wanglab/gogpt-training-data huggingface dataset:
Protein: Contactin (Q9VN14)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for organization of septate junctions and paracellular barrier functions. Septate junctions, which are the equivalent of vertebrates tight junctions, are characterized by regular arrays of transverse structures that span the intermembrane space and form a physical barrier to diffusion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15459097}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:15459097}. Cell junction, septate junction {ECO:0000269|PubMed:15459097, ECO:0000269|PubMed:20935638}. Note=Nrx is required for its cell surface localization.
Interaction partners:
- Neuroglian
- Neurexin-4
- Amyloid-beta-like protein
- Sinuous
- Kune-kune
- Transferrin 2
- Neurexin 1, isoform F
- Lachesin
- LD32918p
- Tyrosine-protein phosphatase 99A
Sequence:
MLAKIGLLASILVLNLVGQITPQFSENLPDPDPQSGQQPQNYQPSYNKDYSPRYNPLYTGQQSADPNQFDNTLVDGQSPNTYKGYYDGRAGGGGLGGNVVGPGNNLGGLGPQYDPFNRNSIGSAGVSYRDAYTDEDNFCPEHWVSFRQTCYRFIRSPKRNWAEAKKICKAHNADLINVDNVEKHSFILKNLILQNQRQNRFFISARQTGPLNWVNDDNTQLVQIEDSFSMDEQVPLENEDLHDNRFLVQNDLNNQNINNPNQFYNSLPGTVNQRNQNNLRGFIGPNQPYGDNRYVRDRVVYAFSKKRDRWMFMPAYEIELNLFICESKVLYSSDNVNIKLDDKRPYHYGLDINDMERIPRGPYFVKQPNDTTFDVNKNRLINDVTLSCLANGYPTPSYTWYREVYVDDRLEYQKIDPLAQDRYTISGGNLIIYEPKQALDQGAYHCVAENKFGRIRSESAHLNFGFIMEFNLKRSAETSEMNWGKSIFCDPPQHYPDVRYYWARDYFPNFVEEDQRVFVSRDGALYFSFIETVDRANYSCTVQTLVSDTGRNGPFFPLRVTPNSNYQALIFANTFPKVFPEAPVAGDEIRLECMAFGYPIPSYNWTRQGLPLQRNAYTINYGRVLIIQNATTNDNGEYSCTITNPRKTLMKSIYINIQMRPQFTIPLKDMIKDYNSDVTFICEAFAIPDANYTWYKNAERLDPANINRDRYIIQDNVLTIKFLEKDKDDAMYQCGAQNQLKTSFSSAQLRVLSMKPSFKKHPLESEVYAVYNGNTTIVCDPEAAPRPKFQWKKDGQVIGSGGHRRILPSGTLTISPTSRDDEGIYTCIASNQAGTDESHARVIVLQEIRFIETPPQRIVSKEHDLIFLHCEAAFDELLDIAYVWKHNGEVLKNNHDGTGRIIVDWNRLTVHNTSMRDAGDYECVVKSAVNEISSKTSVSIEGAPGAPGGVQVIQISKTKAIIEWVDGSHNGRAIRYYNILGRTNWNRTWVNVSTHVQAREVDRYTSRQQAEVVNLTPWSAYEFSVTAVNDLGIGTPSAPSPIYSTYEDKPYIAPRNVGGGGGKIGDLTITWDPLLPQEQHSHGIHYKVFWKLKGAIEWASDEIKKQDHMGVAVVNIPLNNYYTEYEVKVQAINSVGKGPESEIAVIHSAEDMPQVAPQKPIALAYNSTCFNVTWQPIDMSRENIRGKLIGHRLKYWKTTHQEEDSVYYLSRTTRNWALIVGLQPDTYYFVKVMAYNAAGEGPESERFEERTYRKAPQKPPSSVHVYGINPSTVRVVWRYVSPSQDEEPVEGYKVRIWESDQNMITANNTIVPIGQKLESYINNLTPGKSYNMRVLAYSNGGDGRMSSPTLHFQMGKTTRNGANTRHGHNINTALILSTLLLISTFLYTSQ
Protein: Amphiphysin (Q6IT90)
Organism: Lampetra fluviatilis (European river lamprey) (Petromyzon fluviatilis)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
EVSSGIFAKNAKKRITRAQEKVLQKLGKADETKDTQFEQLVHNFSKQYGEGTRLHKEVKAYLAAVKAMHESSKKLIESLQEIYEPDWYGKELIQDIAERNNELWEDFHQKLVDLALLTLDIYLGQFPDIKTRIAKRGRKLVDYDSTRHHLEALTCTRKKDDSKISKAEEDFLKAQKVFEELNVDLQEELPILWNSRIGFYVNTFRSIASLEEKFHREIGLLNHELYEVMVKLGDQHADLAFSIRGAPSDSGPLKITETPCSPPEITVQAPTSLFTGDEQALGPNHMSAPLKSPSLGRKGPPVPPPPKLTPSKEVQQEAIFSLFDDNFVPDFSSAPAEAAKKDEGSLLDIDFDPLKPDTATTPMSPAINQTLLFDLAWEASPQQVQPPPQPVMPVEPVIPVEPAIPVEPAIPVEPAIPVEPAIPVEPVIPVQPVKPAQPDVSTTEETSQKPASLDETSETMEAAMGPLVKSPESESAVVPAEMDVVPAEMAPIPMETPIVEVTASTPTPVDSGPELDMAFVTNGDAEVEASKHVDTSSESTDMPPGFLYKVQAEHDYTPLDADELTLLRGDVVLVLSFENADEQDAGWLTGIKEADWMAYKDLMGRKGVFPENFTQRLE
Protein: Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A (Cam-PDE 1A) (EC 3.1.4.17) (61 kDa Cam-PDE) (Q61481)
Organism: Mus musculus (Mouse)
Function: Calcium/calmodulin-dependent cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cGMP and cAMP, which are key regulators of many important physiological processes. Has a higher efficiency with cGMP compared to cAMP.
Subcellular location: [Isoform 2]: Cell projection, cilium, flagellum {ECO:0000269|PubMed:15901640}. Note=Concentrates in the tail of mature sperm. {ECO:0000269|PubMed:15901640}.
Interaction partners:
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Calmodulin-4
- Calmodulin 5
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Adenine phosphoribosyltransferase
Sequence:
MGSTDTDIEELENATYKYLIGEQTEKMWQRLKGILRCLVKQLEKGDVNVVDLKKNIEYAASVLEAVYIDETRRLLDTEDELSDIQTDSVPSEVRDWLASTFTRKMGMMKKKPEEKPKFRSIVHAVQAGIFVERMYRKNYHMVGLTYPAAVIVTLKEVDKWSFDVFALNEASGEHSLKFMIYELFTRYDLINRFKIPVSCLIAFAEALEVGYSKHKNPYHNLVHAADVTQTVHYIMLHTGIMHWLTELEILAMVFAAAIHDYEHTGTTNNFHIQTRSDVAILYNDRSVLENHHVSAAYRLMQEEEMNILVNLSKDDWRDLRNLVIEMVLATDMSGHFQQIKNIRNSLQQPEGIDRAKTMSLILHAADISHPAKTWKLHYRWTMALMEEFFLQGDKEAELGLPFSPLCDRKSTMVAQSQIGFIDFIVEPTFSLLTDSTEKIVIPLIEEASKSQSSNYGASSSSTMIGFHVADSLRRSNTKGSVCDGSYAPDYSLSAVDLKSFKNNLVDIIQQNKERWKELAAQGELDLHKNSEELGNTEEKHADTRP
Protein: Transcription factor with C2H2 and Zn(2)-Cys(6) DNA binding domain (Eurofung) (C8VA09)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPDPHERFECHHPGCTSSYLRKEHLHRHQAQHTGRVTSPCPFCSRTFARRDTLRRHVRRDHANSQSQLDSARAIRACQVCRGAKLRCRGGFPCTRCRAKGVQCVFEHPAAKFGVEDEPEPGPGPNADADLDATASQSNPSRHQGNAQADPQNRQGQTDGESPSLGPGLVVAQSADRDKTQHWVDLYFTRFHPHWPILHRATFDVAHEPPFLVQTVVMVGLWSNWARTYPSRDEAGEGCELETGDGNPTSQWPIATYQGILIYLIFSLVLYGTDHASFELSLTFRMSPSDHSLLSSVVKTCLENNIFHYPRMLQRYVGVEDITCIWVGVEEIKRLGLALYRVCCMCAGETGREASVRPDGDHGRLLRLCDLDFPPPDEEYLWGAGSNEELSRLLRHRNGTPEQHQTDDGREGSLITGDQKSWISSHILCQCSSTIPVKGSRFAT
Protein: 2-methylisoborneol synthase (2-MIB synthase) (EC 4.2.3.118) (D3KYU2)
Organism: Streptomyces lasalocidi (Streptomyces lasaliensis)
Function: Catalyzes the cyclization of 2-methylgeranyl diphosphate (2-MeGPP) to 2-methylisoborneol (2-MIB), which likely involves the intermediacy of 2-methyllinalyl diphosphate.
Interaction partners:
Sequence:
MPDSGSLGPPTSLPEQPPAPPATAPDAPAATVTDRPVTSSVAHFLAGLHPPVTRPSSPPSPSMPPASSNPSSPPSSSMPPASWAPPSPLSPPAPSLPPTSPPATAPETSAATGSDSVVRRVPVGPTGLGTTALSLARRQAAVPPDAVPAPSGPSAEGPVVPGLYHHPIPEPDPVRVAEVSRRIKRWAEDEVRLYPEEWEGQFDGFSVGRYMVACHPDAPTVDHLMLATRLMVAENAVDDCYCEDHGGSPVGLGGRLLLAHTALDHLHTTAEYAPEWSESLGSDAPRRAYRSAMDHFVRAATPSQADRYRHDMARLHLGYLAEAAWAETGHVPEVCEYLAMRQFNNFRPCPTITDTVGGYELPADLHARPDMQRVIALAGNATTIVNDLYSYTKELDSPGRHLNLPVVIAEREHLSDRDAYLKAVEVHNELMHAFEAAAAELAADCPVPAVLRFLRGVAAWVDGNHDWHRTNTYRYSLPDFW
Protein: Spermatogenesis associated 22 (D3ZKY9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Meiosis-specific with OB domain-containing protein
- Carbohydrate kinase-like, isoform CRA_b.
- Synaptonemal complex central element protein 3
- Heat shock transcription factor 2 binding protein
Sequence:
MKRNLNESSTRSTAGCLPVPLFNQKKRNRQPLTSNPLQSDPGIGTVSDTYGFPSLPTDWAWEAVNPVVAPLKKTVNTGQIPASASYPLRIEDPVCKSIESNAKRSQGGGGYRGNNRNTSSRTWDRNDFRPQHKTVSPAANSEFSSGPVNLGAQRQKQFQTPEFPNLPGHKEAEVPRQTYLSKLPGSTMKGPDRASALQAFKPSFQQNPFNKTVLGDVPRENSLKETTLYQLKEKDNSLRIISAVIESMKYWQAQVKKTVLLFEVLAVLDSAVTPGPHYSKTFLMRDGKNILPCVFYEIDRELPRLIRGRVHRCVGHYDPHKNIFKCVSVRPASASEQKTFQAFVTIVDAEMKYHTKVMNEM
Protein: Iroquois-class homeodomain protein IRX-5 (Homeodomain protein IRXB2) (Iroquois homeobox protein 5) (Q9JKQ4)
Organism: Mus musculus (Mouse)
Function: Establishes the cardiac repolarization gradient by its repressive actions on the KCND2 potassium-channel gene. Required for retinal cone bipolar cell differentiation. May regulate contrast adaptation in the retina and control specific aspects of visual function in circuits of the mammalian retina. Involved in craniofacial and gonadal development (By similarity). Modulates the migration of progenitor cell populations in branchial arches and gonads by repressing CXCL12.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Iroquois-class homeodomain protein IRX-3
- Alpha-ketoglutarate-dependent dioxygenase FTO
Sequence:
MSYPQGYLYQPSASLALYSCPAYSTSVISGPRTDELGRSSSGSAFSPYAGSTAFTAPSPGYNSHLQYGADPAAAAAAAFSYVGSPYDHTPGMAGSLGYHPYAAPLGSYPYGDPAYRKNATRDATATLKAWLNEHRKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKMTWTPRNRSEDEEEEENIDLEKNDEDEPQKPEDKGDLEGPESGGAEQKATAGCERLQGPLSPAGKETEGSLSDSDFKESSSEGRHDELPRPPRAGESSPAGPATARLAEDAGPHYPASVPAPGPHPSAGELPPGSGGSSVIHSPPPPPPPPPAVLAKPKLWSLAEIATSSDKVKDGGGGSEGSPCPPCPGPMGGQTLGGSRASPAPAPARSPSAQCPFPGGTVLSRPLYYTAPFYPGYTNYGSFGHLHGHPGPGPSPTAGPGSHFNGLNQTVLNRADVLAKDPKMLRSQSQLDLCKDSPYELKKGMSDI
Protein: Solute carrier family 22 member 6 (Organic anion transporter 1) (rOAT1) (renal organic anion transporter 1) (rROAT1) (O35956)
Organism: Rattus norvegicus (Rat)
Function: Involved in the renal elimination of endogenous and exogenous organic anions. Functions as organic anion exchanger when the uptake of one molecule of organic anion is coupled with an efflux of one molecule of endogenous dicarboxylic acid (glutarate, ketoglutarate, etc). Mediates the transport of prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) and may be involved in their renal excretion (By similarity). May contribute to the transport of organic compounds in testes across the blood-testis-barrier (By similarity). Also mediates the sodium-independent uptake of 2,3-dimercapto-1-propanesulfonic acid (DMPS), 9-(2-phosphonylmethoxyethyl) guanine (PMEG), 9-(2-phosphonylmethoxyethyl) diaminopurine (PMEDAP), ochratoxin (OTA), acyclovir (ACV), 3'-azido-3-'deoxythymidine (AZT), cimetidine (CMD) and edaravone sulfate. Mediates the sodium-independent uptake of p-aminohippurate (PAH), cidofovir, adefovir, 2,4-dichloro-phenoxyacetate (2,4-D), hippurate (HA), indoleacetate (IA), indoxyl sulfate (IS) and 3-carboxy-4-methyl-5-propyl-2-furanpropionate (CMPF). PAH uptake is inhibited by p-chloromercuribenzenesulphonate (PCMBS), diethyl pyrocarbonate (DEPC), indomethacin, sulindac, diclofenac, carprofen, okadaic acid, benzothiazolylcysteine (BTC), S-chlorotrifluoroethylcysteine (CTFC), cysteine S-conjugates S-dichlorovinylcysteine (DCVC), furosemide, steviol, phorbol 12-myristate 13-acetate (PMA), calcium ionophore A23187, benzylpenicillin, bumetamide, losartan, phenol red, urate and alpha-ketoglutarate (By similarity). PAH uptake is inhibited by glutarate and probenecid.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8VC69}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8VC69}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q4U2R8}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:Q4U2R8}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ATP-binding cassette sub-family C member 2
- Solute carrier family 15 member 1
- Multidrug and toxin extrusion protein 1
- Sodium-dependent phosphate transport protein 1
- Na
- Broad substrate specificity ATP-binding cassette transporter ABCG2
- ATP-binding cassette subfamily C member 4
- Solute carrier family 17 member 3
- Solute carrier organic anion transporter family member 4C1
- Solute carrier organic anion transporter family member 1A3
Sequence:
MAFNDLLKQVGGVGRFQLIQVTMVVAPLLLMASHNTLQNFTAAIPPHHCRPPANANLSKDGGLEAWLPLDKQGQPESCLRFTSPQWGPPFYNGTEANGTRVTEPCIDGWVYDNSTFPSTIVTEWNLVCSHRAFRQLAQSLYMVGVLLGAMVFGYLADRLGRRKVLILNYLQTAVSGTCAAYAPNYTVYCVFRLLSGMSLASIAINCMTLNVEWMPIHTRAYVGTLIGYVYSLGQFLLAGIAYAVPHWRHLQLVVSVPFFIAFIYSWFFIESARWYSSSGRLDLTLRALQRVARINGKQEEGAKLSIEVLRTSLQKELTLSKGQASAMELLRCPTLRHLFLCLSMLWFATSFAYYGLVMDLQGFGVSMYLIQVIFGAVDLPAKFVCFLVINSMGRRPAQMASLLLAGICILVNGIIPKSHTIIRTSLAVLGKGCLASSFNCIFLYTGELYPTVIRQTGLGMGSTMARVGSIVSPLVSMTAEFYPSMPLFIFGAVPVVASAVTALLPETLGQPLPDTVQDLKSRSRGKQNQQQQEQQKQMMPLQASTQEKNGL
Protein: Enhancer of mRNA-decapping protein 2 (P40023)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: mRNA-binding protein which stimulates mRNA decapping by DCP1 and DCP2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- mRNA-decapping enzyme subunit 1
- Enhancer of mRNA-decapping protein 1
- m7GpppN-mRNA hydrolase
- Enhancer of mRNA-decapping protein 3
- ATP-dependent RNA helicase DHH1
- LSM1-LSM7 complex subunit LSM1
- Protein SCD6
- 5'-3' exoribonuclease 1
Sequence:
MGSETKHSAKVKIVTRESPPSAKEHMRPTKTQILVPPTQSLPNGKKPNFGKSTKQRREPRERTSKTGHEDDKATMVTVNIDAFLHDKAPKKKSCKYKKKKTRQYQDRAAASIDSKPHVAGHTAFAGASFTTDIPHEAALPKPSFV
Protein: Nucleoprotein (Nucleocapsid protein) (NP) (Protein N) (P09459)
Organism: Avian paramyxovirus 1 (NDV) (Avian orthoavulavirus 1)
Function: Encapsidates the genome, protecting it from nucleases. The nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA is termed the NC and serves as template for transcription and replication. During replication, encapsidation by N is coupled to RNA synthesis and all replicative products are resistant to nucleases (By similarity).
Subcellular location: Virion {ECO:0000305}. Host cytoplasm.
Interaction partners:
Sequence:
MSSVFDEYEQLLAAQTRPNGAHGGGEKGSTLKVDVPVFTLNSDDPEDRWNFAVFCLRIAVSEDANKPLRQGALISLLCSHSQVMRNHVALAGKQNEATLAVLEIDGFANGMPQFNNRSGVSEERAQRFAMIAGSLPRACSNGTPFVTAGAEDDAPEDITDTLERILSIQAQVWVTVAKAMTAYETADESETRRINKYMQQGRVQKKYILYPVCRSTIQLTIRQSLAVRIFLVSELKRGRNTAGGTSTYYNLVGDVDSYIRNTGLTAFFLTLKYGINTKTSALALSSLSGDIQKMKQLMRLYRMKGDNAPYMTLLGDSDQMSFAPAEYAQLYSFAMGMASVLDKGTGKYQFARDFMSTSFWRLGVEYAQAQGSSINEDMAAELKLTPAARRGLAAAAQRVSEETSSIDMPTQQVGVLTGLSEGGSQALQGGSNRSQGQPEAGDGETQFLDLMRAVANSMREAPNSAQGTPQSGPPPTPGPSQDNDTDWGY
Protein: Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic (CrBSD2) (A0A2K3DZC4)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Chloroplast chaperone required for RuBisCo biogenesis and translational regulation of the RuBisCo large subunit (RbcL). Stabilizes an end-state assembly intermediate of eight RbcL subunits until the small subunits (RBCSs) become available to produce a complete stable RuBisCo complex containing eight small and eight large subunits (By similarity).
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:25124725}. Note=Associates with chloroplastic polysomes. {ECO:0000269|PubMed:25124725}.
Interaction partners:
- Uncharacterized protein
- Galactokinase
- Aldose 1-epimerase
- UTP--glucose-1-phosphate uridylyltransferase
- NAD-dependent epimerase/dehydratase domain-containing protein
- UDP-sulfoquinovose synthase
- UDP-glucose 4-epimerase
- UDP-glucose 4-epimerase
- phosphoglucomutase
- Uncharacterized protein
Sequence:
MNSAALNARTASVAPQPQACHACKCRQLLSRRVPPAQRQVECSAIAPETLQDIIVGGAVVGAVSVALYAGLKKDPVPCSLCQGTGGIRCFACGGDGRNATVSRDDLYDSKALGGGVAPPKRDPLGRTINPRDCKVCRGAGLVLCSQCKGTGFQSAF
Protein: Rca1 (P91666)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSAYYRRAALRKKSPSRGSSFELEMNESGYTSFLALHNSTAETPFLLEDAEGENCRNASNTTTFFRGLNTPSGHQEQDLYWGKPYPRTQPQKKFSAEEEPFSMTPRLQDEHSLPKRRKKHFQSPHSSPKKSKKLLFPHIEEPPKNRFYGGVEKLDIVAKLAQWQPALQCILRHVGAHTLDVMTKVSPAWKQAVYRSQRDLERLQNHRLKLNLTKENPHVPKRCSHVPKANHTVPLQTSNHSSLANSVRLANGLGQLEHPPDGRGCRKGAARRDACCVKCPRCGRGSRVFISEAAKCGENLLSQTLPIGRTTSTFPCMTGPPLKRFLSLDLDEVRTSPQGPPYNFAECTSVICQFRFCVNCLCKSHPGERCLVTELDTPSKLMMPRERLTPPQRAQNRDPKITRKNSLKRLCF
Protein: Argininosuccinate lyase (ASAL) (EC 4.3.2.1) (Arginosuccinase) (Delta crystallin) (P33110)
Organism: Anser anser anser (Western greylag goose)
Function: Delta crystallin, the principal crystallin in embryonic lens, is found only in birds and reptiles. This protein also functions as an enzymatically active argininosuccinate lyase.
Interaction partners:
Sequence:
MASEGDKLMGGRFVGSTDPIMQMLSTSMSTEQRLSEVDIQASIAYAKALEKAGILTKTELEKILSGLEKISEEWSKGVFVVTQSDEDIHTANERRLKELIGDIAGKLNTGRSRNEQVVTDLKLFMKNSLSVISTHLLQLIKTLVERAAIEIDVILPGYTHLQKAQPIRWSQFLLSHAVALTRDSERLGEVKRRINVLPLGSGALAGNPLDIDREMLRSELDFASISLNSMDAISERDFVVEFLSVATLLMIHLSKMAEDLIIYSTSEFGFLTLSDAFSTGSSLMPQKKNPDSLELIRSKAGRVFGRLASILMVLKGLPSTYNKDLQEDKEAVFDVVDTLTAVLQVATGVISTLQISKENMEKALTPEMLSTDLALYLVRKGMPFRQAHTASGKAVHLAETKGITINNLTLEDLKSISPLFSSDVSQVFNFVNSVEQYTAMGGTAKSSVTTQIEHLRELMKKQKEQA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q580A8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Rapamycin-insensitive companion of TOR2
- Uncharacterized protein
- Serine/threonine-protein kinase TOR
- Serine/threonine-protein kinase TOR
- Protein artemis
- Ras-family member, GTP-binding protein, putative
- Small GTPase, putative
- Raptor N-terminal CASPase-like domain-containing protein
- Raptor N-terminal CASPase-like domain-containing protein
- Nuclear cap-binding protein subunit 2
Sequence:
MSNIESPRSSRPFGDSASALTRQFGLVFSNLQNAPDDRPRRVEECLSALLDILVAHALELSEHCLIDYIFQLLCDTFGVSISKGVKSLRVVFDVHLGDPHELRCRCFTLLVRKVCETTNEADCNTILQEMGEVLRENVRSTSDLLGKHFGRAITTMQSSSVTRAKAVGCQTVATMVDAGAVVIKRSPALLDLLNTPCSPPCLIHEIMESNDNWHRQALTRLLVNIAESHCIEVTASMAEQMASTMTSHLSSATEEKHITGLLTVIDAISASSTLQTVPWSLEAVASFVVQRDWRVYTEDVRVRAARATGKILPLLVKDEKLYDLVMKNLLSYISGGDEAVALSALTTFRSVIKSLNNIESHAVLTVDAVSDFIAKSPFNQLAFEILDYLRTQCGEQCVFGVYDLLERADVLNSVEKVAALLHFMGNRAPSNVDWLEECNIDLSPDSDVDVLVRSLSFLETLRYTEALESAVGLVFHKHTDVRRAAVGTVVSLCEVLLSPDKGGSCQGSHVDATITQLNSRVKIAVESLLDVAVTDRQMEIRYYTLKRLSPVFEPYLVQLDNIDALFMSRNDVCRGVRDQAMLLLYRLHSLQPDILHAQLLQLQEYMLREIDVKDGSISSTVYHAFLLQMAAENGTILLSPSTVETSVLRRLEKQPFVSKSLSVALLNLLRAVLDHSGPRNHCDAKQLIQPVLAIVNGSTSSTRRKAAIEALCSILATVPITEQSTHVSVYRALSRIIRGEAEESEAVIYSAMKCLSVIGAVDPTKARYIVKALQEGEIAEEEEVATPALALYKPRLRIHLHMDERYPCIVLYLLVKTLQHSADVEQQASVISVIHSMIHEVPGRQKAMLLTQFLPQLQAWLADPEKVHLYEVILLLMSDLATLLQRFKDVIPASTGLELLKSVRLFCLLPQASQKPLNAGVVELLDRVGRGLSPEEMRDHRWAVEFIHQRLLQDKRDLALVVRAVKSLDSFLAILHERDFQVLLPHVLGCIEPADAATPNVPGLKKKEVNTACFEFLNQIMAKQPLLMKDFCSQIIHTITWYIEESDCQDEMEMGLRTLAFLVGIVQRPARRFIKPIQRLVQQCGLPEDMFTNLLKSAADGLLKARAPLSGHDNLNPELPLTLVSDQPSLSKEDFQQVMKRVLRLGDHDFEVISVTHSEGNTVVYFRFVQGEDLLLNFRSFTSKAQESQSTLSRNLGILKLVQNAMSYCQVDDSLLENISRMPVANKKKREQSWMAWLHNTSVVMLKNSPIQPLRCTAQLAADNTGLSRDLFPFAAAAFIGKLNAQQQEVIIKAFTRALEVSPNDIKQAIFDFAEFIESERGKLNPEMILLVEKLTFVVERDNEERKFGINYDEVSGDVVVSHLEPGGPGALAGVPVGARLLALNGKRLVTTHEVVGAVKGLNRIELTLECPNGGKRGLSFDCLMDIDVLARVALNSKMYARAIFLNEILFAQLLSELSGQVSDRQNAAVRHALEVAERLIEFYNHLGLTMVAKGLVKKMSEKFSSNIIAPEQFGFDEVGALEQLNWWGEALSRYKSRMNVADGTLDTSAFLGALRCYDALGETITMQELIATNWELLDRDAQLEVAPLKAKAALWLGRWDEFDEVVGQPGVMERLDMVERCASLFRQKHYGELLDYVDEHRKSLFDSFFESFTESYNRSYDTLVELQHVRHFEELVSFVKSGSERRKMLRELWHKRVTLMSSRPAHIKTLITINSLVLSPQEDLPSQVVCVRALTKHHWTSLADHTLSTLLHPNGLNTRLANLDPDVIHVYMKHCYVTRGKQETYTLLSDILNNVQLTATSNRAEAWGCCWLLLGEWTVQLFPDCGTKAIETLRTATQLCPENCAAFHSLGILHYDLSRDPNTSQETQTKHHIESITALFKAVALSRRESNGVMEDVLRILSIWFSHSTVNEVNEAIQEGIKSVPCYVWLNVIPQLVARIGITGAKARSILTDLLVSIGSNFPHALLYPLTVTEKSPEVMRRQAAERVLKGIRVTNGPMVEEASLISNEMVRIAILWTEKWHNCIQLAAGKPENVSEIRNILRPLYEEMKKESTPNEQHFVKVHGSTLRRAWAALQKGESQEAWVLLKQVYCELHKAVGERRLQMDDLSPTLVKINKSNVPVPGTFVLGQQLITIQKFHSRVYVMPSKQRPRRFGVDGSDGSKYRFLLKGHEDLRQDERVMQFIELINTIFSSDSLSNAMGLIIPQYAVIPLTDNVGIIGWVENTETIYKMLERWRKDHNISIYKEVSMIVEKGKLVNITEYHHRNKQERKQLLSHVMASTPDDELRRIIWDKNDTCEHWLQYRGTYGHTLAIMSIVGYVLGLGDRHLNNLMLQDKGSVVHIDFGDCFEVAMHRSLYSEAVPFRLTRLLVPALGITGVDGVFRLTCELVMKILRRHSENLLSILEAFIYDPLINWRLTTVAEGENSASLLEAPVAGGEASPFAEPDGLIDGPPMQLSRSVLKVREQAPGTTLEQTGEEETRNTQGDLALARVRAKLTGEDFADGCHVVAGQPSRREVSEDPNDPFSWWSQGLAESSRDVYMTDGRALPSWSSFRTVNNQENLQNVASQVDRLIEEATSLDNLAEAYITGWAPFW
Protein: L-dopachrome tautomerase (DCT) (DT) (EC 5.3.3.12) (DOPAchrome conversion factor) (DOPAchrome isomerase) (DOPAchrome oxidoreductase) (L-dopachrome Delta-isomerase) (SLATY locus protein) (Tyrosinase-related protein 2) (TRP-2) (TRP2) (P29812)
Organism: Mus musculus (Mouse)
Function: Plays a role in melanin biosynthesis. Catalyzes the conversion of L-dopachrome into 5,6-dihydroxyindole-2-carboxylic acid (DHICA).
Subcellular location: Melanosome membrane {ECO:0000250|UniProtKB:P40126}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P40126}. Melanosome {ECO:0000269|PubMed:26620560}. Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000269|PubMed:26620560}.
Interaction partners:
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Tyrosinase
- Melan-A
- Melanocyte protein PMEL
- Microphthalmia-associated transcription factor
- Melanocyte-stimulating hormone receptor
- Membrane-associated transporter protein
- Transcription factor SOX-10
Sequence:
MGLVGWGLLLGCLGCGILLRARAQFPRVCMTLDGVLNKECCPPLGPEATNICGFLEGRGQCAEVQTDTRPWSGPYILRNQDDREQWPRKFFNRTCKCTGNFAGYNCGGCKFGWTGPDCNRKKPAILRRNIHSLTAQEREQFLGALDLAKKSIHPDYVITTQHWLGLLGPNGTQPQIANCSVYDFFVWLHYYSVRDTLLGPGRPYKAIDFSHQGPAFVTWHRYHLLWLERELQRLTGNESFALPYWNFATGKNECDVCTDELLGAARQDDPTLISRNSRFSTWEIVCDSLDDYNRRVTLCNGTYEGLLRRNKVGRNNEKLPTLKNVQDCLSLQKFDSPPFFQNSTFSFRNALEGFDKADGTLDSQVMNLHNLAHSFLNGTNALPHSAANDPVFVVLHSFTDAIFDEWLKRNNPSTDAWPQELAPIGHNRMYNMVPFFPPVTNEELFLTAEQLGYNYAVDLSEEEAPVWSTTLSVVIGILGAFVLLLGLLAFLQYRRLRKGYAPLMETGLSSKRYTEEA
Protein: Superoxide dismutase [Cu-Zn] 4 (EC 1.15.1.1) (Q54TU5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems (By similarity). Protects spores from cellular damage caused by UV LIGHT.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Catalase-B
Sequence:
MVKAICVVKGAVVNGTIIFSQENEGSPVYVNGTISGLSGGLHGFHIHEFGDTSNGCLSAGAHFNPFHVEHGGPNSAIRHVGDLGNITSCPSSKVANVLIQDNVISLFGDLSIIGRTLVVHENQDDLGLGGNLSKTTGNAGARVACGILAKI
Protein: Acetylxylan esterase A (EC 3.1.1.72) (Q75P26)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Acetylxylan esterase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Degrades acetylated xylans by cleaving acetyl side groups from the hetero-xylan backbone. Displays the greatest hydrolytic activity toward alpha-naphthylacetate (C2), lower activity toward alpha-naphthylpropionate (C3) and no detectable activity toward acyl-chain substrates containing four or more carbon atoms.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Probable endo-1,4-beta-xylanase B
- Probable endo-beta-1,4-glucanase B
Sequence:
MILLSYLLTYLLCALTCSARAIHNGRSLIPRAGSLEQVTDFGDNPSNVKMYIYVPTNLASNPGIIVAIHYCTGTAQAYYQGSPYAQLAETHGFIVIYPESPYEGTCWDVSSQATLTHNGGGNSNSIANMVTWTTKQYNADSSKVFVTGTSSGAMMTNVMAATYPNLFAAGVAYAGVPAGCFLSTADQPDAWNSTCAQGQSITTPEHWASIAEAMYPDYSGSRPKMQIYHGNVDTTLYPQNYEETCKQWAGVFGYNYDAPESTESNTPEANWSRTTWGPNLQGILAGGVGHNIQIHGDEDMKWFGFTN
Protein: BZIP domain-containing protein (A7SHQ5)
Organism: Nematostella vectensis (Starlet sea anemone)
Interaction partners:
- BZIP domain-containing protein
- BZIP domain-containing protein
- BZIP domain-containing protein
Sequence:
MISLWACHQERLNPTKVITRNCTITATCALVYKDISSLIIWESAIGAGMPVKENLRTVIQTRRCARGLGPIRLSTVTDRKRKEQLTPEEEEKRRLRRERNKQAANRCRKRKRDKIEMLERTAQEIDDSNKALETDIANMRTELTELMSVLRSHDCVMRSRDVVTQEDRASGLVEEPGPC
Protein: GH03113p (Wrapper) (Q9W260)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Neurexin-4
Sequence:
MTPHMCSVVRCLLAALILGQVQAELDFNNDLENSQKFKSIPTTVKTYENDTVQLPCTLNTPFRYVRWHRDDVALVDSRHPELPPPDRIMLWPNGSLQVANVQSSDTGDYYCEMNSDSGHVVQQHAIEVQLAPQVLIEPSDLTEQRIGAIFEVVCEAQGVPQPVITWRLNGNVIQPQSNTGNRQSLILEIKSRNQAGLIECVASNGVGEPAVANVYLHVLFSPEVSIPQPVVYTKLGSRAHLECIVEAAPAATVKWFHHGLPVALGAHSTTHESELQTNRSVDHYVNAVRHMLVVKSVRNADMGQYECRASNQISVKSGSVELTGRPMPCLFKINPGTQSSTSHVLVWQTESLLPIMEFKLKFRQIPSNNVTRQVRTNWTELTIPAQATNGLIYITTYTLHGLQPASLYEVSVLARNSFGWSDNSKIVRFATGGEVELPNYSTESELQDDFTEEDFHNEITQRSEVLSASMMFNSGSVNGRGGISAFIYSLCLINILRLIS