wanglab/gogpt-training-data huggingface dataset:
Protein: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase stabilizing protein GtfB (Glycosyltransferase stabilizing protein GtfB) (orf4) (Q79T00)
Organism: Streptococcus gordonii
Function: Required for polymorphic O-glycosylation of GspB, a serine-rich repeat cell wall protein encoded upstream in the same operon. A substrate-binding protein that is part of the accessory SecA2/SecY2 system specifically required to export GspB. The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to GspB, attaching the first sugar residue. Upon coexpression in E.coli with GtfA glycosylates GspB constructs. Binds the GspB protein substrate; alone this subunit only recognizes partially glycosylated GspB, but is constrained by GtfA to also recognize unglycosylated protein. The enzyme probably modifies its tertiary conformation by opening and closing its intersubunit interfaces to accomodate the increasingly glycosylated substrate (Probable).
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01473}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01473}.
Interaction partners:
Sequence:
MIQLFDYYNQETQDLHDSLLAAGYACPTIVIEANGFLPDDMISPYTYFLGDEEGVDHPLFFNQVPVPPFWEITGDHQVARVSDMGEERARIHYASQARGRLVKQVDWLDKKGQLRLSERYNKQGRCFAKTAYKSGQEAFNTTYYSTDGQERIVENHVTGDIILTLDQEPLRIFKSRVDFIRFFLERLDLDLDHILFNSLAYSFLVSHSLTGRAGQDILFWQEPLYDELPGNMQLILDNSQLRTQTIVIPDLATYEKAMSLAAADQQQKFLHLGYHYDFKRDNYLRKDALILTHSDQIEGLDTLVQSLPQLVFRIAALTEMSPKLLSMLSYKNVVLYQNASLKQIEQLYLESDIYLDINHGGQVLQAVRKAFENNLLILGFEQTLHDRHYIAQQHIFDSSQPAQLASILEEALCGVEQMRSALQAQGRHANDVPVSLYQETLQSLLGGQHG
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 4 (A0A2R8Y7S2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTPDPPLGGTPRPGPSPGPGPSPGAMLGPSPGPSPGSAHSMMGPSPGPPSAGHPIPTQGPGGYPQDNMHQMHKPMESMHEKGMSDDPRYNQMKGMGMRSGGHAGMGPPPSPMDQHSQGYPSPLGGSEHASSPVPASGPSSGPQMSSGPGGAPLDGADPQALGQQNRGPTPFNQNQLHQLRAQIMAYKMLARGQPLPDHLQMAVQGKRPMPGMQQQMPTLPPPSVSATGPGPGPGPGPGPGPGPAPPNYSRPHGMGGPNMPPPGPSGVPPGMPGQPPGGPPKPWPEGPMANAAAPTSTPQKLIPPQPTGRPSPAPPAVPPAASPVMPPQTQSPGQPAQPAPMVPLHQKQSRITPIQKPRGLDPVEILQEREYRLQARIAHRIQELENLPGSLAGDLRTKATIELKALRLLNFQRQLRQEVVVCMRRDTALETALNAKAYKRSKRQSLREARITEKLEKQQKIEQERKRRQKHQEYLNSILQHAKDFKEYHRSVTGKIQKLTKAVATYHANTEREQKKENERIEKERMRRLMAEDEEGYRKLIDQKKDKRLAYLLQQTDEYVANLTELVRQHKAAQVAKEKKKKKKKKKAENAEGQTPAIGPDGEPLDETSQMSDLPVKVIHVESGKILTGTDAPKAGQLEAWLEMNPGYEVAPRSDSEESGSEEEEEEEEEEQPQAAQPPTLPVEEKKKIPDPDSDDVSEVDARHIIENAKQDVDDEYGVSQALARGLQSYYAVAHAVTERVDKQSALMVNGVLKQYQIKGLEWLVSLYNNNLNGILADEMGLGKTIQTIALITYLMEHKRINGPFLIIVPLSTLSNWAYEFDKWAPSVVKVSYKGSPAARRAFVPQLRSGKFNVLLTTYEYIIKDKHILAKIRWKYMIVDEGHRMKNHHCKLTQVLNTHYVAPRRLLLTGTPLQNKLPELWALLNFLLPTIFKSCSTFEQWFNAPFAMTGEKVDLNEEETILIIRRLHKVLRPFLLRRLKKEVEAQLPEKVEYVIKCDMSALQRVLYRHMQAKGVLLTDGSEKDKKGKGGTKTLMNTIMQLRKICNHPYMFQHIEESFSEHLGFTGGIVQGLDLYRASGKFELLDRILPKLRATNHKVLLFCQMTSLMTIMEDYFAYRGFKYLRLDGTTKAEDRGMLLKTFNEPGSEYFIFLLSTRAGGLGLNLQSADTVIIFDSDWNPHQDLQAQDRAHRIGQQNEVRVLRLCTVNSVEEKILAAAKYKLNVDQKVIQAGMFDQKSSSHERRAFLQAILEHEEQDEEEDEVPDDETVNQMIARHEEEFDLFMRMDLDRRREEARNPKRKPRLMEEDELPSWIIKDDAEVERLTCEEEEEKMFGRGSRHRKEVDYSDSLTEKQWLKKITGKDIHDTASSVARGLQFQRGLQFCTRASKAIEEGTLEEIEEEVRQKKSSRKRKRDSDAGSSTPTTSTRSRDKDDESKKQKKRGRPPAEKLSPNPPNLTKKMKKIVDAVIKYKDSSSGRQLSEVFIQLPSRKELPEYYELIRKPVDFKKIKERIRNHKYRSLNDLEKDVMLLCQNAQTFNLEGSLIYEDSIVLQSVFTSVRQKIEKEDDSEGEESEEEEEGEEEGSESESRSVKVKIKLGRKEKAQDRLKGGRRRPSRGSRAKPVVSDDDSEEEQEEDRSGSGSEED
Protein: Complement factor B-like protease (EC 3.4.21.-) [Cleaved into: Complement factor B-like protease Ba fragment; Complement factor B-like protease Bb fragment] (P81475)
Organism: Gallus gallus (Chicken)
Function: Required in both the classical and alternate pathways of the complement system.
Subcellular location: Secreted.
Interaction partners:
Sequence:
ATTRCDPTLIPIAGGWFELLEGGEALRYRCPPGHIPTPLARRSCGPDGQXEPLXXXXXXXXXXXXXXXXKCRAVWCPPPQDMEHGSFWPRLPRYPPGSRLHFQCFQGFNLRGAPNRTCGEGGRWSGVTPVCDDGSGDCPAPPVXXXXXKEGSRYLLEDTVRFRCGPGLVLLGSAVRQCLEGGVWSGTEPQCRAPLSFDTPSDVAASFMASLSQSVERADSNSSHGPTEKLPRXIRVDGSAXLNVFLLXDA
Protein: Sugar transport protein 13 (Hexose transporter 13) (Multicopy suppressor of snf4 deficiency protein 1) (Q94AZ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport.
Subcellular location: Cell membrane {ECO:0000305|PubMed:15308754}; Multi-pass membrane protein {ECO:0000305|PubMed:15308754}.
Interaction partners:
- At2g39500/F12L6.16
- Bidirectional sugar transporter SWEET12
- Sucrose transport protein SUC3
- Sucrose transport protein SUC2
- Haloacid dehalogenase-like hydrolase domain-containing protein At4g39970
- UDP-galactose/UDP-glucose transporter 5B
- Beta-fructofuranosidase, insoluble isoenzyme CWINV1
Sequence:
MTGGGFATSANGVEFEAKITPIVIISCIMAATGGLMFGYDVGVSGGVTSMPDFLEKFFPVVYRKVVAGADKDSNYCKYDNQGLQLFTSSLYLAGLTATFFASYTTRTLGRRLTMLIAGVFFIIGVALNAGAQDLAMLIAGRILLGCGVGFANQAVPLFLSEIAPTRIRGGLNILFQLNVTIGILFANLVNYGTAKIKGGWGWRLSLGLAGIPALLLTVGALLVTETPNSLVERGRLDEGKAVLRRIRGTDNVEPEFADLLEASRLAKEVKHPFRNLLQRRNRPQLVIAVALQIFQQCTGINAIMFYAPVLFSTLGFGSDASLYSAVVTGAVNVLSTLVSIYSVDKVGRRVLLLEAGVQMFFSQVVIAIILGVKVTDTSTNLSKGFAILVVVMICTYVAAFAWSWGPLGWLIPSETFPLETRSAGQSVTVCVNLLFTFIIAQAFLSMLCHFKFGIFIFFSAWVLIMSVFVMFLLPETKNIPIEEMTERVWKKHWFWARFMDDHNDHEFVNGEKSNGKSNGFDPSTRL
Protein: Beclin-1 (Coiled-coil myosin-like BCL2-interacting protein) (Protein GT197) [Cleaved into: Beclin-1-C 35 kDa; Beclin-1-C 37 kDa] (Q91XJ1)
Organism: Rattus norvegicus (Rat)
Function: Plays a central role in autophagy. Acts as core subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Essential for the formation of PI3KC3-C2 but not PI3KC3-C1 PI3K complex forms. Involved in endocytosis. May play a role in antiviral host defense (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O88597}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endosome membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q14457}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14457}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Note=Interaction with ATG14 promotes translocation to autophagosomes. Expressed in dendrites and cell bodies of cerebellar Purkinje cells. {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}.; SUBCELLULAR LOCATION: [Beclin-1-C 35 kDa]: Mitochondrion {ECO:0000250|UniProtKB:O88597, ECO:0000250|UniProtKB:Q14457}. Nucleus {ECO:0000250|UniProtKB:Q14457}. Cytoplasm {ECO:0000250|UniProtKB:Q14457}.; SUBCELLULAR LOCATION: [Beclin-1-C 37 kDa]: Mitochondrion {ECO:0000250|UniProtKB:O88597}.
Interaction partners:
- Activating molecule in BECN1-regulated autophagy protein 1
- Beclin 1-associated autophagy-related key regulator
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphoinositide 3-kinase regulatory subunit 4
- Nuclear receptor-binding factor 2
- UV radiation resistance associated
- Vacuole membrane protein 1
- non-specific serine/threonine protein kinase
Sequence:
MEGSKASSSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGESQEEEANSGEEPFIETRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEMLEQMNEGDSEQLQRELKELALEEERLIQELEDVEKNRKVVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQMQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSAPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK
Protein: Dynamin-like GTPase OPA1, mitochondrial (EC 3.6.5.5) (E5KLJ9)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
Sequence:
MWRLRRAAVACEVCQSLVKHSSGIKGSLPLQKLHLVSRSIYHSHHPTLKLQRPQLRTSFQQFSSLTNLPLRKLKFSPIKYGYQPRRNFWPARLATRLLKLRYLILGSAVGGGYTAKKTFDQWKDMIPDLSEYKWIVPDIVWEIDEYIDFGHKLVSEVIGASDLLLLLGSPEETAFRATDRGSESDKHFRKGLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQKRKVSDKEKIDQLQEELLHTQLKYQRILERLEKENKELRKLVLQKDDKGIHHRKLKKSLIDMYSEVLDVLSDYDASYNTQDHLPRVVVVGDQSAGKTSVLEMIAQARIFPRGSGEMMTRSPVKVTLSEGPHHVALFKDSSREFDLTKEEDLAALRHEIELRMRKNVKEGCTVSPETISLNVKGPGLQRMVLVDLPGVINTVTSGMAPDTKETIFSISKAYMQNPNAIILCIQDGSVDAERSIVTDLVSQMDPHGRRTIFVLTKVDLAEKNVASPSRIQQIIEGKLFPMKALGYFAVVTGKGNSSESIEAIREYEEEFFQNSKLLKTSMLKAHQVTTRNLSLAVSDCFWKMVRESVEQQADSFKATRFNLETEWKNNYPRLRELDRNELFEKAKNEILDEVISLSQVTPKHWEEILQQSLWERVSTHVIENIYLPAAQTMNSGTFNTTVDIKLKQWTDKQLPNKAVEVAWETLQEEFSRFMTEPKGKEHDDIFDKLKEAVKEESIKRHKWNDFAEDSLRVIQHNALEDRSISDKQQWDAAIYFMEEALQARLKDTENAIENMVGPDWKKRWLYWKNRTQEQCVHNETKNELEKMLKCNEEHPAYLASDEITTVRKNLESRGVEVDPSLIKDTWHQVYRRHFLKTALNHCNLCRRGFYYYQRHFVDSELECNDVVLFWRIQRMLAITANTLRQQLTNTEVRRLEKNVKEVLEDFAEDGEKKIKLLTGKRVQLAEDLKKVREIQEKLDAFIEALHQEK
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q4Q2E8)
Organism: Leishmania major
Interaction partners:
- Serine/threonine-protein kinase TOR
- Serine/threonine-protein kinase TOR
- Uncharacterized protein
- Uncharacterized protein
- Raptor N-terminal CASPase-like domain-containing protein
- Raptor N-terminal CASPase-like domain-containing protein
- Putative serine-threonine kinase
- Putative ras-like small GTPases
- Putative ras-like small GTPases
- Putative ras-like small GTPases
Sequence:
MAESLAPNDVGGISVTKLFSSDSTAALGQQLSSIFSNLNSTPNDRQQRAGECLSALTDTLFLHENELGANESLHERIIVLIDGTFCTSVDKGCSSFRVVFDVKWKDQHEKRNRCFVLLLSRAFKCTTPEDCLKVIQCIGEVLEDNIRTTTDLLADHVEPLLRDLFAADVHRRTVACEVLAKIVSTTTFIIKRNPTLLELLTSSCAPLVTLKDAMETRNLWHRTALIRLTSALVENCYEVTPAVAKDVADLVFRYMRAAADESQLVGVLSALIHVAVTPAFVSAPWDLPQLVCFLCDTDWSVYAVATRVAAVAAINKVAVFICQEEKACYEALRTRSLEFISSDDAVEVVTEGLELLKEMEVLERELHLGGAVVNALCACIQRLPHVPIIYELLELIRERYSDLEVKSIYSLLEGYLDTKQELLNFGKVNALLRFAGPRIRLDDPRVAQLRINVGANQPVPVILHSLPLLTTLQRTEQLHEVLEILSHDDRGVRRVAVSTALELCEIIMERNKFRNATQEGSAQRMQWLDEEVRNAVERVLDVAVADRDPGIRLWALQHLTVPFFPYLCLCDNLDAIFMARNDNDKATRDQALTLLCQLLPYHPTVVQPQLQRAQEYMLHDVATMDASVSFAVCKAGLLKMCVDHDALLIEGSTVEAIVLRRLEAQPFISRSLSIALLQLIRSILERTASQHHSDFHSFLRPLLLIVNGGDSCTRRREALETLTAFISHITKTDISGLSEVYRAAARIIRRETEEEESVTIAAMKVLSSIGAVTPVKMRHVFRMVESDEMEEEEVVVTPALAHCKPRLRISTDMPERYPSVVLYYLVRSLQLALDPKQQVDTLVAVRTMLHDVEGKVELNLLTQLLPQLQTWLRDPERAFLYETVLGLMNDLAILLCQFKGTVAPSVGYELLRSVQAFCLRPQASQKPFSAYVVQLLDSLAKGIPAQEMRDNRWAIEFIHQRLSQNKNDLDLVHRVVKSLESFIAVMHEKELQMILPHVLQCIEPAKASPGGKLSKSKDINDACFDFLNFVMAKQLTLVKHCCAQIVHTIMWYIELSDSNEEMDVGLNTLATLVDTVKMPAKRFIMPIERVAVRNGFPPQYFVNLVQSAAGGAKTHMTTSSGTGLNPDRPITLVSHLPRLSQAEFEHEMRSTPRSENVLIDVLDVRHHHGQTMIDFRFHPGTDTAACCNLFSRKATDNKSAMRRNLGILRVEQTEERSRPVGAEVIKALANLPVAKTKKREQSWVLWLHNATVTLLRNSPYAVLRDTCAVADRNTELAKDLFPFAVAAVCGHLETPLRAQLMDIFDRALAAAPADVKQGLFCFAEFMESERDDDRVKLVKAMRESVVSVDRESTSQKFGINYDQDPERGVIVTKLAPNGVGARAGVPIGAQLLAINDIPVRAVSDIRGLIEGLTHIELLLSYEVEEKTKSKPKPLMNLEVLASVAFSGEMHIKAIYFNEVLFESLSSKICKIADRKDSQMRRVMTIAEDLIQYYRHLNMTMTANGLLKTLTRKFSDEIFAPEQFGFEEIASLEQLNWWSEALRRYEARMDSFGTRCLEVASLVGVLRCEQALGHSSRVQELAEQYWEQLPADAQREVAPFRAKAAFCLGAWDTFDALALDKRMQSCFGVVERCAALFRAECHDELLRYTDKVRESMLESFADSLNENYNRAYEGMTRLQHLRHFEELVSFTTACEERQALLKRVWHRRLVQMSSRPDDLMTVLSINSLVLEPEDDLHSYVYVIRCLCKSQWFSHAEHLLQRLLRENASLEVLCECDPELIHTYIKYVYLAKDKHGAYVELKNILSAVEVDPEDPRAEMWGQCWLLLGEWTMYLFPECGEEAIKELMCATELGPNSAAAFHSLGILHCDLARDPSTQGEVQNNHLICCINSLFKSIQLCNDVPGSLVMQDVLRILSVWFANSGIREINEAVHHGVQVVADHVWLNVVPQLIARIGIEARYARAILTDLLIRVGSQYSHALIYPLTVAEKSPDAVRRHMAERVIMGMRDIPENDRIVKEASLVSNEMVRIAILWTEKWHAAIQQAAYKPNNTAAIFSMLQPLYAELDRASTPNELSFRCNFGQTLRRAKVALEEAKTDEAWGFLRQVYAQLRRGVLERRLYMSDVSPTLDGIQDSIVAVPGTFEHDKPLITIRKFHSRVYVMPSKQKPRRIGLDASDGKKYRFLLKGHEDMRQDERVMQFIRLIDTIFQSDNAASAIGLSIPQYAVIPLTDNVGVVGWVENTETIYKMLETYRQAHEVSVYEEVNLIMKKGGLDTIEDYHRLPKQQRKALLNYAMENTPKNELRHIFWDHNDTCEQWLSYRQTYGQTLAAMSMVGYVLGLGDRHLNNLMLQGNGTVVHIDFGDCFEVAMHRALYAEAVPFRLTRLLVCALGITGVDGLYRMTCELAMKNLHRHSENLLSILEAFIYDPIINWRLNTVNDVTEKSGSKSAQQESNNGGTAALAGETAAAACLGIDNAAQAEAKPVAMQLSKSVSKPVPHSALPGESQMFENGEETRNQQGDLALARVQAKLTGQDFGVINSSFSMMRSSRRLEAGGSQPQGSSWGSNSLAGFTDSPKDSFAAPLLTTYLSLRVLNGGAESLDVPHQVDRLIQEATSLDNLSDAFLTGWAPFW
Protein: Putative gustatory receptor 59c (Q9W1U5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Gustatory and pheromone receptor 32a
- Putative gustatory receptor 58c
- Putative gustatory receptor 98b
- Gustatory receptor
- Putative gustatory receptor 28a
- Gustatory receptor for bitter taste 22e
- Ionotropic receptor 7a
- Putative gustatory receptor 89a
- Putative gustatory receptor 22f
- Putative gustatory receptor 98d
Sequence:
MVDLVKTILLIAYWYGLAVGVSNFEVDWLTGEAIATRRTTIYAAVHNASLITLLILFNLGNNSLKSEFISARYLHEYFFMLMTAVRISAVLLSLITRWYQRSRFIRIWNQILALVRDRPQVVRGRWYRRSIILKFVFCVLSDSLHTISDVSAQRKRITADLIVKLSLLATLTTIFNMIVCQYYLAMVQVIGLYKILLQDLRCLVRQAECICSIRNRRGGVYSIQCCSLADQLDLIAERHYFLKDRLDEMSDLFQIQSLSMSLVYFFSTMGSIYFSVCSILYSSTGFGSTYWGLLLIVLSTASFYMDNWLSVNIGFHIRDQQDELFRVLADRTLFYRELDNRLEAAFENFQLQLASNRHEFYVMGLFKMERGRLIAMLSSVITHTMVLVQWEIQNDES
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (H0YLB7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MENTEGYRCDDFVVNDTKLGLVQKVREHLQNLENSAFTADRHKKRKLLENSTLNSKLLKVNGSTTAICATGLRNLGNTCFMNAILQSLSNIEQFCCYFKELPAVELRNGKTAGRRTYHTRSQGDNNVSLVEEFRKTLCALWQGSQTAFSPESLFYVVWKIMPNFRGYQQQDAHEFMRYLLDHLHLELQGGFNGVSRSAILQENSTLSASNKCCINGASTVVTAIFGGILQNEVNCLICGTESRKFDPFLDLSLDIPSQFRSKRSKNQENGPVCSLRDCLRSFTDLEELDETELYMCHKCKKKQKSTKKFWIQKLPKVLCLHLKRFHWTAYLRNKVDTYVEFPLRGLDMKCYLLEPENSGPESCLYDLAAVVVHHGSGVGSGHYTAYATHEGRWFHFNDSTVTLTDEETVVKAKAYILFYVEHQAKAGSDKL
Protein: Cathepsin D (EC 3.4.23.5) [Cleaved into: Cathepsin D 12 kDa light chain; Cathepsin D 9 kDa light chain; Cathepsin D 34 kDa heavy chain; Cathepsin D 30 kDa heavy chain] (P24268)
Organism: Rattus norvegicus (Rat)
Function: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation.
Subcellular location: Lysosome. Melanosome {ECO:0000250}. Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Cathepsin B
- Lysosome-associated membrane glycoprotein 1
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- BH3-interacting domain death agonist
- Angiotensinogen
- Procathepsin L
- Lysosome-associated membrane glycoprotein 2
- Cathepsin S
- Insulin-2
Sequence:
MQTPGVLLLILGLLDASSSALIRIPLRKFTSIRRTMTEVGGSVEDLILKGPITKYSMQSSPRTKEPVSELLKNYLDAQYYGEIGIGTPPQCFTVVFDTGSSNLWVPSIHCKLLDIACWVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCKSDLGGIKVEKQIFGEATKQPGVVFIAAKFDGILGMGYPFISVNKVLPVFDNLMKQKLVEKNIFSFYLNRDPTGQPGGELMLGGTDSRYYHGELSYLNVTRKAYWQVHMDQLEVGSELTLCKGGCEAIVDTGTSLLVGPVDEVKELQKAIGAVPLIQGEYMIPCEKVSSLPIITFKLGGQNYELHPEKYILKVSQAGKTICLSGFMGMDIPPPSGPLWILGDVFIGCYYTVFDREYNRVGFAKAATL
Protein: Valerianol synthase TPS1B (EC 4.2.3.204) (Terpene synthase 1b) (ChTps1b) (A0A348AUV6)
Organism: Camellia hiemalis (Camellia)
Function: Terpene synthase that catalyzes the biosynthesis of the terpene valerianol, which is a volatile compound of floral scent.
Interaction partners:
Sequence:
MASSQVGDMVNGNAEPTRHLAKFPPSLWGDRFTSFTLDKQLWDKYGNEIEVLKEQVRSMVVAGGRKAAEQINLINVLQRLGVSYHFEKEIEEQLEQLFAKFEDNEDYDLFTIALHFRIFRQHGYKMSCDVFNKFRDSNGEFKETMSNDVQGMLSLYEATYLKIRGEGFLDEAHAFTIAQLESLVEGPHLSSDLSEQVMHALKQSIHRGFPRLEAKHFISFYEKDASRNETLLRLAKLDFNQLQLSHREELCHIFRWWKELDLISKVPYARDRAVECFFWSTCAYYEPQHSVGRAVLTKIMLLLSVTDDTYDAYGTYNELKIYTNAVQRWDVSAMDELPDYMKALYRALLNVYDEVERDLAKQGRAYGVHHSKEAFKEIVRSYEIEAEWFKEGYVASFEEYMKNALVTSTGRLHTTSCFMGLEADVATTEAFEWILTKPKMVAASGAIGRLVDDVMSHDEEQERGHVATGLDCYMKQHGVSKQEAIVELYKMIENAWRDINEEMLKPTAISMKLLIRVLNLSRISDVVYKYVDGYTHPEIIKDHVISLFEDPIPM
Protein: Myosin tail domain-containing protein (Q3UW38)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKVALEQTERTRRLSEQELLDSSDRVQLLHSQNTSLINTKKKLEADLAQCQAEVENSIQESRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELESELDAEQKRGAEALKGAHKYERKVKEMTYQAEEDRKNILRLQDLVDKLQAKVKSYKRQAEEAEEQANTQLSRCRRVQHELEEAEERADIAESQVNKLRAKSRDVGGQKMEE
Protein: Napsin-A (EC 3.4.23.-) (Aspartyl protease 4) (ASP4) (Asp 4) (Napsin-1) (TA01/TA02) (O96009)
Organism: Homo sapiens (Human)
Function: May be involved in processing of pneumocyte surfactant precursors.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Keratin, type II cytoskeletal 7
- Homeobox protein Nkx-2.1
- Keratin, type I cytoskeletal 20
- Protein LIAT1
- Pulmonary surfactant-associated protein B
- Keratin, type II cytoskeletal 5
- Surfactant protein C
- Paired box protein Pax-8
- Homeobox protein CDX-2
- Hepatocyte nuclear factor 1-beta
Sequence:
MSPPPLLQPLLLLLPLLNVEPSGATLIRIPLHRVQPGRRILNLLRGWREPAELPKLGAPSPGDKPIFVPLSNYRDVQYFGEIGLGTPPQNFTVAFDTGSSNLWVPSRRCHFFSVPCWLHHRFDPKASSSFQANGTKFAIQYGTGRVDGILSEDKLTIGGIKGASVIFGEALWEPSLVFAFAHFDGILGLGFPILSVEGVRPPMDVLVEQGLLDKPVFSFYLNRDPEEPDGGELVLGGSDPAHYIPPLTFVPVTVPAYWQIHMERVKVGPGLTLCAKGCAAILDTGTSLITGPTEEIRALHAAIGGIPLLAGEYIILCSEIPKLPAVSFLLGGVWFNLTAHDYVIQTTRNGVRLCLSGFQALDVPPPAGPFWILGDVFLGTYVAVFDRGDMKSSARVGLARARTRGADLGWGETAQAQFPG
Protein: Cellular tumor antigen p53 (K7PPA8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}. Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
Interaction partners:
Sequence:
MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD
Protein: Spermatogenesis-associated protein 24 (Testis protein T6441 homolog) (Q86W54)
Organism: Homo sapiens (Human)
Function: Binds DNA with high affinity but does not bind to TATA boxes. Synergises with GMNN and TBP in activation of TATA box-containing promoters and with GMNN and TBPL1 in activation of the NF1 TATA-less promoter. May play a role in cytoplasm movement and removal during spermiogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19515240}. Nucleus, nucleolus {ECO:0000269|PubMed:19515240}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19515240}. Note=Associated with chromatin. {ECO:0000250}.
Interaction partners:
Sequence:
MATPLGWSKAGSGSVCLALDQLRDVIESQEELIHQLRNVMVLQDENFVSKEEFQAVEKKLVEEKAAHAKTKVLLAKEEEKLQFALGEVEVLSKQLEKEKLAFEKALSSVKSKVLQESSKKDQLITKCNEIESHIIKQEDILNGKENEIKELQQVISQQKQIFRNHMSDFRIQKQQESYMAQVLDQKHKKASGTRQARSHQHPREK
Protein: Alpha-tubulin N-acetyltransferase 1 (Alpha-TAT) (Alpha-TAT1) (TAT) (EC 2.3.1.108) (Acetyltransferase mec-17 homolog) (Q6PH17)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules. Promotes microtubule destabilization and accelerates microtubule dynamics; this activity may be independent of acetylation activity. Acetylates alpha-tubulin with a slow enzymatic rate, due to a catalytic site that is not optimized for acetyl transfer. Enters the microtubule through each end and diffuses quickly throughout the lumen of microtubules. Acetylates only long/old microtubules because of its slow acetylation rate since it does not have time to act on dynamically unstable microtubules before the enzyme is released. May be involved in neuron development. Acetylates alpha-tubulin in neurons, but not in cilia.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03130}. Membrane, clathrin-coated pit {ECO:0000255|HAMAP-Rule:MF_03130}. Cell junction, focal adhesion {ECO:0000255|HAMAP-Rule:MF_03130}. Cell projection, axon {ECO:0000255|HAMAP-Rule:MF_03130}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03130}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03130}.
Interaction partners:
- Protein deacetylase HDAC6
- NAD-dependent protein deacetylase sirtuin-2
Sequence:
MDFPYDLNALFPERISVLDSNLSAGRKAHGRPDPLPQVTTVIDELGKASSKAQQLPAPITSAAKLQANRHHLYLLKDGEQNGGRGVIVGFLKVGYKKLFLLDQRGAHLETEPLCVLDFYVTETLQRHGYGSELFDFMLKHKQVEPAQMAYDRPSPKFLSFLEKRYDLRNSVPQVNNFVVFAGFFQSRSAVQLRKVPPRKPEGEIKPYSLMEREVVREEQRVLPWPFVRPGGPPHSPPLLPSSPQSRSLSVGSSPSRAPLRPAAATVLQQGQTPSSPLNDSCRAKRTSSLNRSRLSFH
Protein: Dual specificity testis-specific protein kinase 1 (EC 2.7.12.1) (Testicular protein kinase 1) (Q63572)
Organism: Rattus norvegicus (Rat)
Function: Dual specificity protein kinase activity catalyzing autophosphorylation and phosphorylation of exogenous substrates on both serine/threonine and tyrosine residues. Regulates the cellular cytoskeleton by enhancing actin stress fiber formation via phosphorylation of cofilin and by preventing microtubule breakdown via inhibition of TAOK1/MARKK kinase activity. Inhibits podocyte motility via regulation of actin cytoskeletal dynamics and phosphorylation of CFL1 (By similarity). Positively regulates integrin-mediated cell spreading, via phosphorylation of cofilin (By similarity). Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of ciliary vesicle directional trafficking to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1 (By similarity). Probably plays a central role at and after the meiotic phase of spermatogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22302232}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:22302232}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q15569}. Cell projection, lamellipodium {ECO:0000269|PubMed:22302232}. Note=Colocalizes with SPRY4 in vesicular spots in the cytoplasm (By similarity). Localized to F-actin-rich lamellipodia at the cell periphery following fibronectin-mediated cell adhesion of Schwann cells (PubMed:22302232). {ECO:0000250|UniProtKB:Q15569, ECO:0000269|PubMed:22302232}.
Interaction partners:
- Alpha-parvin
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L2
- Adhesion G protein-coupled receptor L3
Sequence:
MAGERPPLRGPGPGETPVEGPGGAGGGPGRGRPSSYRALRSAVSSLARVDDFDCAEKIGAGFFSEVYKVRHRQSGQVMVLKMNKLPSNRSNTLREVQLMNRLRHPNILRFMGVCVHQGQLHALTEYMNGGTLEQLLSSPEPLSWPVRLHLALDIAQGLRYLHAKGVFHRDLTSKNCLVRREDGGFTAVVGDFGLAEKIPVYREGARKEPLAVVGSPYWMAPEVLRGELYDEKADVFAFGIVLCELIARVPADPDYLPRTEDFGLDVPAFRTLVGNDCPLPFLLLAIHCCSMEPSARAPFTEITQHLEQILEQLPEPTPLAKMPLAKAPLTYNQGSVPRGGPSATLPRSDPRLSRSRSDLFLPPSPESPPSWGDNLTRVNPFSLREDLRGGKIKLLDTPCKPATPLPLVPPSPLTSTQLPLVASPESLVQPETPVRRCRSLPSSPELPRRMETALPGPGPSPVGPSTEERMDCEGSSPEPEPPGPAPQLPLAVATDNFISTCSSASQPWSARPGPSLNNNPPAVVVNSPQGWAREPWNRAQHSLPRAAALERTEPSPPPSAPREQEEGLPCPGCCLSPFSFGFLSMCPRPTPAVARYRNLNCEAGSLLCHRGHHAKPPTPSLQLPGARS