wanglab/gogpt-training-data huggingface dataset:
Protein: LD44138p (Lethal (3) 05822, isoform A) (Lethal (3) 05822, isoform B) (Lethal (3) 05822, isoform C) (Lethal (3) 05822, isoform D) (Q9VE96)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- CIN85 and CD2AP related, isoform J
- AT02196p
- CG14797-PA
- LD22662p
- 5'-AMP-activated protein kinase subunit beta-1
- LD33689p
- Endophilin-A
Sequence:
MTIPSRPAPAPPGSRGQSAAAGANASLEQLRLQLQQQHLQQQQGAGGGLQKLTIKLPPPPKGPLQSQHKRTTVSNNNNGSLFDEPTGGTSITRKFPQARYTPATNWDDDPFGGGSNGNDRFKKMPPPRPPPPKVLVNGQNMTKSNSSMASAVTGGTGRLMSNIFHRKKSTSTASAAASKAAAENRVYGLSSGNAGATPSNNSSSSASSAAFSNVDWNAAWNTATTTTTTTSSSSHSSHYASQQTADAQLISFDSPPSSPTFTQKSNSDCVSVDSFSSDSNFSSPNNGSVSQPESGFEDDYHRSRPSTQSPLDPWEAVDSVGLGGVDSFGSAPVRQTYQVQSRGSDNPLCNGKSLLPPTQSLTMPTIIKPKISQKPKAPKPPPFIGGHLPPGYSIPSGYAGSETPPSPPMPKGPPPPPPPASSGGISLLDVINGKVDALALSNGCQGYMEEEVVPYAVALYDFDGIEPGDLSFREGEKIYLLDHPTPEWLRGRTRSGCEGIFPINYVDIKVPLGATGGAAAAPTASAAAPSPSPSQQQLPTALCLYHFPGEVEGDLALQENELVTVLYRINEDWLYGEVAGRQGQFPANFLDQVPANLPTL
Protein: Acetylserotonin O-methyltransferase (EC 2.1.1.4) (Hydroxyindole O-methyltransferase) (B3GSH5)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine).
Interaction partners:
- Serotonin N-acetyltransferase
- Cytochrome P450 1A2
- Cytochrome P450 1B1
- Indoleamine 2,3-dioxygenase 1
- Indoleamine 2,3-dioxygenase 2
- Cytochrome P450 1A1
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase family 3 member A2
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase X, mitochondrial
Sequence:
MAPGREGELDRDFRVLMSLAHGFMVSQVLFAALDLGIFDLAAQGPVAAEAVAQTGGWSPRGTQLLMDACTRLGLLRGAGDGSYTNSALSSTFLVSGSPQSQRCMLLYLAGTTYGCWAHLAAGVREGRNQYSRAVGISAEDPFSAIYRSEPERLLFMRGLQETWSLCGGRVLTAFDLSRFRVICDLGGGSGALAQEAARLYPGSSVCVFDLPDVIAAARTHFLSPGARPSVRFVAGDFFRSRLPRADLFILARVLHDWADGACVELLGRLHRACRPGGALLLVEAVLAKGGAGPLRSLLLSLNMMLQAEGWERQASDYRNLATRAGFPRLQLRRPGGPYHAMLARRGPRPGIITGVGSNTTGTGSFVTGIRRDVPGARSDAAGTGSGTGNTGSGIMLQGETLESEVSAPQAGSDVGGAGNEPRSGTLKQGDWK
Protein: Protein henna (EC 1.14.16.1) (EC 1.14.16.4) (Phe-4-monooxygenase) (Phenylalanine-4-hydroxylase) (PAH) (Tryptophan 5-hydroxylase) (TRH) (Tryptophan 5-monooxygenase) (P17276)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Pterin-4-alpha-carbinolamine dehydratase
- RE21057p
- Aromatic-L-amino-acid decarboxylase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase
- Dihydropteridine reductase
- Sepiapterin reductase
- Tyrosine aminotransferase
- Tyrosine 3-monooxygenase
- AT18092p
Sequence:
MYQRQVSFDKPTRVEDSAYIVEGVDIKEARNTCLLFSPKDSSLSSGALANILAIFKKHDINLVHIESRSSLRVPGYEFFVEADGKSGALGKAIEDVKEQCSYFNIISRDYKDNATAVPWFPRRIRDLDRFANQILSYGSELDADHPGFTDPEYRKRRKYFADIAYNYKHGEPLPHVDYTKEEIETWGIIFRNLTKLYKTHACREYNHVFPLLVDNCGFREDNIPQLEDVSNFLRDCTGFTLRPVAGLLSSRDFLAGLAFRVFHSTQYIRHPSKPMYTPEPDVCHELMGHVPLFADPAFAQFSQEIGLASLGAPDDYIEKLSTIFWFTVEYGVCRQEGELKAYGAGLLSSYGELEYCLTDKPQLKDFEPEVTGVTKYPITQFQPLYYVADSFETAKEKTIKFANSIPRPFGVRYNAYTQSVEVLDSKPQISNLMDNINSEFQILQNAVAKLRV
Protein: U4/U6.U5 small nuclear ribonucleoprotein component snu23 (Q09776)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- U4/U6.U5 tri-snRNP-associated protein snu66
- Uncharacterized protein C1782.03
- Pre-mRNA-splicing factor brr2
- Pre-mRNA-splicing factor 38
- Pre-mRNA-splicing factor dre4
- Uncharacterized WD repeat-containing protein C227.12
- U4/U5/U6 small nuclear ribonucleoprotein prp3
- LSM complex subunit lsm3
- LSM complex subunit lsm7
- Pre-mRNA-processing factor 31
Sequence:
MDRYNPPRRNGNSKKNEVVITGGRTQRIDFEKDVNKTTILPAGASVGRRGRGAGWYCEACNETYKDSLSWLDHLNSTQHLRKTRTVIIEKRATLEEVKERMEYWRRQLLEPEKGSEEYSLKERVERYHQELEAKKLRRKQKKVNKEKNSPRLVGENTELAAIMGISSFGSTNL
Protein: valine--tRNA ligase (EC 6.1.1.9) (Valyl-tRNA synthetase) (Q6FTE7)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- leucine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Phenylalanine--tRNA ligase beta subunit
- Alanine--tRNA ligase
- GMP synthase
- rRNA biogenesis protein RRP5
Sequence:
MSRRLLSLTHNCFRYQQKFHVSLLSPVNNSIWKSHFYNQKRYFRMSDLDNLPPVDPKTGEVIINPLKEDGTEKTPKEIEKEKKKAEKLLKFAAKQAKKKAASNAGGNSEKKEKKKAKKEVEPIPAFVDATVPGEKKILVSLDDPALKAYNPANVESSWYDWWVKSGAFDPEFTADGKVKPEGLFCIPAPPPNVTGALHIGHALTIAIQDSLIRYNRMKGKTVLFLPGFDHAGIATQSVVEKQLWAKEKKTRHDFGRTKFVEKVWEWKEEYHQRIKNQIKFLGASYDWNREAFTLDPQLSKSVVEAFVRLHDDGTIYRAARLVNWSVKLNTAISNLEVENKDVKGRTLLSVPNYDEKVEFGVLTSFAYPVADSDEKLVIATTRPETIFGDTAIAVHPDDARYKHLHGKFVQHPFLPRKLPIICDSEAVDMEFGTGAVKITPAHDQNDYNTGKRHNLEFINILTDDGLLNENCGPEWQGMKRFDARKKVIEDMKKLNLYIGQEDNEMTIPTCSRSGDIIEPLLKPQWWVAQGEMAKDAIKAVKNGEIKIAPKSSEAEYFHWLENIQDWCISRQLWWGHRCPVYFIDIEGQENDRNDGNYWVAGRDLAEAETKAKAKFPDAKFTLHQDEDVLDTWFSSGLWPFSTLGWPDKTKDMEDFYPFSMLETGWDILFFWVTRMILLGIKLTGSVPFNEVFCHSLVRDAQGRKMSKSLGNVVDPLDVITGIKLEDLHAKLLMGNLDPREVEKAKLGQKESYPNGIPQCGTDAMRFALCAYTTGGRDINLDILRVEGYRKFCNKIYQATKFALMRLGDDYVPPAKEGLSGNESLVEKWILHKLTKTSQTVNDALEKRDFLTSTSAIYEFWYLICDVYIENSKHLIQEGSDLEKKSARDTLYILLDNALKLIHPFMPFISEEMWQRIPKRSTETVNTIVRASYPVYQKVYDDEKSAASYELVLDITKEARSLLAEYNILKEGKVFVESDHTESFETAQSQKDSIVSLIKAINEVDVVRSASEIPEGCVLKAVNPQVNVHLLVKGHIDIDAEIAKVEKKIEKARKTKQGIEQIINGKDYDTKANEQAKEANKVRLENSIADIEGFETTIENLKRLKL
Protein: p44-7 outer membrane protein (Q2GIY9)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MMSMAIVMAGNDVRAHDDVSALETGGAGYFYVGLDYSPAFSKIRDFSIRESNGETKAVYPYLKDGKSVKLESHKFDWNTPDPRIGFKDNMLVAMEGSVGYGIGGARVELEIGYERFKTKGIRDSGSKEDEADTVYLLAKELAYDVVTGQTDNLAAALAKTSGKDIVQFAKAVEISNSTIGDKVCRTRYDTAKKDHYAKYAKTTDKGSASKNDTSLCGDIGHSTVTSGHSTTPQVLKNFISATLGNGSQNWPTSTGTGSSTNDNAEAVAKDLTKLTTEEKTIVAGLLAKTIEGGEVVEIRAVSSTSVMVNACYDLLSEGLGVVPYACVGLGGNFVGVVDGTRCTIRPSLTLYAHSK
Protein: Roundabout guidance receptor 1 L homeolog precursor (Roundabout-1) (Q8UVD7)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MVSELAHFFLLCGIMCLTQGSRLRQEDFPPKIVEHPSDLIVSKGEPATLNCKAEGRPTPTIEWYKGGDKVETDKDDPRSHRMLLPSGSLFFLRIVHGRKIRPDEGVYVCVARNYLGEAVSHNASLEVAILRDDFRQNPSDVMVAVGEPAVMECQPPRGHPEPTISWKKDGTPIDDDKDERITIRGGKLMITYTRKSDAGKYVCVGTNMVGERESEVAELTVLERPSFLRRPSNMAVTVDDSVEFKCEARGDPVPTVRWRKDDGDLPKSRYEIRDDHTLKIRKVTAGDMGSYTCVAENMVGKAEASAVLTVQEPPNFVVKPRDQVVALGRTVTFQCEATGNPQPAIFWQKEGSQNLLFSYQPPQSSSRFSVSQTGDLTITTVQKSDVGYYICQTLNVAGSITTKAFLEVTDVVADRPPPVIRQGPVNQTVAVDGTLLMNCIASGIPIPTIHWRKDGILIPTQDSRIKQQDSGALQIRYAKLSDTGRYTCTVSTPSGEANWSAFIEVQEFGVPVQPPRATDPNLIPSAPSKPEVTDVSKNTVTLSWQPNLNSGATPTSYLIEAFSHASGSSWQTVAENVKTDSFAVKGLKPNAIYLFLVRAVNAYGLSDPSQISDPVKTQDIPPTSQGVDHKQVQRELGDVVLHLHNPTILSSSSIEVHWTVDQQSQYIQGYKILFRPSSENRGESAWSIFEVRTPAKNSAVIPELRKGVNYEIKARPFFNEFQGADSEVRFAKTMEEAPSAPPQSVTVTKNDGNGTAIVVAWQPPPEDTQNGMVQEYKVWCLGNESRYHINKTVDGSTLSVVIPSLVPGIRYSVEVAASTGAGSGVKSEPHYIQLDSFGNPVPPGDQVSLAQQISDVVKQPAFIAGIGAACWIILMVFSIWLYRHRKKRNGLTSSYAGIRKVPSFTFTPTVAYQRGGEAVSSAGRPGLLNISEPAAQPWLADTWPNTGNNHNECPINCCTSGNGNSDSNLTTYSRPADCIANYNNQLDSKQTNLMVPDSAVYGDVDLSNKINEMKTFNSPNLKDGRFVNPAGQPTPYATTQLIQSNISNNINTSAGDVDEKHWKPPCQQKPDVTPMQYNIMEQNKINKDYRASDTIPSTIPYNQSHDQNAGGSYNSSDRGSSTSGSQGHKKSTRTPKVSKQAGMNWADLLPPPPAHPPPHGATEDYTLSADESYDRALPCPIPPTRMYLQQDELEEEDERGPTPPIRGAASSPAAVSYSHQSTATLTPSPQDELQPMLQDCPEEIGHPQHQLERRRHQISPPPPPRPISPPHTYGYISGPIVSDMDTDVPEEEGDDGEMEVTKIQSRRHLLRGLEQTPASSVGDLESSVTGSMINGWGSASEEDNVSSGRSSVSSSDGSFFTDADFAQAVAAAAEYAGLKVARHQMQEATGGRRPFHASHCPRPTSPVSTDSNMSTAVIQKSRPAKKQKHQQGHLRKDVYTDDLPPPPLPPPAIKSPTGPSKAQLEGRPGLSQKYLVAEQRLERPGERKGVSYRGREGPDSRQQHAEARTNSGERRESSEKQLDGKMRKGKALKWDGTPTITNQMQEDILPYCKPTFPTSNNPRDPSSSSSMSSRGSGGRRRGEQTTGRRNAAEMQLLGNYEQGVDEDEIEETES
Protein: Ctf1p (A0A1D8PGH7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MTDQTKIKSEKDHQNIISEKVDSDVKVSTDTPTKINNNNNNNDDKSNPSESTTTGKSSSTTTNKKDKPKAFTIKYKRPRGSRACTVCRSRKVRCDAEIHIPCTNCITFGCDCILPEVKKRGNQSGESKAKKQKTAANSKTPTTTTTTTTTANGNTSNGNSTGKTATAATATKSNTKEKNYTNKKSSTSTNTRDNGTLPVSENSSNISSTTTTTTTTGTATNNNNNNNNNTSAPITTAASALSSLSKSAINTSNTSTTSTSANEPILNISQISVPPSLTSTYKNRPSMHKKELLDSKAKTSLTFLGSSSIGVVPQRAGENHVELTTDIFDTMDVTLDSVELEILKIRGAFLLPNKELSLDLINAYFEHVHPLMPVINRSLFMKKFHDPNDNPSLMVLHAVLLLGCRVSKNPLLLDSRGTNDLASITFFRRAKTLYETNYESDPISIIQTLILIGSYWDGPEDVTKNSFYWTRVAVGLAQGFGFQRDVSKSQNLTVSEKKIWRRIWWCLFEKDRNVSIAFGRPVVIDLNDCDVPMLTIDDFDETDPELGINDPYTVDETQALYFIHLVKLAEITGIIIKHQYSVKSESMKRRNAFSIIEHCDMLMGIWFTNLPPQLSFSLADNSTQNFYACLLNAQYYNRLYLIHRSNLVRMARSSSTNPNNYKYPSWGISFQSARMISIISKILLDRDLLQYVPVMFIYIAFSALIMLIYHVDSTNAVIASTATDSLYVSRAVLKELQKSWPIAGVLLKLFDKYANDKLKRSKLIESSSKVADYKEIMAQEKMRNSSTSPLASDSYGRVKSTPEVTTYQEPPQQPQQRPSRASQQQQQQVPSQLPLPQTKQSQSQSQPQPQPPQQGYGPDNYRKNIFSPGSNSTTSGISPGGNVYQDYQTSPANISHTLRQLQEQQQQQQQQQQQQQQQQQSQQQSHYQQQDFGYNGSQQSYNNNNNNNSNINTQQQHNNSSKPPQIEELVKQYKLPMKRAAQGETSDASDKPTTDTSPTSSIKSFPEISMVTDNLTNKQDFIDNFEPTQLFPNFSIPPTRAQSPTPNYEDHNDNGIGSNIYGSMNQEMTMRDSVAPSQQEQHQQFHNDVIGNGQHQHINGDNNNRDPHTPGFQTNFIDSAFNYLNLQSGIDMNEDIHSLFHMMN
Protein: Thyroxine-binding globulin (Serpin A7) (T4-binding globulin) (P35577)
Organism: Rattus norvegicus (Rat)
Function: Major thyroid hormone transport protein in serum.
Subcellular location: Secreted.
Interaction partners:
- Transthyretin
- Albumin
- Thyroglobulin
Sequence:
MSMFFYLFLLVLGLQATIHCAPHNSSEGKVTTCHLPQQNATLYKMPSINADFAFRLYRKLSVENPDLNIFFSPVSISAALAMLSFGSGSSTQTQILEVLGFNLTDTPVKELQQGFQHLICSLNFPNNELELQMGNAVFIGQQLKPLAKFLDDVKTLYETEVFSTDFSNVSAAQHEINSYVEKQTKGKIVGLIQDLKLNIIMILVNYIHFKAQWANPFRVSKTEESSNFSVDKSTTVQVPMMHQLEQYYHYVDVELNCTVLQMDYSANALALFVLPKEGHMEWVEAAMSSKTLKKWNHLLQKGWVELFVPKFSISATYDLGSTLQKMGMRDAFAESADFPGITKDNGLKLSYAFHKAVLHIGEEGTKEGASPEAGSLDQPEVAPLHAVIRLDRTFLLMILEKRTRSVLFLGKVVDPTKE
Protein: Zinc transporter ttm-1 (Toxin-regulated target of MAPK 1) (Toxin-regulated target of p38MAPK) (O45923)
Organism: Caenorhabditis elegans
Function: Promotes excretion of zinc from intestinal cells into the intestinal lumen in response to increased dietary zinc. Involved in cadmium resistance, possibly by promoting its transport from cells. Involved in resistance to B.thuringiensis pore-forming toxin Cry5B downstream of the sek-1 and pmk-1 MAPK kinase pathway.
Subcellular location: [Isoform a]: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23717214}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform b]: Apical cell membrane {ECO:0000269|PubMed:23717214}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23717214}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein ttm-2
- Zinc transporter ZIP3
- SUppressor of activated let-60 Ras
- Metallothionein-2
- Histidine ammonia-lyase
- Zinc transporter ZIP8
- CaDmium Responsive
- Protein MAK10 homolog
- Putative cytochrome P450 CYP13A4
- Similar to Transporter Of divalent Cations
Sequence:
MTISMISPSSIRLSSDKRDSSSSNLPANIEEDTQSVSSSDSGVSADSIDHHHHGHGHGHSHGGHGHSHTHNNDDSSSDCSGAGGGAHKHSHDEKYQKGRRAEKVLWAVAALSAVFIAAEFVGGFWAQSLAIMTDAGHMLSDLLSFIISIFAIRCARLPASKRLSFGYERAEVLGALTSVIILWVLTTVLVVVAIQRIVNNEHEVDADVMLITAGVGVLFNIVMGLVLHFGTGGHGHTHGGHSSHGHAHDGKNVNVRAALIHVIGDLVQSIGVLIAALIIRFTGWTLADPICTFLFSIIVLFTTVTVMRDIFFVLMEATPSHYDLSDVKKALSALEGVKGVHDLHLWSIGMDKTAFSVHLALESPNRAMENVAEARSLIRRRFGVAVATVQVEPFDEKIDSCDTCQQQETA
Protein: Retinal guanylyl cyclase 1 (RETGC-1) (EC 4.6.1.2) (CG-E) (Guanylate cyclase 2D, retinal) (Rod outer segment membrane guanylate cyclase) (ROS-GC) (Q02846)
Organism: Homo sapiens (Human)
Function: Catalyzes the synthesis of cyclic GMP (cGMP) in rods and cones of photoreceptors. Plays an essential role in phototransduction, by mediating cGMP replenishment. May also participate in the trafficking of membrane-asociated proteins to the photoreceptor outer segment membrane (By similarity).
Subcellular location: Photoreceptor outer segment membrane {ECO:0000269|PubMed:7912093}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:30319355}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Guanylyl cyclase-activating protein 1
- Guanylyl cyclase-activating protein 2
- Guanylyl cyclase-activating protein 3
- Aryl-hydrocarbon-interacting protein-like 1
- Neurocalcin-delta
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- Protein RD3
- Retinal guanylyl cyclase 2
- Peripherin-2
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
Sequence:
MTACARRAGGLPDPGLCGPAWWAPSLPRLPRALPRLPLLLLLLLLQPPALSAVFTVGVLGPWACDPIFSRARPDLAARLAAARLNRDPGLAGGPRFEVALLPEPCRTPGSLGAVSSALARVSGLVGPVNPAACRPAELLAEEAGIALVPWGCPWTQAEGTTAPAVTPAADALYALLRAFGWARVALVTAPQDLWVEAGRSLSTALRARGLPVASVTSMEPLDLSGAREALRKVRDGPRVTAVIMVMHSVLLGGEEQRYLLEAAEELGLTDGSLVFLPFDTIHYALSPGPEALAALANSSQLRRAHDAVLTLTRHCPSEGSVLDSLRRAQERRELPSDLNLQQVSPLFGTIYDAVFLLARGVAEARAAAGGRWVSGAAVARHIRDAQVPGFCGDLGGDEEPPFVLLDTDAAGDRLFATYMLDPARGSFLSAGTRMHFPRGGSAPGPDPSCWFDPNNICGGGLEPGLVFLGFLLVVGMGLAGAFLAHYVRHRLLHMQMVSGPNKIILTVDDITFLHPHGGTSRKVAQGSRSSLGARSMSDIRSGPSQHLDSPNIGVYEGDRVWLKKFPGDQHIAIRPATKTAFSKLQELRHENVALYLGLFLARGAEGPAALWEGNLAVVSEHCTRGSLQDLLAQREIKLDWMFKSSLLLDLIKGIRYLHHRGVAHGRLKSRNCIVDGRFVLKITDHGHGRLLEAQKVLPEPPRAEDQLWTAPELLRDPALERRGTLAGDVFSLAIIMQEVVCRSAPYAMLELTPEEVVQRVRSPPPLCRPLVSMDQAPVECILLMKQCWAEQPELRPSMDHTFDLFKNINKGRKTNIIDSMLRMLEQYSSNLEDLIRERTEELELEKQKTDRLLTQMLPPSVAEALKTGTPVEPEYFEQVTLYFSDIVGFTTISAMSEPIEVVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPQRNGQRHAAEIANMSLDILSAVGTFRMRHMPEVPVRIRIGLHSGPCVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVNLSTVGILRALDSGYQVELRGRTELKGKGAEDTFWLVGRRGFNKPIPKPPDLQPGSSNHGISLQEIPPERRRKLEKARPGQFS
Protein: Distal membrane-arm assembly complex protein 2 (ATP synthase subunit s-like protein) (Q9D7K5)
Organism: Mus musculus (Mouse)
Function: Required for the assembly of the mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). Involved in the assembly of the distal region of complex I.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18614015}.
Interaction partners:
- FAD-dependent oxidoreductase domain-containing protein 1
- Distal membrane-arm assembly complex protein 1
- NADH dehydrogenase 1 beta subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 beta subcomplex subunit 1
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- Transmembrane protein 70
- NADH dehydrogenase 1 alpha subcomplex subunit 3
Sequence:
MAAPRAVLHLGAREWNGRARRIHGMSELVTPDSSREKKRTLLQFLSDHFQDIQTLREYLLQKQISKVNRENRSFTNIQEKYGPYVAGAVFILKQGGAVKFQDKEEWIRPNNRSHFLAEIQKFQNVPVEAVDASGCAINYQGLSNLLPLKELRSLSLQRCPNLDDWCLSRLYLLAGSLQELSLAGCPRISERGLACLHHLQNLRRLDISDLPAVSHPGLTQILVEEMLPHCEVLGADWAQNLKLEPDKQPPDTSTPLSS
Protein: Phospholipid transfer protein (Lipid transfer protein II) (P55065)
Organism: Mus musculus (Mouse)
Function: Mediates the transfer of phospholipids and free cholesterol from triglyceride-rich lipoproteins (low density lipoproteins or LDL and very low density lipoproteins or VLDL) into high-density lipoproteins (HDL) as well as the exchange of phospholipids between triglyceride-rich lipoproteins themselves. Facilitates the transfer of a spectrum of different lipid molecules, including sphingomyelin, phosphatidylcholine, phosphatidylinositol, phosphatidylglycerol, and phosphatidyl ethanolamine. Plays an important role in HDL remodeling which involves modulating the size and composition of HDL (By similarity). Also plays a key role in the uptake of cholesterol from peripheral cells and tissues that is subsequently transported to the liver for degradation and excretion (By similarity). Two distinct forms of PLTP exist in plasma: an active form that can transfer phosphatidylcholine from phospholipid vesicles to HDL, and an inactive form that lacks this capability (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P55058}. Nucleus {ECO:0000250|UniProtKB:P55058}. Note=Nuclear export is XPO1/CRM1-dependent. {ECO:0000250|UniProtKB:P55058}.
Interaction partners:
- Apolipoprotein A-II
- Apolipoprotein B-100
- Apolipoprotein E
- Apolipoprotein A-I
- Phosphatidylcholine-sterol acyltransferase
- Serum paraoxonase/arylesterase 1
- Hepatic triacylglycerol lipase
- Apolipoprotein A-IV
- Apolipoprotein C-III
- Apolipoprotein M
Sequence:
MVLLWALFLALLAGAHAELPGCKIRVTSAALDLVKQEGLRFLEQELETITIPDVYGAKGHFYYNISDVRVTQLHLISSELHFQPDQDLLLNISNASLGLHFRRQLLYWFLYDGGYINASAEGVSIRTGLQLSQDSSGRIKVSNVSCEASVSKMNMAFGGTFRRMYNFFSTFITSGMRFLLNQQICPVLYHAGTVLLNSLLDTVPVRSSVDDLVGIDYSLLKDPVVSNGNLDMEFRGAFFPLKEDNWSLPNRAVEPQLEDDERMVYVAFSEFFFDSAMESYFQAGALQLTLVGDKVPSDLDMLLRATYFGSIVLLSPTVINSPLKLKLEATSPPRCTIKPSGTTISITASVTITLAPPMLPEVELSKMIMEGRLSAKLTLRGKALRVKLDLRRFQIYSNQSALESLALIPLQAPLKTLLQIGVMPLLNERTWRGVQIPLPEGINFVREVVTNHAGFVTVGADLHFAKGLREVIDKNRPADVAASHVPPPSAAAA
Protein: Pre-mRNA-splicing factor CWC15 (Complexed with CEF1 protein 15) (Q03772)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Pre-mRNA-splicing factor SNT309
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor PRP46
- Pre-mRNA-processing protein 45
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-splicing factor SNU114
- Pre-mRNA-splicing factor CWC2
- Pre-mRNA-splicing factor CEF1
- Pre-mRNA-splicing factor ATP-dependent RNA helicase PRP22
- Pre-mRNA-splicing factor BUD31
Sequence:
MTTSHRPQLEARSGAKAAAYTPTGIEHARLLPGHTTLKYRKFKEEENLRANCAQEDRSNDKSLEEAVMNEEKQDVVGSGNLQETRSEKDQKDSLQELLVTQKNKVEDKAELEGNEQLKGGNSSRRSWRKGTAFGRHKVTKETNIKEHATKKSASGYINDMTKSEYHQEFLHKHVR
Protein: Leupaxin (O60711)
Organism: Homo sapiens (Human)
Function: Transcriptional coactivator for androgen receptor (AR) and serum response factor (SRF). Contributes to the regulation of cell adhesion, spreading and cell migration and acts as a negative regulator in integrin-mediated cell adhesion events. Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a critical role as an adapter protein in the formation of the adhesion zone in osteoclasts. Negatively regulates B-cell antigen receptor (BCR) signaling.
Subcellular location: Cytoplasm. Cell junction, focal adhesion. Nucleus. Cytoplasm, perinuclear region {ECO:0000250}. Cell projection, podosome. Cell membrane. Note=Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin.
Interaction partners:
- Protein-tyrosine kinase 2-beta
- Vinculin
- Tyrosine-protein phosphatase non-receptor type 12
- Proline-serine-threonine phosphatase-interacting protein 2
- Apolipoprotein B-100
- ARF GTPase-activating protein GIT1
- Rho guanine nucleotide exchange factor 6
Sequence:
MEELDALLEELERSTLQDSDEYSNPAPLPLDQHSRKETNLDETSEILSIQDNTSPLPAQLVYTTNIQELNVYSEAQEPKESPPPSKTSAAAQLDELMAHLTEMQAKVAVRADAGKKHLPDKQDHKASLDSMLGGLEQELQDLGIATVPKGHCASCQKPIAGKVIHALGQSWHPEHFVCTHCKEEIGSSPFFERSGLAYCPNDYHQLFSPRCAYCAAPILDKVLTAMNQTWHPEHFFCSHCGEVFGAEGFHEKDKKPYCRKDFLAMFSPKCGGCNRPVLENYLSAMDTVWHPECFVCGDCFTSFSTGSFFELDGRPFCELHYHHRRGTLCHGCGQPITGRCISAMGYKFHPEHFVCAFCLTQLSKGIFREQNDKTYCQPCFNKLFPL
Protein: Neutral protease 2 (EC 3.4.24.39) (Deuterolysin) (Q5B671)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU361126}.
Interaction partners:
- P/Homo B domain-containing protein
Sequence:
MVFVPFFYLLAGLTLASGKPILLPRLAQEASQDVAEHSFDVTLESLGNSTVKAEVTNTGTEGLRLIQRGGILDQFPTRKVNVKGGDSDPKFTGVRVEYILSHLTADGFVQLSPNQTVGSVFDVADLYELSPGQEYTAVAKGLLQYTTLANEKRFLTFSYKSNNISFTAPTDTTKRLEDRSTLVCSDEYNQVVQDAISRAAEMATAAAADARTGSALFQKYFKSTSEDDIEEVAGRLDAIAKEATTTGQLKYYCEPTAEDYCAGNVAAMTYPTLNRVVNCPGYYASTKVSNYCGYLDQAAITLHEYAHADALYSPGTEDIAYGYESVLSLDTEDSKNNADNFAYYASSVYLQCDANEEPGEIGSELDVDVGSSGSGSTQTPTATAEPTYPPGPTSTGTTGTGTGTGIGTDTGTGTGWTWPWGQGWGMNDDSGSGDSGSLTGTTSDTNTGSNTGYGTGYGTDFGTGPSGVYGGWDADKSSDSSAAAVTSAPTAAPVTTTDGQELWNLNDLVNWLVSMYAGDGQMQGQTQGQTQTKTASSNLDSGSGGYNAEAGQSATGTQATQAENDKDCDE
Protein: Peptidyl-prolyl cis-trans isomerase CYP63 (AtCYP63) (PPIase CYP63) (EC 5.2.1.8) (Cyclophilin-63) (Cyclophilin-like protein CypRS64) (Q9LY75)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. May be implicated in the folding, transport, and assembly of proteins. Probably involved in early steps of spliceosomal assembly.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:15166240}. Nucleus speckle {ECO:0000269|PubMed:15166240}. Note=Moves from nuclear bodies to nuclear speckles upon interaction with SR proteins.
Interaction partners:
- UPF0235 protein At5g63440
- At2g29210/F16P2.41
- Serine/arginine-rich splicing factor RS41
- non-specific serine/threonine protein kinase
- Serine/arginine-rich splicing factor RS40
- Cysteine proteinase RD21A
- Probable cysteine protease RD21C
- At1g09850
- Probable cysteine protease RD21B
- Eukaryotic translation initiation factor 4B2
Sequence:
MTKKKNPNVFLDVSIGGDPVQRIVIELFADVVPKTAENFRALCTGEAGVGKSTGKPLHFKGSSFHRVIKGFMAQGGDFSNGNGTGGESIYGGKFSDENFRLDHDGAGVLSMANCGPNTNGSQFFILFKRQPHLDGKHVVFGKVVEGMAVIKKMELVGTSDGKPTSPVKIIDCGETSQIRAHDAAEREKGKSKKSNKNFSPGDVSDREAKETRKKESNEKRIKRKRRYSSSDSYSSSSDSDSDSESEAYSSSSYESSSSSDGKHRKRKSTTRHKGRRGERKSKGRSGKKKARPDRKPSTNSSSDTESSSSSDDEKVGHKAIKSVKVDNADQHANLDDSVKSRSRSPIRRRNQNSRSKSPSRSPVRVLGNGNRSPSRSPVRDLGNGSRSPREKPTEETVGKSFRSPSPSGVPKRIRKGRGFTERYSFARKYHTPSPERSPPRHWPDRRNFQDRNRDRYPSNRSYSERSPRGRFRSPPRRRSPPRYNRRRRSTSRSPDGYRRRLRDGSRSQSPRHRSRSQSPRKRQPISQDLKSRLGPQRSPIRGGRTSPAESLSPSHSPSPPGKRGLVSYAD
Protein: glycine--tRNA ligase (EC 6.1.1.14) (Diadenosine tetraphosphate synthetase) (Q8ILP6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- tyrosine--tRNA ligase
- Tyrosine--tRNA ligase
- Alanine--tRNA ligase
- isoleucine--tRNA ligase
- leucine--tRNA ligase
- D-aminoacyl-tRNA deacylase
- glutamine--tRNA ligase
- threonine--tRNA ligase
- leucine--tRNA ligase
- Isoleucine--tRNA ligase, putative
Sequence:
MIIIVIFLLSMFFFENKTYCFISKINIKNLRHNKNNNNKYHLFASRELRKISSFVLDNRILFNKQKIRKRKFNFFNVYSNKMSDMDNIKEQKENDGCGSLEELIERYVCEISSLIERNECIKGIDDEDLKKEFMENEKLLQDKKMKLKDLYGKPSEELKLVENRTKLENLVKRKFFYTNSFEIYGGASGLFDYGPSGCLLKSELENLWRCHFIYYDEMLEISGSCVTPYQVLKTSGHVDRFTDLMIRDVVTNDCYRADKYLGDFLKAKIEELRKKNTKGDEHVDEKEKKQKRDDDINENKENNKNNENNKNDENNENNKNDENNKNNDNNNNNNNSCNYNCDMVGGLHNGNERLIQKIELILRKLDGMNEEEIKEIIKEYNIKSPLKNDLSEPFPFNLMFQTKIGPKDDNTEDKNKEKCKNVSNNKNLNSTNTNNNMNNVAFLRPETAQGIFVNFKKLLEYNGGKTPFAGAQLGLGFRNEISPRNGLLRVREFQMAEIEYFVNPKKKNHEKYYLFKYLMLPLYPRDNQLTDGVVIKNMTLEEAVEKNIIANEALAYFLARTYLFLLKCGINKDGIRFRQHLKTEMAHYANDCWDAEILTSFGFIEVVGHADRSAYDLQHHMKYTGANLYACEKYNEPIEVEYVKMIPNKAKIGHTFKSEQNKIYACLNEKSNEELLIIDEELSKNNKYILNISNNDSINNECKYELTRDMLSFQKYKKKVQEENFIPNVIEPSFGIGRLIFCILEHSFRIRRFTDDKEERQYLSLPYKLAPIKCSILSISNNKAFYPYIKQIQMLLNQYNISSKIDNSSVSIGKKYARTDEIGIPFAVTIDFQTLKDKTITLRERDSMLQIRISMSHLVDIINSMLHAKKNWNEYIAQYGLFTQQVLDS