wanglab/gogpt-training-data huggingface dataset:
Protein: Neuron navigator 2 (F1LR12)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKSGLPKPVHSAAPILHVPPARTGPQPCYLKLGSKVEVSKTAYTSQIPLKSQGLQEPTGEGLPLRKSSSLENGFDTQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAQIIQVVANDKIEDINGCPKNRSQMIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYKQQQQQQQPEKQHLSSSPLPPAGSQVAGAPSQCQSGILQQQGLATPQAPCQPLQPASHQQAKTQAEMQSSASAKDSCQSKIIRFTLGQKKISRLPGPTARVAAAGSEAKTRGGSTAANNRRSQSFNNYDKSKPVPSPPQPAPPSNHEKEPLASSASSHPGMSENVPASLESSPSIPVNCSSSAIPQPSMTSKPWRSKSLSVKHSATSSMLSVKPAGPEAPRPTPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERLEILPSFEESEELEVANRAPPTAGPASSSPKIALKGIAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKETGKDLTKRVSVTDRPDLKEEPKEELSGVVVTEMPKKSSKIASFIPKGGKLSSTKKEATAPSHSGIPKPGMKNMPGKSPSAPIPPKEGERSRGKLSSGLPPQKPQLDSRHSSSSSSLASSEGKGPGGTTLNHSISSQTVSGSIGTTQTTGSNTVSVQLPQPQQQYSHPNTATVAPFLYRSQTDTEGNVTAESSSAGVSMEPSHYTKSGQPALEELTAPARQAASSHRGAGVKQSCTLETTFDTNVTTEISGRSILSLTGRPTPLSWRLGQSSPRLQAGDAPSMGNGYPPRANASRFISAEAGRYVYSAPLRRQLASRGSSICHVDVSDKVGDEVDLEGISMDAPGYMSDGDVLSKNIRTDDITSGYMTDGGLGLYTRRLNRLPDGMAVVRETLQRNTSLGLGDADSWDDSSSVSSGISDTIDNLSTDDINTSSSISSYANTPASSRRNLDVQTDAEKHSQVERNSLWSGDDIKRSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSGKKNPVLSQTGSWRRGMTAEVGITMPRTKPSAQTGTLKTSGTGKTDDAKVSEKGRLSPKASQVKRSPSDAGRSSGDESKKTLPSSSRTPTANANSFGFKKQSGSAAGLAMITASGATVTSRSATLGKIPKSSALVGRSTGRKTSMDGAPNQDDGYLSLSSRTNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMSSKSAGLPVPKLREPSKTSLGSSLPGLVNQTDKEKGISSDNESVASCNSVKVNPATQPVSNSTQATLQPGTKYTDVASPTLRRLFGGKPTKQVPIATAETMKSAVVISNPHATMTQQGNLESPSGSGVLSSGSSSPLYSKNVDLNQSPLASSPSSAHSGPSNSLTWGTSSSAVSKDGLGFQSVSSLHTSCESIDISLGSGGGLSHNSSPGPVASTKEDSLMPFVRTSSVKTTLSESPLSSPAASPKFCRSTLPPEPLGSSACLYTPTSQLRTQEDTKEWFRSHSAGGLQETATNSPFSSGSSVTSPSGTRFNFSQLASPTAVTQMSLSNPTMLRTHSLSNADGQYDPYTDSRFRNSSMSLDEKSRTMSRSGSFRDGFEEEEKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAAQAAINGVINTPELNCKGNGSAQATDLRIRRQHSSDSVSSINSATSHSSVGSNIESDSKKKKRKNWLRSSFKQAFGKKKSPKSASSHSDIEEMTDSSLPSSPKLPHNGSTGSTPLLRNAHSNSLISECMDSEAETVMQLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQGSGCSRAPSQVSISASPRQSLGLSQHSLNLTESTSLDMLLDDTGECSARKEGGRHVKIVVSFQEAMKWKEDSRPHLFLIGCIGVSGKTKWDVLDGVVRRLFKEYIIHVDPVSQLGLNSDSVLGYSIGEIKRSNTSETPELLPCGYLVGENTTILVTVKGLTENSLDSLVFESLIPKPILQRYVSLLTEHRRIILSGPSGTGKTYLANRLSEYVVLREGRELTDGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDMPLVIILDNLHHVSSLGEIFNGLLNCKYHKCPYIIGTMNQATSSTPNLQLHHNFRWVLCANHTEPVKGFLGRFLRRKLMETEISGRVRNAELVKIINWIPKVWHHLNRFLEAHSSSDVTIGPRLFLSCPIDVDGSRVWFTDLWNYSIIPYLLEAVREGLQLYGRRAPWEDPAKWVMDTYPWAASPQQHEWPPLLQLRPEDVGFDGYSLPREGSTSKQVPPSDTEGDPLMNMLMRLQEAANYSSPQSYDSDSNSNSHHDDILDSSLESTL
Protein: Polypyrimidine tract-binding protein (SMPTB) (Q80XZ1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- ELAV-like protein 1
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Heterogeneous nuclear ribonucleoprotein L
- Heterogeneous nuclear ribonucleoprotein K
- RCG31562, isoform CRA_c.
- Heterogeneous nuclear ribonucleoproteins C1/C2-like
- CUGBP Elav-like family member 1
- Nucleolin
- Uncharacterized protein.
Sequence:
MSRNSPPAAEGNGSKRFKGDSWGTRDPSRLVHILRLPSCVTEGEILCLALPFGEVSNLLFLRAKNQAFVEMSTEESANTMINYYTWMPPVLRGQPVHIQFAHYRELKVSSSPSQEISLSQAGDSREATASSLVAVPGQAAASGQTAVPSQLGAQPCLPPEDSYQAGTVALAPPASAVDTELVVAWQSPVLRILVENYFYRVTLEVLHQIFSRFGTVLKIITCTKNNRFQALLQYAHVMSAERAKLFLDGQNIYDACCTLRISFSGLTNLMVKYNNDKSRDYMRPDLPSDDSQPSPVQVQNMASALPAPAMSSASPYASIALPHTFAIPQAAGLANPEVFKTLHPQAIQEVAMASSSSSSSTAAAAVGAAEIAAAAVPGAEGSMVTSGSPGVGSPVLLVANLNQEKVTPRSLFILFGAYGDVHRVKILFNRKENALVQMADGSQAELALRHLNGHKLYGKALCILLSKHQSVKLPREGKEDQGLTKDYANSPLHRFKKPGSKNFQNIFPPSATLHLSNLPSLVSEEELKNLFSSNGYAVKAFRFFPKNHKMALIRMGSTEEAIQALVDLHGHLLGQNHHMRVSFSRMTI
Protein: Protein PB1-F2 (P0C0U1)
Organism: Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Function: Plays an important role in promoting lung pathology in both primary viral infection and secondary bacterial infection. Promotes alteration of mitochondrial morphology, dissipation of mitochondrial membrane potential, and cell death. Alternatively, inhibits the production of interferon in the infected cell at the level of host mitochondrial antiviral signaling MAVS. Its level of expression differs greatly depending on which cell type is infected, in a manner that is independent of the levels of expression of other viral proteins. Monocytic cells are more affected than epithelial cells. Seems to disable virus-infected monocytes or other host innate immune cells. During early stage of infection, predisposes the mitochondria to permeability transition through interaction with host SLC25A6/ANT3 and VDAC1. These proteins participate in the formation of the permeability transition pore complex (PTPC) responsible of the release of mitochondrial products that triggers apoptosis.
Subcellular location: Host mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_04064, ECO:0000269|PubMed:12805420}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04064, ECO:0000269|PubMed:12805420}. Host cytoplasm, host cytosol {ECO:0000255|HAMAP-Rule:MF_04064, ECO:0000269|PubMed:12805420}. Note=Inner mitochondrial membrane in most cells types. Otherwise is detected in the nucleus and cytosol. {ECO:0000255|HAMAP-Rule:MF_04064}.
Interaction partners:
Sequence:
MGQEQDTPWILSTGHISTQKRQDGQQTPKLEHRNSTRLMGHCQKTMNQVVMPKQIVYWKQWLSLRNPILVFLKTRVLKRWRLFSKHE
Protein: Calcium-dependent secretion activator 1 (Calcium-dependent activator protein for secretion 1) (CAPS-1) (rCAPS) (Q62717)
Organism: Rattus norvegicus (Rat)
Function: Calcium-binding protein involved in exocytosis of vesicles filled with neurotransmitters and neuropeptides. Probably acts upstream of fusion in the biogenesis or maintenance of mature secretory vesicles. Regulates catecholamine loading of DCVs. May specifically mediate the Ca(2+)-dependent exocytosis of large dense-core vesicles (DCVs) and other dense-core vesicles by acting as a PtdIns(4,5)P2-binding protein that acts at prefusion step following ATP-dependent priming and participates in DCVs-membrane fusion. However, it may also participate in small clear synaptic vesicles (SVs) exocytosis and it is unclear whether its function is related to Ca(2+) triggering.
Subcellular location: Synapse {ECO:0000269|PubMed:10792045, ECO:0000269|PubMed:11927595, ECO:0000269|PubMed:14530279, ECO:0000269|PubMed:1516133, ECO:0000269|PubMed:9697858}. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle membrane {ECO:0000269|PubMed:10792045, ECO:0000269|PubMed:11927595, ECO:0000269|PubMed:9697858}; Peripheral membrane protein {ECO:0000305}. Note=Membrane-associated to vesicles. Strongly enriched in synaptic fractions. Preferentially binds to dense core vesicles but not to synaptic vesicles. Binds phosphoinosides, with a strong selectivity for PtdIns(4,5)P2 over PtdIns(3,4,5)P3. Probably localizes to different vesicles compared to CADPS2. {ECO:0000269|PubMed:10792045, ECO:0000269|PubMed:11927595, ECO:0000269|PubMed:14530279, ECO:0000269|PubMed:1516133, ECO:0000269|PubMed:9697858}.
Interaction partners:
- Syntaxin-1A
Sequence:
MLDPSSSEEESDEILEEESGKEVLGSAASGARLSPSRTNEGSAGSAGMGGSGAGAGVGAGGGGGSGASSGGGAGGLQPSSRAGGGRPSSPSPSVVSEKEKEELERLQKEEEERKKRLQLYVFVMRCIAYPFNAKQPTDMARRPRKISKQQLQTVKDRFQAFLNGETQIVADEAFMNAVQSYYEVFLKSDRVARMVQSGGCSANDSREVFKKHIEKRVRSLPEIDGLSKETVLSSWMAKFDAIYRGEEDPRKQQARMTASAASELILSKEQLYEMFQNILGIKKFEHQLLYNACQLDNPDEQAAQIRRELDGRLQMADQIARERKFPKFVSKEMENMYIEELKSSVNLLMANLESMPVSKGGEFKLQKLKRSHNASIIDMGEESENQLSKSDVLLSFSLEVVIMEVQGLKSLAPNRIVYCTMEVEGGEKLQTDQAEASKPTWGTQGDFSTTHALPAVKVKLFTESTGVLALEDKELGRVILHPTPNSPKQSEWHKMTVSKNCPDQDLKIKLAVRMDKPQNMKHSGYLWTIGKNVWKRWKKRFFVLVQVSQYTFAMCSYREKKAEPQELLQLDGYTVDYTDPQPGLEGGRAFFNAVKEGDTVIFASDDEQDRILWVQAMYRATGQSHKPVPPTQVQKLKPRAETCLSMDAPISQFYADRAQKHGMDEFISSNPCNFDHASLFEMVQRLTLDHRLNDSYSCLGWFSPGQVFVLDEYCARNGVRGCHRHLCYLRDLLERAENGAMIDPTLLHYSFAFCASHVHGNRPDGIGTVTVEEKERFEEIKERLRVLLENQITHFRYCFPFGRPEGALKATLSLLERVLMKDIVTPVPQEEVKTVIRKCLEQAALVNYSRLSEYAKIEENVGRLITPAKKLEDTIRLAELVIEVLQQNEEHHAEAFAWWSDLMVEHAETFLSLFAVDMDAALEVQPPDTWDSFPLFQLLNDFLRTDYNLCNGKFHKHLQDLFAPLVVRYVDLMESSIAQSIHRGFERESWEPVNNGSGTSEDLFWKLDALQTFIRDLHWPEEEFGKHLEQRLKLMASDMIESCVKRTRIAFEVKLQKTSRSTDFRVPQSICTMFNVMVDAKAQSTKLCSMEMGQEHQYHSKIDELIEETVKEMITLLVAKFVTILEGVLAKLSRYDEGTLFSSFLSFTVKAASKYVDVPKPGMDVADAYVTFVRHSQDVLRDKVNEEMYIERLFDQWYNSSMNVICTWLTDRMDLQLHIYQLKTLIRMVKKTYRDFRLQGVLDSTLNSKTYETIRNRLTVEERTASVSEGGGLQGISMKDSDEEDEEDD
Protein: Flotillin-2 (O61492)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play a role in axon growth and regeneration. May be involved in epidermal cell adhesion and epidermal structure and function.
Subcellular location: Membrane {ECO:0000250}. Note=In neuronal cells, associated with GPI-anchored cell-adhesion molecules. {ECO:0000250}.
Interaction partners:
- Flotillin-1
- Kekkon 5, isoform A
Sequence:
MGNIHTTGPNEALIVSGGCCGSTKKRTIVGGWAWAWWLVTDVQRLSLNVMTLNPMCENVETSQGVPLTVTGVAQCKIMKSSSYKQTDYHNDEADELLGTASEQFLGKSVKEIKQTILQTLEGHLRAILGTLTVEEVYKDRDQFAALVREVAAPDVGRMGIEILSFTIKDVYDDVQYLASLGKAQTAVVKRDADAGVAEANRDAGIREAECEKSAMDVKYSTDTKIEDNTRMYKLQKANFDQEINTAKAESQLAYELQAAKIRQRIRNEEIQIEVVERRKQIEIESQEVQRKDRELTGTVKLPAEAEAFRLQTLAQAKQCQTIEGARAEAERIRKIGSAEAHAIELVGKAEAERMRMKAHVYKQYGDAAIMNIVLESLPKIAAEVAAPLAKTDEIVLIGGNDNITNDVTRLVAQLPPSINALTGVDLSKVLSKIPGAKA
Protein: Allene oxide cyclase, chloroplastic (OsAOC) (EC 5.3.99.6) (Protein COLEOPTILE PHOTOMORPHOGENESIS 2) (Protein HEBIBA) (Q75KD7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the production of 12-oxo-phytodienoic acid (OPDA), a precursor of jasmonic acid (JA). Required for the production of JA in response to wounding. Necessary for flower and coleoptile development regulation by light, including blue (BL), red (RL) and far red (FR) lights. Involved in the auxin-mediated signaling pathway leading to growth stimulation. Essential for photodestruction of phyA upon activation by RL and FR. Implicated in responses to salt stress (NaCl).
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:Q9LS01}.
Interaction partners:
- Putative 12-oxophytodienoate reductase 11
- 12-oxophytodienoate reductase 7
- Putative 12-oxophytodienoate reductase 8
- Putative 12-oxophytodienoate reductase 12
- Allene oxide synthase 1, chloroplastic
- Putative 12-oxophytodienoate reductase 3
- Allene oxide synthase 2
- Putative 12-oxophytodienoate reductase 10
- 12-oxophytodienoate reductase 1
- Allene oxide synthase 3
Sequence:
MAAAAPSRVSVRAAAPGQTGGFAKIRPQVVVAAAARSAGVSGRRARSVRASLFSPKPATPKDARPAKVQEMFVYEINERDRESPAYLRLSAKQTENALGDLVPFTNKLYSGSLDKRLGISAGICILIQHVPERNGDRYEAIYSFYFGDYGHISVQGPYLTYEESYLAVTGGSGVFEGAYGQVKLNQIVFPFKIFYTFYLKGIPDLPRELLCTPVPPSPTVEPTPAAKATEPHACLNNFTN
Protein: Heat shock factor protein 1 (Heat shock transcription factor 1) (Hsf1 protein) (Q1LXV0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEYHSVGPGGVVVTGNNVPAFLTKLWTLVEDPDTDPLICWSPNGTSFHVFDQGRFSKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPEKDDTEFQHPYFIRGQEQLLENIKRKVTTVSNIKHEDYKFSTDDVSKMISDVQHMKGKQESMDSKISTLKHENEMLWREVATLRQKHSQQQKVVNKLIQFLITLARSNRVLGVKRKMPLMLNDSSSAHSMPKFSRQYSLESPAPSSTAFTGTGVFSSESPVKTGPIISDITELAQSSPVATDEWIEDRTSPLVHIKEEPSSPAHSPEVEEVCPVEVEVGAGSDLPVDTPLSPTTFINSILQESEPVSALTPPPSEQKCLSVACLDKTELHDHLESIDSGLENLQQILNAQSINFDSSPLFDIFSSAASDVDLDSLASIQDLLSPDPVKETESGVDTDSGKQLVQYTSQPIVLPDPLSTDSSSTDLPMLLELQDDSYFSSEPTEDPTIALLNFQPVPEDPKLS
Protein: Cytochrome P450 86B1 (EC 1.14.-.-) (Q9FMY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in very long chain fatty acids (VLCFA) omega-hydroxylation. Required for the synthesis of saturated VLCFA alpha, omega-bifunctional suberin monomers.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11522915, ECO:0000269|PubMed:19525321}; Single-pass membrane protein {ECO:0000269|PubMed:11522915, ECO:0000269|PubMed:19525321}. Note=In vitro import assays suggest an association with the outer chloroplastic membrane; also detected in the chloroplasts of guard cells when expressed in a heterologous system.
Interaction partners:
- Cytochrome P450 superfamily protein
- Omega-hydroxypalmitate O-feruloyl transferase
- Protein HOTHEAD
- Glycerol-3-phosphate acyltransferase 5
- Probable fatty acyl-CoA reductase 5
- Probable fatty acyl-CoA reductase 4
- At3g02940
- Transcription factor MYB41
- ABC transporter G family member 6
- Myb domain protein 9
Sequence:
MNFNSSYNLTFNDVFFSSSSSSDPLVSRRLFLLRDVQILELLIAIFVFVAIHALRQKKYQGLPVWPFLGMLPSLAFGLRGNIYEWLSDVLCLQNGTFQFRGPWFSSLNSTITCDPRNVEHLLKNRFSVFPKGSYFRDNLRDLLGDGIFNADDETWQRQRKTASIEFHSAKFRQLTTQSLFELVHKRLLPVLETSVKSSSPIDLQDVLLRLTFDNVCMIAFGVDPGCLGPDQPVIPFAKAFEDATEAAVVRFVMPTCVWKFMRYLDIGTEKKLKESIKGVDDFADEVIRTRKKELSLEGETTKRSDLLTVFMGLRDEKGESFSDKFLRDICVNFILAGRDTSSVALSWFFWLLEKNPEVEEKIMVEMCKILRQRDDHGNAEKSDYEPVFGPEEIKKMDYLQAALSEALRLYPSVPVDHKEVQEDDVFPDGTMLKKGDKVIYAIYAMGRMEAIWGKDCLEFRPERWLRDGRFMSESAYKFTAFNGGPRLCLGKDFAYYQMKSTAAAIVYRYKVKVVNGHKVEPKLALTMYMKHGLMVNLINRSVSEIDQYYAKSFDEGYIN
Protein: Uncharacterized protein YJR039W (P47107)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
Sequence:
MPAGRIRIAMTDNIIVSEVDGPPDVVKCFIREEDGLEGQSRELVVIGLEYIDVFEGVEQDEARKKLRLRTVGYTMAAFYFKDHTAPNRRFYILLKATGRLDFVNLDYKIVKSLETGIDQVRSEPKFMFQDPLRTALVFNLSCTEIYEISTEDIFCLEETDVKLSYVTSSPIVSIDACINFNDFLDKDVFTLSILTRAHNEVAYKLEACVCVFESKPAKGTKWQRTTNLTFVEEATVSQVLLKSVTNIGHFVFTPWKTYFIKHALSSKQTIDGKTVDKIYQGPGAFGSDNMERIELLQPILADTTLNHLTFTFMTSTAILITCRMNAILSSFEDDTYIWEKALFERLPINGGSSHDHYLAAFFNEKCWILVSPKGHLTVYSVRNEGHSNFVHLGSFLCKSTLYSDLIGNYTKSHLSCGSLHCGQGYLCLKFRSCGDIFASTCMKLLFKSKDSVPRQVYSTRKGIYWADVNNNVYRDSERIDFEINGSFIATKDGTLLKDNTIVTLVPIQRDNECNYAYVTKQGYLRWSFSKVYYRIQNTGVDLTIDNCFLSAISSKGSFLTVLVLNDEITVFDHCNRLKSQKVVFHRLSDLASIFLYEYESTVYIFMSDTEGNLCVMKLATFEIVEEVKICKKKLQFCEVPNSDYFFIYTADTIIFFKPSKIKGRFKIQEVYAPCPISCLIPGEKDGSVVMVTSQGQFYDVLVPGDAGRATLCSKFEKVLKTCLKFITLESSSRYVIVAALPVANPLQDKYSEIYVYDIKQFKNISAFNFSNLNNDIESIKYENAMISDIIAVPMLKRTETLGKRKTSELYKEVIFNSCILVSLNLDSIDGIDSKNMNNLLLFSFDEESGFIEFVFGINTGFSISGLHNYYNGCVLVYGEFVQAYQLNYSVHDNKFSIEQVSNRLNISGITITSSIFFDKRKAKMARKQQNIGTWVYLEEMILLDVRKGVMRFNVIHTTDGNIEKVQLQVQPLNLFERDLINSITDTGKMFTGAAAITFKNIRYLLISYGDQKLTLFSLKLDGEEEIDERVYHVAEQVTTINSVRTTDSRMSTFLGESTFMPLFLVSTLSNGCYVIGILHEESDISLHILSEKKAVFAKRSVQKFLGFLDPQMDDHTVISEI
Protein: Tubulin beta-7 chain (Beta-7-tubulin) (P29515)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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 alpha-6 chain
- Tubulin alpha-2 chain
- Tubulin alpha-5 chain
- Tubulin alpha-1 chain
- Gamma-tubulin complex component 4
- Mitotic spindle checkpoint protein MAD2
- Microtubule-associated protein RP/EB family member 1C
- Tubulin alpha-4 chain
- Tubulin beta-9 chain
- Tubulin alpha-3 chain
Sequence:
MREILHIQGGQCGNQIGSKFWEVVNLEHGIDQTGRYVGDSELQLERVNVYYNEASCGRYVPRAVLMDLEPGTMDSVRSGPYGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMMTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLSTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRNLTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMLNVQNKNSSYFVEWIPNNVKSTVCDIPPTGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEEGEYEEEEAEYEQEETY
Protein: Leucine twenty homeobox (E1BS07)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Oligodendrocyte transcription factor 2
- TAL bHLH transcription factor 2
- Sonic hedgehog protein
Sequence:
MKPEWRTLLNPIVGAVTAERARAGLTTIKPRIQEEGHREPCPARQWDLYSRTDRRRDGRTAPAMMFPSLIAPPAVYPSLLRPTPTLTLPQSLQSAFSSHSSFLVEDLIRISRPGAYPPRSAPPPSSMSPPASAPRTDSGTPELPGCTAARRICSSQSSGSDSTFLKFGVNAILSSTPRAESSPALLQSVPPKTFSFPYFEGSFQPFIRSSYFPAASAVVPIPGTFSWPLAARGKPRRGMLRRAVFSDVQRKALEKMFQKQKYISKPDRKKLAAKLGLKDSQVKIWFQNRRMKWRNSKERELLSSGGCREQTLPTKFNPHPDLSDVGKKCSGEEEEEDEGPMACPPSPRHPLPYHPAPQHLRDRLGPQTPPSPSHSSSPSKPSDCSDSEEEDEEGEEEEEITVS
Protein: Serine protease inhibitor Kazal-type 12 (Q9D256)
Organism: Mus musculus (Mouse)
Function: Inhibits trypsin.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Serine protease inhibitor Kazal-type 11
Sequence:
MKPAGAFLLLISLACLFLSVDAVSQGGFQAFCSNYEKTLAPDGKSCPKTHKPVCGTDGKTYQNRCAFCQTAMERSLGKLGFKHEGKC
Protein: RNA uridylyltransferase (EC 2.7.7.52) (Q57UM5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVSKYHRLLQQGLREEEGVTERHMVAGGEQRHGHVDDDNAEGDADFYDQKDERRAKMSNPKHESANVSAGGKQNRSVRDCLPGSLPPVANTSTDAAVRFDRERKNAGHGIDISCVEGDGAQMGTYVSTGRSDAKAGGGSSAIGVTADDESDGNLDTDGSDASEGDEVESTTDADVYGEDDTTEGPRGGVRLYSCDACPHAVFTTHAALLAHAEEHHADLLPDHARLRRIAQKLNPVWNRALNARRNTITSWGKKIFHVAAQRDAGESKMQEAHRARAQLECVVRRWHDKARVFIFGSSVAMGVWDGTADIDFAVVDVDAMERGSWPPLEKNAVRSITELLRRVGFSFVNLEPISHARVPIIKHHASSPILTVARRDAEDVVARSIRFILNGPATREDRLLLEGSVRDAVGPTGVQQVWWNRTSDMMSATLESTTAAVRAAMCSPALASASLRTKVQPAHDECRPELYNIDFDLSFRAFGIRNSTLLRKYLLSHPCARPGAIVLKDWSKTSGVNNSVNGYFTSYAINIMWIYYLVQKGYVPYVDPLEIPESLVNYTDFDPRYTPMIDPEITNTEREELYKAAGDMLVGFFYFYSFEFDWGHNVISLNRPGITTKRMLGWHVEDVVPVASTSVSSGGGGSNVKRHPTRYELCIEDPYEENLNLGRHIGVTKSLRVRTELYRGLLSLLKEGETRSCVFAAADSSGTPAAGGKQSAALPARALFKLMALTTQAISESRRLPQSNSDNSGRIGNGDNESLTEVGGGHRVEGAGVDPASCAGASLSSFGEPPIGVHEKTLESIFVEKAPMEFQLVRKVWNWHQLIHRLGYKIHRGHVMPRREVGVRCTARRDAEETTTELASDVDTTKSLRPGRGLTDTMLRDLSRGYMTLTPEWVAWSAPWVSQHLRGYSRLTTVRSAVADETPPALATVPSVVKPPTGEAVMGAMRTTRRNAAPARRVELLKLWLWRGISKVTPFKSPR
Protein: UBX domain-containing protein 2 (O14048)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway.
Interaction partners:
- Nuclear protein localization protein 4
- Ubiquitin fusion degradation protein 1
- UBX domain-containing protein 3
- Cell division cycle protein 48
- Uncharacterized protein C17C9.11c
- UBX domain-containing protein 10
- Probable proteasome subunit beta type-4
- ATPase family gene 2 protein
- DSC E3 ubiquitin ligase complex subunit 1
Sequence:
MDGDEASLVANFCAITNSTPEKAQEYLSVADGDLSTAITLFFESGGVTDVQSSYIEAPSQTEPVEEIRAPIAPTREVLVDPLADMSAGTSIMGNNFGFGGFPRMNRRQRRRMGIFDQSPSQIPFPSSNTEDSSEESDSSSRASRLAKLFRPPYDIISNLSLDEARIEASSQKRWILVNLQTSTSFECQVLNRDLWKDESVKEVIRAHFLFLQLLDDEEPGMEFKRFYPVRSTPHIAILDPRTGERVKEWSKSFTPADFVIALNDFLEGCTLDETSGRKNPLGAKSQKPVEAMSEDEQMHKAIAASLGNGNSTTESQGESSSQQAESHGVADDTVHKIDSAECDAEEPSPGPNVTRIQIRMPNGARFIRRFSLTDPVSKVYAYVKGVAEGADKQPFSLTFQRKSLWTSLDSTIKEAGIQNTALQFEFQ
Protein: CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5) (D4A5W8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU365024}.
Interaction partners:
- Phosphatidate cytidylyltransferase 1
- Cardiolipin synthase
- Phosphatidate cytidylyltransferase 2
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidate cytidylyltransferase, mitochondrial
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
Sequence:
MAAPAAGPVFWRRLLGLLPGRPGLAALLGRLSDRLGRSRERRRRRSPWLLLAPLLSPTVPQVTSPPCCLCPEGVHRFQWIRNLVPEFGVSSSHVRVLSSPAEFFELMKGQIKIAKRRVVMASLYLGTGPLEQELVDCLESSLEKSLQAKFPSDLKVSILLDFTRGSRGRKNSRTMLLPLLQRFPEHVRVSLFHTPNLRGLLRLLIPERFNETIGLQHIKVYLFDNNVILSGANLSDSYFTNRQDRYVFLQDCAEIADFFTELVDAVGDVSLQLQGDDTVEVVDGMVHPYKGDRAAYCRAANKRVMDVIHSARTRQQMLHAQTFHSDSLLSQEEAAAAGDRRPAPDTWIYPLIQMKPFEIQIDEIVTETLLTEAERGAKVFLTTGYFNLTQAYMDLVLGTRAEYQILLASPEVNGFFGAKGVAGAIPAAYVHIERQFYSEVCSLGQQDRVQLQEYWRRGWTFHAKGLWLYLAGSSLPCLTLIGSPNFGYRSVHRDLEAQIAIVTESRALQQQLHQEQEQLYLRSGVVSSATFEQPGRQVKLWVKMVTPLIKNFF
Protein: Type A von Willebrand factor domain-containing protein (Q54SU8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNCGSKYTFVQDDEEEEFVVDSNIFFQGAQPQQPQQPQQPQQPQQQQQQQQQQQQQQQQQQQQQQSRGFFSIFGRSAAPQAPPPAPMNNRAPNQLKAKIKKATTNVLVVNLGTVAKESSIQTGDGYFCKKCNCGFSNINALKEITLNDGKKHPNIPTDGGFDGNKTWKCEFCYEENEIVIDKEEIPQTNIIDYILESEPVGDNNNNNNNNKTKEEKEKDEKEKNEKDDSFVIFCIDISGSMEVTQSVNGLSIPSSLVSNSGIYDNEIPEKLAALTKVSYVSRLQCVQIGLLHQIESIAEKYPNKRVGIVTFSDKVTMFGDGSTEPVTISDKAKLLDLSQLVEEGGLLQMNNPVSKTKNSLLEKVKTLRGSGSTALGSAVAACVGITGGSRGSQIIICTDGQSNMGLGATEAPEKQQMVFEQIANMAQRSGTSISVLTIKGTDTKLEVIGKLANNTGGEVNIMDPINLNDGFKEILSLPTLATNVSVKIFLHKGLYVSDFDNNNNTEKSFVERVIGNVNQDTTISFEYGVRSSKLIDKSLKSIPFQLQIFYTTLTGKKCVRMITQTQEITTSSDLAEEHANIEALGINMVQTSTKIASSGDYEKSRAKNYSHAGLMQKVMMKKQKATKVDSDEIDSMSNYMQQAQDIETQLSNTVSNEKSYNSSGDRLKSRQQNRDDATANMLYNMSNMNSTKSKKKFI
Protein: Nus factor SuhB (Inositol-1-monophosphatase) (I-1-Pase) (IMPase) (Inositol-1-phosphatase) (EC 3.1.3.25) (P0ADG4)
Organism: Escherichia coli (strain K12)
Function: Part of the processive rRNA transcription and antitermination complex (rrnTAC). The complex forms an RNA-chaperone ring around the RNA exit tunnel of RNA polymerase (RNAP). It supports rapid transcription and antitermination of rRNA operons, cotranscriptional rRNA folding, and annealing of distal rRNA regions to allow correct ribosome biogenesis. This subunit may play a central role in organizing the structure. Involved in 30S ribosomal subunit biogenesis; thought to be required for loop formation between NusB/NusE (rpsJ, ribosomal protein S10) bound to boxA upstream of the rRNA operons and the elongating RNAP complex. This would promote correct co-transcriptional folding of rRNA. Plays a role in transcription antitermination in a plasmid context in vivo. Required for rrn transcription antitermination; required for integration of NusB/NusE into the antitermination complex. The Nus factor complex (NusA, NusB, NusE (rpsJ), NusG and SuhB) represses expression of suhB and possibly other genes via boxA; the Nus complex prevents or promotes Rho-mediated transcription termination depending on gene context. Involved in post-transcriptional control of gene expression (Probable). Enzymatic activity is not required for complementation of the cold-sensitive phenotype of the dnaB121 mutation (Probable).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:10747806}.
Interaction partners:
- Transcription termination/antitermination protein NusG
- Transcription antitermination protein NusB
- Small ribosomal subunit protein uS10
- Transcription termination/antitermination protein NusA
- DNA-directed RNA polymerase subunit omega
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit beta
- NAD kinase
- DNA-directed RNA polymerase subunit alpha
- Small ribosomal subunit protein uS4
Sequence:
MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGTDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKQYATTYINIVGKLFNECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMLTGNIVAGNPRVVKAMLANMRDELSDALKR
Protein: tryptophan--tRNA ligase (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (Q580R7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- tryptophan--tRNA ligase
- Tyrosyl/methionyl-tRNA synthetase, putative
Sequence:
MTEAVVTPWSVEGDVNYDKLIKDFGSHAIDEALLERIERVLGKKPHHFLRRGIFFSHRDLNLLLDVYESGQPFYLYTGRGPSSESMHMGHLIPFMFTKWLQDSFRVPLVIQMTDDEKFYFRNIPMEQVEAMTTENIKDIIAMGFDPELTFIFRDFDYMGCMYRTVAKIERAFTASQVRGCFGFAMEDNCGRWMFPAIQAAPSFSAAFPHIFPPSMGNVFCLIPQAIDQDPYFRLTRDIAPRLGYLKPAVIHSKFFPGLSGPKGKMSSSSGTAVLLTDTEKMVKDKINKHAFSGGGATKQEHFLLGANVEVDVPIQWLSFFLEDDEELARVKKEYMLGRIMTGEVKKLLINTITAITKTHQEKRKLVTDEDVQLFTSTRIMGPAKKAATQ