldo-keto reductase family 1 member C3
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- Polyprenal reductase
- UDP-glucuronosyltransferase 2B15
- UDP-glucuronosyltransferase 1A6
- Dehydrogenase/reductase SDR family member 9
- UDP-glucuronosyltransferase 2B17
- UDP-glucuronosyltransferase 1A1
Sequence:
MDSKYQCVKLNDGHFMPVLGFGTYAPAEVPKSKALEAVKLAIEAGFHHIDSAHVYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWSNSHRPELVRPALERSLKNLQLDYVDLYLIHFPVSVKPGEEVIPKDENGKILFDTVDLCATWEAMEKCKDAGLAKSIGVSNFNHRLLEMILNKPGLKYKPVCNQVECHPYFNQRKLLDFCKSKDIVLVAYSALGSHREEPWVDPNSPVLLEDPVLCALAKKHKRTPALIALRYQLQRGVVVLAKSYNEQRIRQNVQVFEFQLTSEEMKAIDGLNRNVRYLTLDIFAGPPNYPFSDEY
Protein: Biogenesis of lysosome-related organelles complex 1 subunit 4 (BLOC-1 subunit 4) (Protein cappuccino homolog) (Q22756)
Organism: Caenorhabditis elegans
Function: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in gut granule biogenesis.
Interaction partners:
- Biogenesis of lysosome-related organelles complex 1 subunit 5
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Dysbindin protein homolog
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- SNAPIN protein homolog
- KxDL domain-containing protein
Sequence:
MTGVDDISSNVHKLVGVTAGMNTAASTGPMNLVLDKCSVVLEELRTIQILTETHSEGLSEQLKMTEKNILEMENLFDQIDQLCLFVQKAKSDLDKLEKLYNVVDRQ
Protein: Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial (ETF-QO) (ETF-ubiquinone oxidoreductase) (EC 1.5.5.1) (Electron-transferring-flavoprotein dehydrogenase) (ETF dehydrogenase) (Q921G7)
Organism: Mus musculus (Mouse)
Function: Accepts electrons from ETF and reduces ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}.
Interaction partners:
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Electron transfer flavoprotein subunit beta
- Trifunctional enzyme subunit beta, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Ubiquinone biosynthesis protein COQ9
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Hydroxysteroid dehydrogenase-like protein 2
Sequence:
MLVRLTKLSCPAYHWFHALKIKKCLPLCAPRCSSTSAVPQITTHYTVHPREKDKRWEGVNMERFAEEADVVIVGAGPAGLSAAIRLKQLAAEQGKDIRVCLVEKAAQIGAHTLSGACLDPAAFKELFPDWKEKGAPLNTPVTEDRFAILTEKHRIPVPILPGLPMNNHGNYIVRLGHLVSWMGEQAEALGVEVYPGYAAAEVLYHEDGSVKGIATNDVGIQKDGAPKTTFERGLELHAKVTVFAEGCHGHLAKQLYKKFDLRASCDAQTYGIGLKELWIIDEKKWKPGRVDHTVGWPLDRHTYGGSFLYHLNEGEPLVAVGFVVGLDYQNPYLSPFREFQRWKHHPSIQPTLEGGKRIAYGARALNEGGLQSIPKLTFPGGLLIGCSPGFMNVPKIKGTHTAMKSGSLAAESIFKQLTSENLQSKTTGLHVTEYEDNLKQSWVWKELHAVRNIRPSCHGILGVYGGMIYTGIFYWILRGMEPWTLKHKGSDSDQLKPAKDCTPIEYPKPDGQISFDLLSSVALSGTNHEHDQPAHLTLKDDSIPVNRNLSIYDGPEQRFCPAGVYEFVPLEQGDGFRLQINAQNCVHCKTCDIKDPSQNINWVVPEGGGGPAYNGM
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (Q5TGY6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGCVFCKKLEPVATAKEDAGLEGDFRSYGAADHYGPDPTKARPASSFAHIPNYSNFSSQAINPGFLDSGTIRGVSGIGVTLFIALYDYEARTEDDLTFTKGEKFHILNNTEGDWWEARSLSSGKTGCIPSNYVAPVDSIQAEEWYFGKIGRKDAERQLLSPGNPQGAFLIRESETTKGAYSLSIRDWDQTRGDHVKHYKIRKLDMGGYYITTRVQFNSVQELVQHYMEVNDGLCNLLIAPCTIMKPQTLGLAKDAWEISRSSITLERRLGTGCFGDVWLGTWNGSTKVAVKTLKPGTMSPKAFLEEAQVMKL
Protein: DUF2179 domain-containing protein (A0A0H2UPY2)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MIKKIYPIFTILLGAAIYAFGLTYFVVPHHLFEGGATGITLITFYLFKIPVSLMNLLINIPLFILAWKIFGAKSLYSSLLGTLALSGWLAFFEHIPLHIDLQGDLLITALIAGILLGIGLGIIFNAGGTTGGTDILARILNKYTHISIGKLLFILDFCILMLILLIFKDLRLVSYTLLFDFIVSRVIDLIGEGGYAGKGFMIITKRPDQLAKAINDDLGRGVTFISGQGYYSKENLKIIYCIVGRNEIVKTKEMIHRIDPQAFITITEAHEILGEGFTFEKE
Protein: Cyclin-L1 (Cyclin-L) (Cyclin Ania-6a) (Q9R1Q2)
Organism: Rattus norvegicus (Rat)
Function: Involved in pre-mRNA splicing. Functions in association with cyclin-dependent kinases (CDKs). May play a role in the regulation of RNA polymerase II (pol II). Inhibited by the CDK-specific inhibitor CDKN1A/p21 (By similarity).
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:11683997, ECO:0000269|PubMed:9651213}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UK58}. Note=Found in nuclear intrachromatin granules clusters (IGC), also called nuclear speckles, which are storage compartments for nuclear proteins involved in mRNA processing. {ECO:0000269|PubMed:11683997, ECO:0000269|PubMed:9651213}.
Interaction partners:
- cyclin-dependent kinase
Sequence:
MASGPHPTSTAAAASASSAAPSAGGSSSGTTTTTTTTTGGILIGDRLYSEVSLTIDHSVIPEERLSPTPSMQDGLDLPSETDLRILGCELIQAAGILLRLPQVAMATGQVLFHRFFYSKSFVKHSFEIVAMACINLASKIEEAPRRIRDVINVFHHLRQLRGKRTPSPLILDQNYINTKNQVIKAERRVLKELGFCVHVKHPHKIIVMYLQVLECERNQTLVQTAWNYMNDSLRTNVFVRFQPETIACACIYLAARALQIPLPTRPHWFLLFGTTEEEIQEICIETLRLYTRKKPNYELLEKEVEKRKVALQEAKLKAKGLNLDGTPALSTLGGFSPASKPSSPREVKAEEKSPVSINVKTVKKEPEDRQQASKSPYNGVRKDSKRSRNSRSASRSRSRTRSRSRSHTPRRHYNNRRSRSGTYSSRSRSRSRSHSESPRRHHNHGSPHLKAKHTREDLKSSNRHGHKRKKSRSRSQSKTRDHSDVTKKHRHERGHHRDRRERSRSFERSHKGKHHGGSRSGHGRHRR
Protein: Flap endonuclease 1 (FEN-1) (EC 3.1.-.-) (Flap structure-specific endonuclease 1) (Q7K734)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5'-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. It enters the flap from the 5'-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a genome stabilization factor that prevents flaps from equilibrating into structures that lead to duplications and deletions. Also possesses 5'-3' exonuclease activity on nicked or gapped double-stranded DNA, and exhibits RNase H activity. Also involved in replication and repair of rDNA and in repairing mitochondrial DNA.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03140}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03140}. Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03140}. Note=Resides mostly in the nucleoli and relocalizes to the nucleoplasm upon DNA damage. {ECO:0000255|HAMAP-Rule:MF_03140}.
Interaction partners:
- 3'-5' exonuclease
- DNA ligase
- DNA polymerase
- Proliferating cell nuclear antigen 1
- DNA-
- Replication factor C subunit 1
- DNA polymerase delta small subunit, putative
- Proliferating cell nuclear antigen 2
- DNA-directed DNA polymerase
- Replication factor C subunit 5, putative
Sequence:
MGIKGLTKFIADAAPNAIKEIKIESLMGRIIAIDASMSLYQFIIAIRDSEQYGNLTNESGETTSHISGLMSRSIRLMENGLKPIYVFDGAPPELKGSELEKRGEKRQKAEELLKKAKEEGNLEEIKKQSGRTVRVTRKQNEEAKKLLTLMGIPIIEAPCEAESQCAFLTKYNLAHATATEDADALVFGTKILIRNLNANATSNQNKNKNNSKRGYILTEINLEQVLKGLNLTMDEFIDFCILCGCDYCDTIKGIGSKTAYNLIKEYNCIEKIIENIDQNKYQVPSNFRFQEARKSFINPNVLPKEDIKIDWNEPQIEELKHFLIKDYNFNELRVTNYINRLLKARKVTTQRRLDNFFTACTKKSTKLIVEETKKEQTLPARKGKKRPTAGDKNKQKAVKRKIEQANANGHHKMKEENKSVDNEKNEDGIKSVDNEKNEDGIKSVDDEKNLDDEKNLDDEKNKDDEKNKDDEKNKDDEKNKDDEKNKDDEKKSLDNFSSNLFDSDKESESGNIIKNEKQNMDDEKINDNLPSLFGDHSRIRHTENKDNISDINNNNNNNNSSSNNNNISNNHFNSVSSNSTFNSSTKLKSEDTLKSNSPLKEDSPNSYNNIKNNNHTININSQINNHKEPISNNNLNNINNSTEIKKKNTLFLLPFCPKDVTNVKKKKYTQRC
Protein: RAVE complex protein Rav1 C-terminal domain-containing protein (Q580H5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Vacuolar proton pump subunit B
- ATP synthase, putative
- S-phase kinase-associated protein, putative
- SKP1 component dimerisation domain-containing protein
- V-type proton ATPase subunit C
Sequence:
MSLSGILFPQRCHHAAHAFSSRGELWTALVTDHNFLVLRGGTLCASGPLSAPCDGDGAGFEAEAHSDLPEPPPTPLACRICCSERDDDIRVIVISMSGVYVVDVTGPRMQMTYHSLCVCGGIPGCSRATVHSSPNEAQMPVCLSEWSHTQKEECARKALDAEFVTSTVLVIAYSDAVELIELSWRGRQWHERRDRNEEERSRGVMRWRVRGSYSKLAVCRVSMYLSVSQRSSLVEVFPLQPRLSDQEQRTEQSTVSFPPVLHAPREACVDSFRSLSYRTPTPSLLETAEGSAYVWRGASTRLCNYKITSLEWHRVSGYSLLCVTCHESDRGQPFIVFFIAQLCPVHEGAHVRAGLETQHGSGMVGVNSSTVHEVMLTLVPAGKVPHSSISGTPLSVHIVPNYICSHSEVQGSDKLELLCVEKDGSVFRSSYCYDPHQGNCLVRCSSTECLVPQLLGPIQKHYGDITTVDVLPAWRPRAVAFGPLTPAVAALLEAQRYRLVLRFRNGMVARVVVDLAAATVRVEAFLTLGVDAHPPLLATAVVDGVSGPQQIVLGLTQDRLFVVRRTLFSGGLTEASVSVVGPLALEHLQKLVCGSSVCGDDDAGNEMKGNTCVEESEALRSFMQAKCPEKLHMLPVLLKACGGDARKLLRQLTAKYGSPTPAAFSDKTILDEGRSCDGSGDRSKNGRFNSVTPSLLPSALKVGALRLTTGGIRCCVEMSVKDTDKPHHHQWWYIPATPLASVVGEWDSLIAHGVLPPSTALVQCLDAPLPAELLRERRPSRDGLACVSWSTSAQSLVVQSRLLPHETPLKFRPFESMAQPYNPVRVDCVKLVNNVIVVCVMGATRDEEIKTVLMVYVLDALRDVATQPVFEQELVIHNVATFFMCDTGGLFVLRRDSKSIVRWMRVTTNGVGSGHCWREYCVRGGSESQEAITTMAPLYTKSSGMNCHCYEGASCTHFVYVSSEEGLIKVCETSPKKDLRSALKGEIIVEEGGSCPYTEVGRTSTRCAKVELYHPTVITLLLAMHRPRVARAALEGILESAAEASVASQSVDDSGPRRVAEVLCQNSTKGPLDAWPVPAATEEIAGVAVRTHQLEGGEEENLCDYAAAFGLDIPLELLDQMTEVVMHAKLRGLSSQEQLTLLCTVESLRAVRVSGVANDAGASRCLFSHKFLQLQQRRRAAVASAESLPANHTSFLWAALSDCQPQLLDVLSATDGNVLSWANVEVSGVPFWLDSVHRLRAIAERVAREQYQRSRDVRECALMYCLARKPGVISALCRTCGNTKLEMFFSRDFNEAKNRSAASANAFAAVSKNLIEYGAAFFVLAAEPRNAAQVLLQREGNVSLALFLIRIATDDNPDDLSWFIEQRRLEETSCGAMSKSEEACLLWRGGRKHEALSLLTVQAPLHVLEGADRLALLKFARRRTGAERGPAQREMLRLLMHTVRLSHAAGMRLPTSLFCQEALSWLLGLSKEDAGDDPTAQGNGSAANRVATSGIVADFNSGTLAFNAFDMDGDDGERGEMAASSQSPEVAVASPMSEAVSVPTVRAGAGEIYRIDPAIVYSLLRELDFIREELQNSVSTQPQQQVQKHQNTAVCDILSCAARLLVAVGGRDPAAGAFSCLQQMLECLPQGQWGKSCVDRLSESPRYAEGEGNGMGLCTVIIALRVSLMSVATYNKDCALATALLGLPMIDDILLVEGAQTVTVNTIAVYVRTVCHVLENLRSQTAEWAQEEEKRETSMGSDMHGVDGSESLNFALYNPFEGSGSAGSGVRPNDNSGRLRNDKLRAMLLVWCTARLHLSALKELLLEASGLRSASQDSQSTQVALQQWLVSYMLCRVTLDFNAAAVQFVGDVVSVLQLRDPLPADPNGVFIEVEQQLLQIAGVLGHSLPTATSLLGDNGVCESCGQQQRYVDLLKLCVSHSEVFCQTTTCNTSLSGMTESALTLLSNTVAPRTVENLLHGRLVQGTKEALRFVEATWLQRHLTRHNYREQFLSPLREGPSVLRRDESLVLQQCGRAVTSVDYDRSSHDVIVWATAADVSVRGGYCGMLSRPNDTSPVVRPRADNGGPSFHPTREGGVTGLSPGGSSREGVLFGSPIRSLTKPAASPNSTPGSDRKLLSRRPSLPLLDGSRVAAHPRLPFFSAPHLDGCIDFYSFTAAECVKTFDCGDSRAVTGVAYSTDGCTFVAGLEDGSVRGWRFDLQPVDRAVQPLFVYHVLPTGGIRTVMFCGASQSHIAVIGFSYDSLATGQRNPEEEEGVCGLRGEPKPASAKPKSKKGLLGFPRFGNYERNTTELLLLVDLVLRPGTFAWQELSVVPEHAVYIKGLDSIMCISTNGAVALYDMWSSRLYTFVRTPNVTVTCVAASYHDDIVAVGLVDGAVLLLHSNSIRGAVQACNGSTSHVASECVAEKALASKESLLLKASRLQLIPSTSPRCDVHSVVFTPSVMLAGLGDGRVLAVGFPFSTIKFGKA
Protein: Chloroplastic import inner membrane translocase subunit HP30-2 (Hypothetical inner plastid envelope protein of 30 kDa 2) (AtHP30-2) (Hypothetical protein 30-2) (Q9FLT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with HP30-1 and HP20, triggers the import and insertion of transit sequence-less multi-pass transmembrane proteins (e.g. CEQORH) into the chloroplastic inner membrane.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:17098851}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast inner membrane {ECO:0000269|PubMed:17098851, ECO:0000269|PubMed:24248378}; Multi-pass membrane protein {ECO:0000255}. Note=Seems to be present both in chloroplast and mitochondrion. {ECO:0000269|PubMed:17098851}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM22-1
- Mitochondrial import inner membrane translocase subunit TIM22-4
- Mitochondrial import inner membrane translocase subunit TIM22-3
- Uncharacterized protein At4g28440
- Chloroplastic import inner membrane translocase subunit TIM22-2
- Outer envelope pore protein 16-4, chloroplastic
- Alternative NAD
- Triglyceride lipase
- Mitochondrial import inner membrane translocase subunit TIM10
- YlmG homolog protein 1-1, chloroplastic
Sequence:
MGKDGEGDKKRETMAVMSLMKDQQNPIQQFQVKFKEIETGFKSWLSKQKLPVEAAVVTAMGGVQGAFIGGLMGTLSPEMPQAGIDPQAMASLKQTQALVGGPLVQARNFAAITGVNAGIACVMKRIRGKEDLESAVVAAFGSGVAYSLVSAGLQGQPMNAITTAAGFAVFQGVFFKLGERFSKPSVEDPYYTRGRSMLLKLGLEKYEKNFKKGLLADPTLPLLTDSALRDVSIPPGPRLLILDHIQRDPELKGKRGSRG
Protein: Carboxypeptidase S (EC 3.4.17.4) (GLY-X carboxypeptidase) (YSCS) (P27614)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Necessary for use of certain peptides as sole nitrogen source. May also cleave intracellularly generated peptides to recycle amino acids for protein synthesis.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:11566881, ECO:0000269|PubMed:1569061}; Single-pass membrane protein {ECO:0000269|PubMed:11566881, ECO:0000269|PubMed:1569061}. Note=Lysosome-like vacuoles.
Interaction partners:
- Protein ARG5,6
- Carboxypeptidase Y
- E3 ubiquitin-protein ligase RSP5
- Protein SNA3
- Argininosuccinate synthase
- Cerevisin
- Dipeptidyl aminopeptidase B
- Aminopeptidase Y
- Saccharopepsin
- Vacuolar protein sorting-associated protein 27
Sequence:
MIALPVEKAPRKSLWQRHRAFISGIVALIIIGTFFLTSGLHPAPPHEAKRPHHGKGPMHSPKCEKIEPLSPSFKHSVDTILHDPAFRNSSIEKLSNAVRIPTVVQDKNPNPADDPDFYKHFYELHDYFEKTFPNIHKHLKLEKVNELGLLYTWEGSDPDLKPLLLMAHQDVVPVNNETLSSWKFPPFSGHYDPETDFVWGRGSNDCKNLLIAEFEAIEQLLIDGFKPNRTIVMSLGFDEEASGTLGAASLASFLHERYGDDGIYSIIDEGEGIMEVDKDVFVATPINAEKGYVDFEVSILGHGGHSSVPPDHTTIGIASELITEFEANPFDYEFEFDNPIYGLLTCAAEHSKSLSKDVKKTILGAPFCPRRKDKLVEYISNQSHLRSLIRTTQAVDIINGGVKANALPETTRFLINHRINLHSSVAEVFERNIEYAKKIAEKYGYGLSKNGDDYIIPETELGHIDITLLRELEPAPLSPSSGPVWDILAGTIQDVFENGVLQNNEEFYVTTGLFSGNTDTKYYWNLSKNIYRFVGSIIDIDLLKTLHSVNEHVDVPGHLSAIAFVYEYIVNVNEYA
Protein: Protein Wnt (Q564K5)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|RuleBase:RU003500}.
Interaction partners:
Sequence:
MRGSTFLLLSIVGIYGAILNAAAWSVNNFLMTGPKAYLTYSSSVAAGAQSGMEECKFQFGWERWNCPESALQLSTHNRLRSATRETSFVHAISSAGVMYTLTRNCSLGDFESCGCDDSRNGRVGGRGWVWGGCSDNVEFGERISKLFVDALETGHDTRALINLHNNEVGRLAVKATMKRACKCHGVSGSCSIQTCWLQLADFREIGNYLKMKYDQAHKLEMDKRRMRAGNSADSRGATAETFHHVHSTELVFLEDSPDYCTRNASLGHHGTEGRECLQTGKNLSQWERRSCRRLCTECGLKVEERRTEVVSSCNCKFHWCCTVRCEQCRQLVAKHFCARRDAAVANHTKRRNKGHRR
Protein: Protein sine oculis (Q27350)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for visual system development. May transcriptionally regulate genes necessary for optic lobe invagination and Bolwig's nerve formation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:7910468}.
Interaction partners:
- Protein phosphatase eya
- Dachshund, isoform B
- Protein groucho
- Protein atonal
- Protein teashirt
- Eyegone, isoform A
- Protein decapentaplegic
- Paired box protein Pax-6
- Homeobox protein homothorax
- Protein hedgehog
Sequence:
MLQHPATDFYDLAAANAAAVLTARHTPPYSPTGLSGSVALHNNNNNNSSTSNNNNSTLDIMAHNGGGAGGGLHLNSSSNGGGGGGVVSGGGSGGRENLPSFGFTQEQVACVCEVLQQAGNIERLGRFLWSLPQCDKLQLNESVLKAKAVVAFHRGQYKELYRLLEHHHFSAQNHAKLQALWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRSVLRDWYSHNPYPSPREKRDLAEATGLTTTQVSNWFKNRRQRDRAAEHKDGSTDKQHLDSSSDSEMEGSMLPSQSAQHQQQQQQQQHSPGNSSGNNNGLHQQQLQHVAAEQGLQHHPHQPHPASNIANVAATKSSGGGGGGGVSAAAAAQMQMPPLTAAVAYSHLHSVMGAMPMTAMYDMGEYQHL
Protein: Protein ECM5 (Extracellular matrix protein 5) (Q03214)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in cell wall organization and biogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:14562095}.
Interaction partners:
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit a
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit alpha
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit d
- Histone deacetylase RPD3
- ATP synthase subunit 4
- ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit g, mitochondrial
Sequence:
MSGHDSVTKISHILNEPVNEKVMVQNGFHESSKIADIELEIQERPSIKQWESPRSAVIPTSNHNFSPFLYTQFKSRGAAPFAPETIKSVDLVELPEGVPARVFHEKTGLFYQISPHSIPTFILAKKELPDPIKFYELVEDLGSVYGCVKLKIIPDADKFTQLNVDVDRLWFKARKQFFNSNEFQRTKIVDFYAKLYNFHNKIKKSTLTRIPSIDKRTLDLYRLRSCVKLRGGFNAVCEKKLWAQIGRELGYSGRIMSSLSTSLRSAYAKILLDFDIYEEEEQAARNNEKNEDMVESEIFRHSNSRSRDEEEPLHKKAKIHRDVFRAGSINHEFKRMRDIKHIKGFPTYFNSLTEFKLGYTQSTETTLPGYDFTFWENGMEIYDKSKYETKTSPVYNLRQYYEKSLAVFTAIVAKFGSSYPDLFAKHTTLPQKEFERLYFHLLSEHFIDFEIDTGLGLPCSMRSPGNNSSNEKFAIKNILDQWNLDNIPLNELSLLQHLDLDMANFTRTTYDIGMLFSCQGWSVSDHFLPSIDFNHLGSTKLVYSIAPKDMEKFEALIARGKSEWDTIQSRPRYSTSDDELKSFIETDFYKSFLDAEQSADYSNTGDNSKNSFPEDKIAGNTLHDGSQSDFIFEPNFILANGIKLYKTTQEQGSYIFKFPKAFTCSIGSGFYLSQNAKFAPSSWLRFSSEAAKWTSKMGFLPGLDVNQLLINALLNSNNPVLRKKCRDLISNYVVEEAENSKKLGELIGTVDVVYNKLNYISDISLESTGLSKIVVTHGALQRNLSLKEFVVLLEKPENGAHSICGIPIRDQSGNLNVCLHSYFDSASLGIALDGLDKPPTSYLLVHNEDFEKKWDVLMTSTFRNRTVPLNIIQYLISHTDSNTEFNRMLRSNFDDSLLLIEKCKKFIKTFVDVSCSVKDVDFGNGFNLRHLPLKFSDNMADNLESLYESVRKCSIEFSEKPTIIRLYHVSRQFPIDNRDIIDGNNLDLLKELYQKSLTIPLKVSYWTKLTRKICRLEWLSVYEHIFIERCDIKNEDPAKYSLPLLYSYFEFGLKYCDSEDIDKLGEVRKLILKYQDMMQKVRVFLKKDPPSKISLSDLEDVLLDIEEYRLPIQSSFFSELDYVIREIENAKKMNDVNILYNTDNIDKIDELIRKNDPKFVKFANQFNGSRLDKRPLASDNSGSVKAKQELKVFKLWNQHLDQIMQKNKFIEILPSIFRCLDLKSDKYIPLESCSKRQTKYCFCRRVEEGTAMVECEICKEWYHVDCISNGELVPPDDPNVLFVCSICTPPCMAVDNIEGVTFELDDLKRILVESLKLSLIPDPPILKNLFDVFAFALNFKNEMEKELFTNGYVNQLSSTHKIKYYLRKLKGSQCGFTNLTDPLRKHCQVKDAEAIKWLTDNGRIIITGIPN
Protein: Endoplasmic reticulum transmembrane protein (Q93XZ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU367026}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367026}.
Interaction partners:
- 2-oxoglutarate
- Proton pump-interactor 1
- Nuclear pore complex protein NUP98A
- Pyrophosphate-energized membrane proton pump 2
Sequence:
MIHLLYTVIFAEMALILLLLFKTPLRKLIILTFDRIKRGRGPVVVKTIGTTVFVVLLSSIYSLVNIQRRSEDGAVLNPTDQVLASKHLLEASLMGFVLFLSLMIDRLHHYIRELRLLRKTMETAKKQNRGFEDGKTTSGEEVKALGEEIAALKAKIKTLESESESKGKELKGAQGETEALRKQADGFLMEYDRLLEDNQNLRNQLESIGHSPEGKKGM
Protein: Dual specificity protein phosphatase (EC 3.1.3.16) (EC 3.1.3.48) (Q7SZF3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- mitogen-activated protein kinase
- mitogen-activated protein kinase
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase.
- Mitogen-activated protein kinase 14A
- Mitogen-activated protein kinase 14B
- Stress-activated protein kinase JNK
- Mitogen-activated protein kinase 8
Sequence:
MVTMDELCEMDCSVLKRLMKDDGAKCLLLDCRSFLAFSAGHLRGAVNIRCNTIVRRRAKGSVSLDQILSGDDEARSRLKSGLYSAVILYDERSSDTNTMKDDSTITLVHNALCRDTFSTEVYLLKGGYDRFSTQYPDYCLKTRTLSVSSSQSSMESSCLSCATPQHDQGGPVEILPFLFLGSALHASKKDMLDRMGISALLNVSSNCPNHFEGDYQYKCIPVEDNHKEDISSWFIEAIEFIDSVKDSNGRVLVHCQAGISRSATICLAYLMKKKRVRLEEAFEFVKQRRSIISPNFSFMGQLLQFESQVLATSCSVEAASPSASLGPKSSSTPTSPFIFSFPMSVVTHNQPGSLTYLQSPITTSPSC
Protein: Integrin beta (A0A494C0X7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}. Membrane raft {ECO:0000256|ARBA:ARBA00035630}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00035630}.
Interaction partners:
Sequence:
MLGLRPPLLALVGLLSLGCVLSQECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIFAVTSRMVKTYEKLTEIIPKSAVGELSEDSSNVVHLIKNAYNKLSSRVFLDHNALPDTLKVTYDSFCSNGVTHRNQPRGDCDGVQINVPITFQVKVTATECIQEQSFVIRALGFTDIVTVQVLPQCECRCRDQSRDRSLCHGKGFLECGICRCDTGYIGKNCECQTQGRSSQELEGSCRKDNNSIICSGLGDCVCGQCLCHTSDVPGKLIYGQYCECDTINCERYNGQVCGGPGRGLCFCGKCRCHPGFEGSACQCERTTEGCLNPRRVECSGRGRCRCNVCECHSGYQLPLCQECPGCPSPCGKYISCAECLKFEKGPFGKNCSAACPGLQLSNNPVKGRTCKERDSEGCWVAYTLEQQDGMDRYLIYVDESRECVAGPNIAAIVGGTVAGIVLIGILLLVIWKALIHLSDLREYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES
Protein: Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' theta isoform (AtB' theta) (PP2A, B' subunit, theta isoform) (Q8LF36)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The B regulatory subunit may modulate substrate selectivity and catalytic activity, and may also direct the localization of the catalytic enzyme to a particular subcellular compartment (By similarity). Associates with the serine/threonine-protein phosphatase PP2A catalytic subunit C and regulatory subunit A to positively regulates beta-oxidation of fatty acids and protoauxins in peroxisomes by dephosphorylating peroxisomal beta-oxidation-related proteins. Required for the formation of the PP2A holoenzyme that negatively regulates brassinosteroid signaling by dephosphorylating and inactivating BRI1 in the cytoplasm.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:25489022, ECO:0000269|PubMed:26517938}. Peroxisome {ECO:0000269|PubMed:19672620, ECO:0000269|PubMed:25489022}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine protein phosphatase 2A regulatory subunit B''beta
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''epsilon
- Serine/threonine protein phosphatase 2A regulatory subunit B''alpha
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''gamma
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''delta
Sequence:
MWKQILSKLPKKSSSKNHSSSSSSTSKSSDNGASKSGNSQTQNAPPVKPSADSGFKEGNLKGNGNGFTPYEALPGFKDVPNAEKQNLFVRKLSLCCVVFDFSDPTKNVKEKDIKRQTLLELVDYVASPNGKFSETVIQEVVRMVSVNIFRTLNPQPRENKVIDALDLEEEEPSMDPTWPHLQLVYEILLRLIASPETDTKLAKKYIDQSFVSRLLDLFDSEDPRERDCLKTVLHRIYGKFMVHRPFIRKSINNIFYRFVFETEKHNGIAEFLEILGSIINGFALPLKDEHKVFLVRALVPLHKPKSLQMYHQQLSYCITQFVEKDCKLADTVIRGLLKSWPVTNSSKEVMFLNELEEVLEATQPPEFQRCMVPLFRQVARCLNSLHFQVAERALFLWNNDHIENLIMQNRKVILPIIFPALERNTQKHWNQAVHSLTLNVQKIFNDIDAELFKDCLAKFREDESKEAEIGAKREATWKRLEEIGNQKQKSSL