wanglab/gogpt-training-data huggingface dataset:
Protein: Sll1380 protein (P74162)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Photosystem I reaction center subunit IV
- Ycf36 protein
- Ferredoxin
- Ycf49-like protein
Sequence:
MTTATHLLKLAATVLLGSLVTTAPLVRAQFTAPAPQNNTSTPIPKVELNFQPLETALASQQFSQANEITRRLLLAATNRTLQGWLTTDTIEQIPCQDLKTIDQLWLQHSNNRFGFTPQLEAFLATGNRPGRLMSPESYDQFGDRIGWRKENQWVIFKKNLDFTLNAPAGHLPSPRDEYQINGGRLEYTALMGRFQVCQSGQVPTAPVRFTPFGS
Protein: LD04782p (Q8T0G6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTRSVYLNSDLSLREAAKRALGPELNLTNFSVVPFSICHHTENIDTNQLDYIPSRPEEPTHKSSFGEDYMITFVWPIVIIVAMLVAASIIACCLHWCRQRSGKMELGDEEERKSFRAKGIPVIFQDEYEEKPEIGNKSPVILKDEKPPLLPPSYNTSNMNGDNDVDDYVPPPSVVVGGREVRGKSPATPSYRKPPPYVSP
Protein: Selenoprotein V (SelV) (P59797)
Organism: Homo sapiens (Human)
Function: May be involved in a redox-related process.
Interaction partners:
- Thioredoxin reductase-like selenoprotein T
- Selenoprotein K
- Selenoprotein H
- Protein adenylyltransferase SelO, mitochondrial
- Selenoprotein S
- Selenoprotein F
- Ethanolaminephosphotransferase 1
- Selenide, water dikinase 2
- Selenoprotein M
- Selenoprotein N
Sequence:
MNNQARTPAPSSARTSTSVRASTPTRTPTPLRTPTPVRTRTPIRTLTPVLTPSPAGTSPLVLTPAPAQIPTLVPTPALARIPRLVPPPAPAWIPTPVPTPVPVRNPTPVPTPARTLTPPVRVPAPAPAQLLAGIRAALPVLDSYLAPALPLDPPPEPAPELPLLPEEDPEPAPSLKLIPSVSSEAGPAPGPLPTRTPLAANSPGPTLDFTFRADPSAIGLADPPIPSPVPSPILGTIPSAISLQNCTETFPSSSENFALDKRVLIRVTYCGLUSYSLRYILLKKSLEQQFPNHLLFEEDRAAQATGEFEVFVNGRLVHSKKRGDGFVNESRLQKIVSVIDEEIKKR
Protein: Guanylate-binding protein 9 (Q8BTS3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MTQPQMAPICLVENHNEQLLVNQEAIEILEKISQPVVVVAIVGLYRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLDTEGLGDVEKSNPKNDSWIFALSVLLSSTFVYNSMSTINHQALEQLHYVTELTELIRSKSSRNPHGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDEYLENALKLIPGYNPRVQASNSARECIRCFFPNRKCFVFDRPTHDRELLQKLETISEDQLDLKFREGTKAFVSYVFTYAKIKTLREGIKVTGNRLGTLVTTYVDAINSGAVPCLDDAMTSVARRENSVAVQKAADHYSEQMAQRLRLPTDTLQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVEIISEKIAFFWLKNEEASNKYCQEELDRLSKDFMDNISTFSVPGGHRIYTDMRKKIERDYWQVPRKGVKACEVFQNFLQSQYIIESSILQADRALTAGEKAIAEERAQKEVAEKEQELLRQKQKEQQEYMEAQEKRNKENLEQLRRKLMQEREQDIKDHDMMLEKQLKDQKAFLEEGFTNKAEEINAEIERLEHNIKDKKENIGPILELIEKAFCAGVFSSLIMVALLTHNPSLLRK
Protein: RNA-binding protein, putative (Q580U7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Spliceosome-associated protein, putative
- Splicing factor 3B subunit 10
- Uncharacterized protein
- Splicing factor 3B subunit 1, putative
- RNA-binding protein, putative
- Small nuclear ribonucleoprotein E
- Sm protein B
- Sm protein G
- U2 small nuclear ribonucleoprotein B, putative
- SURP motif domain-containing protein
Sequence:
MTTFKREDLRRVFFSDLSDQCNEDIIHELCTQFGPVANIVWPTSSNLGGTQQMTFCFADFYNAEDAKYCFEALHRSRTKLFGKELRVSHASTDVHQKEIGSRSSNRHVVHELHEIGAKVVVRGVDLSVTEYELTSFFAQFGNFAVPPRMVRDFDGNFRGVVILSYDDFASSDRVIEEMHQKIYRDRPISVTYAELPDGSGRLHGTAEERANAALFREEARKHEERIAREQQEHERERTRKRQQNTSWAAGIDPYARVR
Protein: Pyrroline-5-carboxylate reductase 3 (P5C reductase 3) (P5CR 3) (EC 1.5.1.2) (Pyrroline-5-carboxylate reductase-like protein) (Q53H96)
Organism: Homo sapiens (Human)
Function: Enzyme that catalyzes the last step in proline biosynthesis. Proline is synthesized from either glutamate or ornithine; both are converted to pyrroline-5-carboxylate (P5C), and then to proline via pyrroline-5-carboxylate reductases (PYCRs). PYCRL is exclusively linked to the conversion of ornithine to proline.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23024808}.
Interaction partners:
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- Pyrroline-5-carboxylate reductase 2
- Proline dehydrogenase
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Proline dehydrogenase 1, mitochondrial
- Hydroxyproline dehydrogenase
- Delta-1-pyrroline-5-carboxylate synthase
- Prolyl 4-hydroxylase subunit alpha-2
- Prolyl 4-hydroxylase subunit alpha-1
- Cytosol aminopeptidase
Sequence:
MAAAEPSPRRVGFVGAGRMAGAIAQGLIRAGKVEAQHILASAPTDRNLCHFQALGCRTTHSNQEVLQSCLLVIFATKPHVLPAVLAEVAPVVTTEHILVSVAAGVSLSTLEELLPPNTRVLRVLPNLPCVVQEGAIVMARGRHVGSSETKLLQHLLEACGRCEEVPEAYVDIHTGLSGSGVAFVCAFSEALAEGAVKMGMPSSLAHRIAAQTLLGTAKMLLHEGQHPAQLRSDVCTPGGTTIYGLHALEQGGLRAATMSAVEAATCRAKELSRK
Protein: Mitochondrial glutamate carrier 2 (GC-2) (Glutamate/H(+) symporter 2) (Solute carrier family 25 member 18) (Q9DB41)
Organism: Mus musculus (Mouse)
Function: Responsible for the transport of glutamate from the cytosol into the mitochondrial matrix with the concomitant import of a proton (symport system).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:12865426}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MIACRMSSQDLSISAKLINGGIAGLVGVTCVFPIDLAKTRLQNQQGKDVYRGMTDCLMKTARAEGFLGMYRGAAVNLTLVTPEKAIKLAANDFLRQLLMQDGTQRNLKMEMLAGCGAGICQVVITCPMEMLKIQLQDAGRLAVCHQASASATPTSRPYSTGSTSTHRRPSATLIARELLRTQGLSGLYRGLGATLLRDIPFSIIYFPLFANLNQLGVSELTGKASFTHSFVAGCTAGSVAAVAVTPLDVLKTRIQTLKKGLGEDTYSGVTDCARKLWTQEGPAAFMKGAGCRALVIAPLFGIAQGVYFIGIGERILKCFE
Protein: Gentisate 1,2-dioxygenase (GDO) (EC 1.13.11.4) (Q7X284)
Organism: Streptomyces sp
Function: Involved in the degradation of salicylate via a pathway involving coenzyme A derivative. Catalyzes the oxygen-dependent ring fission of gentisate between the carboxyl and proximal hydroxyl groups at positions 1 and 2 of the aromatic ring to form maleylpyruvate. The substrate specificity is strong, since salicylate, catechol, protocatechuic acid, homogenetisate, 2,3-dihydroxybenzoate or 5-aminosalicylate cannot substitute for gentisate in the ring cleavage reaction.
Interaction partners:
Sequence:
MTDTTSEQTERKLLDELYADFEDAGLIPLWTQVDGLMPMSPQPAAVPHLWRWAELLPIAQRSGELVPVGRGGERRAMALSNPGFPGLPYATPTLWTAIQYLGPREVAPSHRHSQGAFRFVVEGEGVWTNVDGDAVAMRRGDLLLTPSWAFHEHQNVTDEPMAWLDGLDIPLVSKLDAGFFEFGPDELSTRETPERSRGERLWGHPGLRPIGRPDQPNSPLNAYRWEHTDAALTAQLELEQEGVPGVLEPGHAGVRFSNPTTGRDALVTMRTEMRRLRAGTRTAPVRTVGSAIWQVFEGEAVARVGDKVFEIAKGDLFVVPSWCEVSLSARTQVDLFRFSDEPVYEALGLARTSRGEHK
Protein: Di-N-acetylchitobiase (EC 3.2.1.-) (Q01459)
Organism: Homo sapiens (Human)
Function: Involved in the degradation of asparagine-linked glycoproteins. Hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N-acetylglucosamine chitobiose core from the reducing end of the bond, it requires prior cleavage by glycosylasparaginase.
Subcellular location: Lysosome.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MSRPQLRRWRLVSSPPSGVPGLALLALLALLALRLAAGTDCPCPEPELCRPIRHHPDFEVFVFDVGQKTWKSYDWSQITTVATFGKYDSELMCYAHSKGARVVLKGDVSLKDIIDPAFRASWIAQKLNLAKTQYMDGINIDIEQEVNCLSPEYDALTALVKETTDSFHREIEGSQVTFDVAWSPKNIDRRCYNYTGIADACDFLFVMSYDEQSQIWSECIAAANAPYNQTLTGYNDYIKMSINPKKLVMGVPWYGYDYTCLNLSEDHVCTIAKVPFRGAPCSDAAGRQVPYKTIMKQINSSISGNLWDKDQRAPYYNYKDPAGHFHQVWYDNPQSISLKATYIQNYRLRGIGMWNANCLDYSGDAVAKQQTEEMWEVLKPKLLQR
Protein: Small ribosomal subunit protein uS19 (40S ribosomal protein S15) (RIG protein) (P62841)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein eS8
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein eL43
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL21m
Sequence:
MAEVEQKKKRTFRKFTYRGVDLDQLLDMSYEQLMQLYSARQRRRLNRGLRRKQHSLLKRLRKAKKEAPPMEKPEVVKTHLRDMIILPEMVGSMVGVYNGKTFNQVEIKPEMIGHYLGEFSITYKPVKHGRPGIGATHSSRFIPLK
Protein: Adenylate kinase, putative (EC 2.7.4.3) (Q38EC4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Adenylosuccinate lyase
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- Pyruvate kinase
- Adenosine kinase
- Adenosine kinase
- Phosphodiesterase
- Nucleoside diphosphate kinase
- Nucleoside diphosphate kinase, putative
- Nucleoside diphosphate kinase, putative
Sequence:
MTSTEKPKVFFVLGGPGSGKGTVCARLVEEFGYTHFSAGDLLRQASRDKTTEVAQKISQILVEGGIVPSELTVALLKNALNTHPSPRGYVIDGFPRKMDQMFMFEEDIVPAKAILFFDCTEETMEARLIGRASSGSGRDDDNIETIRRRFRTNAEQCVPVVEHYKKQGRLYTVDGNRSREEVYADVKKIFLKEGEELLKK
Protein: Zinc finger protein 846 (Q147U1)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MDSSQHLVTFEDVAVDFTQEEWTLLDQAQRDLYRDVMLENYKNLIILAGSELFKRSLMSGLEQMEELRTGVTGVLQELDLQLKTKGSPLLQDISAERSPNGVQLERSNTAEKLYDSNHSGKVFNEHPFLMTHMITHIGEKTSEDNQSGKALRKNFPHSFYKKSHAEGKMPKCVKHEKAFNQFPNLTRQNKTHTQEKLCECKDCWRTFLNQSSLKLHIRSHNGDKHYVCKECGKAFSNSSHLIGHGRIHSGEKPYVCKECGKAFTQSTGLKLHIRTHSGEKPYKCKECGKAFTHSSYLTDHTRIHSGKKPYVCMECGKAFTRSTGLILHMRIHTGEKPYECKECGKAFIHSSYLTKHVRIHSGEKLYLCKACGKAFTRSSGLVLHMRTHTGEKPYECKECGKAFNNSSMLSQHVRIHTGEKPYECKECGKAFTQSSGLSTHLRTHTGEKACECKECGKAFARSTNLNMHMRTHTGEKPYACKECGKAFRYSTYLNVHTRTHTGAKPYECKKCGKNFTQSSALAKHLRTKACEKT
Protein: Ferredoxin CarAc (Carbazole 1,9a-dioxygenase, ferredoxin component) (CARDO) (D5IGG4)
Organism: Sphingomonas sp
Function: Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol. Acts as a mediator in the electron transfer from fdr to CarAa.
Interaction partners:
Sequence:
MTAKVRVIFRAAGGFEHLVETEAGVSLMEAAVLNGVDGIEAVCGGACACATCHVYVGPEWLDALKPPSETEDEMLDCVAERAPHSRLSCQIRLTDLLDGLTLELPKAQS
Protein: NAC domain-containing protein 40 (ANAC040) (Protein NTM1-like 8) (Q9XIN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator activated by proteolytic cleavage through regulated intramembrane proteolysis (RIP), probably via metalloprotease activity. Regulates gibberellic acid-mediated salt-responsive repression of seed germination and flowering via FT, thus delaying seed germination under high salinity conditions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17410378, ECO:0000269|PubMed:18363782, ECO:0000269|PubMed:19704545}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00353, ECO:0000269|PubMed:17410378, ECO:0000269|PubMed:18363782, ECO:0000269|PubMed:19704545}. Note=Localized primarily in plasma membrane as dormant form and, upon salt stress, is processed into a transcriptionally active and nuclear form after a proteolytic cleavage through regulated intramembrane proteolysis (RIP). {ECO:0000269|PubMed:17410378, ECO:0000269|PubMed:18363782, ECO:0000269|PubMed:19704545}.
Interaction partners:
- MYB-like transcription factor TCL1
- Protein VERNALIZATION INSENSITIVE 3
- glucan endo-1,3-beta-D-glucosidase
- DNA replication ATP-dependent helicase/nuclease JHS1
Sequence:
MSKEAEMSIAVSALFPGFRFSPTDVELISYYLRRKIDGDENSVAVIAEVEIYKFEPWDLPEESKLKSENEWFYFCARGRKYPHGSQSRRATQLGYWKATGKERSVKSGNQVVGTKRTLVFHIGRAPRGERTEWIMHEYCIHGAPQDALVVCRLRKNADFRASSTQKMEDGVVQDDGYVGQRGGLEKEDKSYYESEHQIPNGDIAESSNVVEDQADTDDDCYAEILNDDIIKLDEEALKASQAFRPTNPTHQETISSESSSKRSKCGIKKESTETMNCYALFRIKNVAGTDSSWRFPNPFKIKKDDSQRLMKNVLATTVFLAILFSFFWTVLIARN
Protein: Transcription factor zip-2 (Q21148)
Organism: Caenorhabditis elegans
Function: Transcription factor that binds to the promoter and the enhancer regions of target genes (By similarity). May act together with the bZIP transcription factor, cebp-2. Involved in responding to mitochondrial damage. Plays a role in the delay of age-associated mitochondrial fragmentation and muscle decline. Has a protective role in response to infection by the Gram-negative bacterium P.aeruginosa. Required to prevent P.aeruginosa ToxA-mediated lethality. Required for the activation of infection response genes irg-1 and irg-2 following P.aeruginosa infection.
Subcellular location: Nucleus {ECO:0000269|PubMed:22520465, ECO:0000269|PubMed:26876169}.
Interaction partners:
- CCAAT/enhancer-binding protein homolog 2
- Transcription factor atf-7
- G-protein coupled receptors family 1 profile domain-containing protein
- Transcription factor zip-3
- Protein irg-2
- Mitogen-activated protein kinase pmk-1
- Protein irg-1
- BZIP domain-containing protein
- Cytochrome c oxidase subunit 5A, mitochondrial
- COX5B-domain-containing protein
Sequence:
MEPLSAPLAVGFSAWPPSPPLPPLAHSPLQDAVHADHNHRRILNSCRNLPDCLTTTVPQLHQINSAEQSPLQFTHQPNCDLIVVLDEQTTYTTTMTRRSLPKADRYLSEPNMSTPQASHGSFEFDVPEYTSFDYAFDFPPVPEAFPPAANSSSAASPDADFLDLDSLMSCDITSLDAYIHDDSIASPSNASHISPPASDIDPVDEFFPQLVHNNKIQSSSSSTVETTITRGRKTSSVSSDSSSDYRHKRDKNNLASQKSRQKRQAKIRESKEERERLEKRKVQLQAMVLTLETQVEDYKRLVMMFVKR
Protein: cDNA FLJ60592 (B4DJD2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MYKLFNGTFLKAMEDGGVKLLKERLEKFFHRYLQTLHLQSCDLLDIFGGISFFPLDKMTYLKIQFFINRMEESLNIVKYTAFLYNDQLIWSGLEQDDMRILYKYLTTSLFPRHIEPELAGRDSPIRAEMPGNLQHYGRFLTGPLNLNDPDAKCRFPKIFVNTDDTYEELHLIVYKAMSAAVCFMIDASVHPTLDFCRRLDSIVGPQLTVLASDICEQFNINKRMSGSEKEPQFKFIYFNHMNLAEKSTVHMRKTPSVSLTSVHPDLMKILGDINSDFTRVDEDEEIIVKAMSDYWVVGKKSDRRELYVILNQKNANLIEVNEEVKKLCATQFNNIFFLD
Protein: Deoxyribodipyrimidine photo-lyase (EC 4.1.99.3) (DNA photolyase) (Photoreactivating enzyme) (P00914)
Organism: Escherichia coli (strain K12)
Function: Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.
Interaction partners:
- Peptidyl-tRNA hydrolase
- Uncharacterized protein YbgA
- ABC transporter ATP-binding protein ModF
- Protein RecA
- UvrABC system protein A
- Methylated-DNA--protein-cysteine methyltransferase
Sequence:
MTTHLVWFRQDLRLHDNLALAAACRNSSARVLALYIATPRQWATHNMSPRQAELINAQLNGLQIALAEKGIPLLFREVDDFVASVEIVKQVCAENSVTHLFYNYQYEVNERARDVEVERALRNVVCEGFDDSVILPPGAVMTGNHEMYKVFTPFKNAWLKRLREGMPECVAAPKVRSSGSIEPSPSITLNYPRQSFDTAHFPVEEKAAIAQLRQFCQNGAGEYEQQRDFPAVEGTSRLSASLATGGLSPRQCLHRLLAEQPQALDGGAGSVWLNELIWREFYRHLITYHPSLCKHRPFIAWTDRVQWQSNPAHLQAWQEGKTGYPIVDAAMRQLNSTGWMHNRLRMITASFLVKDLLIDWREGERYFMSQLIDGDLAANNGGWQWAASTGTDAAPYFRIFNPTTQGEKFDHEGEFIRQWLPELRDVPGKVVHEPWKWAQKAGVTLDYPQPIVEHKEARVQTLAAYEAARKGK
Protein: mRNA export factor RAE1 (Rae1 protein homolog) (mRNA-associated protein mrnp 41) (P78406)
Organism: Homo sapiens (Human)
Function: Acts as mRNA export factor involved in nucleocytoplasmic transport. Plays a role in mitotic bipolar spindle formation. May function in attaching cytoplasmic mRNPs to the cytoskeleton both directly or indirectly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9256445}. Nucleus {ECO:0000269|PubMed:9256445}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:17172455}. Nucleus envelope {ECO:0000269|PubMed:33360543}. Note=Recruited from interphase nuclei to spindle MTs during mitosis. {ECO:0000269|PubMed:17172455}.
Interaction partners:
- Nuclear pore complex protein Nup98-Nup96
- Nuclear RNA export factor 1
- mRNA export factor GLE1
- Nuclear pore complex protein Nup214
- Nuclear pore complex protein Nup153
- Nuclear RNA export factor 2
- Nucleoporin SEH1
- Nucleoporin NUP42
- Nuclear RNA export factor 3
- Nuclear RNA export factor 5
Sequence:
MSLFGTTSGFGTSGTSMFGSATTDNHNPMKDIEVTSSPDDSIGCLSFSPPTLPGNFLIAGSWANDVRCWEVQDSGQTIPKAQQMHTGPVLDVCWSDDGSKVFTASCDKTAKMWDLSSNQAIQIAQHDAPVKTIHWIKAPNYSCVMTGSWDKTLKFWDTRSSNPMMVLQLPERCYCADVIYPMAVVATAERGLIVYQLENQPSEFRRIESPLKHQHRCVAIFKDKQNKPTGFALGSIEGRVAIHYINPPNPAKDNFTFKCHRSNGTNTSAPQDIYAVNGIAFHPVHGTLATVGSDGRFSFWDKDARTKLKTSEQLDQPISACCFNHNGNIFAYASSYDWSKGHEFYNPQKKNYIFLRNAAEELKPRNKK
Protein: Fasciclin-like arabinogalactan protein 10 (Q9LZX4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be a cell surface adhesion protein.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Fasciclin-like arabinogalactan protein 15
- Fasciclin-like arabinogalactan protein 19
- Fasciclin-like arabinogalactan protein 21
- Fasciclin-like arabinogalactan protein 18
- Arabinogalactan protein 14
- Classical arabinogalactan protein 9
- Classical arabinogalactan protein 1
- Classical arabinogalactan protein 26
- Phenylcoumaran benzylic ether reductase 1
- Fasciclin-like arabinogalactan protein 17
Sequence:
MATSRAFTLFAFTLSLLTVASTVSGHNITQILSDTPEYSSFNNYLSQTKLADEINSRTTITVLVLNNGAMSSLAGKHPLSVVKNALSLLVLLDYYDPLKLHQLSKGTTLTTTLYQTTGHALGNLGFVNVTDLKGGKVGFGSAAPGSKLDSSYTKSVKQIPYNISVLEINAPIIAPGILTAPAPSSAGVSNITGLLEKAGCKTFANLLVSSGVIKTFESTVEKGLTVFAPSDEAFKARGVPDLTNLTQAEVVSLLEYHALAEYKPKGSLKTNKDAISTLATNGAGKYDLTTSTSGDEVILHTGVGPSRLADTVVDETPVVIFTVDNVLLPAELFGKSSSPAPAPEPVSAPTPTPAKSPSPVEAPSPTAASPPAPPVDESSPEGAPSDSPTSSENSNAKNAAFHVNAPALFTALVTIAATSLLL
Protein: Biorientation of chromosomes in cell division protein 1 (Biorientation defective protein 1) (Protein FAM44B) (Q96IK1)
Organism: Homo sapiens (Human)
Function: Required for proper chromosome biorientation through the detection or correction of syntelic attachments in mitotic spindles.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17938248}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:17938248}. Note=Localizes at the centrosomes throughout the cell cycle, only dissociating during cytokinesis. Localizes at the kinetochore from prometaphase until anaphase.
Interaction partners:
- Spindle and kinetochore-associated protein 3
- SKA complex subunit 1
- Spindle and kinetochore-associated protein 2
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Protein Spindly
- Centromere protein F
- CXXC-type zinc finger protein 1
- WD repeat-containing protein 5
- Retinoblastoma-binding protein 5
- Set1/Ash2 histone methyltransferase complex subunit ASH2
Sequence:
MADGGGGGGTGAVGGGGTSQASAGAATGATGASGGGGPINPASLPPGDPQLIALIVEQLKSRGLFDSFRRDCLADVDTKPAYQNLRQKVDNFVSTHLDKQEWNPTMNKNQLRNGLRQSVVQSGMLEAGVDRIISQVVDPKLNHIFRPQIERAIHEFLAAQKKAAVPAPPPEPEGQDPPAPSQDTS
Protein: Dpr-interacting protein alpha, isoform A (Dpr-interacting protein alpha, isoform C) (RE16159p) (Q9W4R3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Defective proboscis extension response 10, isoform A
- Defective proboscis extension response 6, isoform F
- Defective proboscis extension response 3, isoform B
Sequence:
MPVSAKRLLRNFQFTSCDRNGKMLIHLLLIVSLLEAIGAFQPEFVESISNVSVAVGRDATFTCHVRHLGGYRVGWLKADTKAIQAIHENVITHNPRVTVSHLDQNTWNLHIKAVSEEDRGGYMCQLNTDPMKSQIGFLDVVIPPDFISEDTSSDVIVPEGSSVRLTCRARGYPEPIVTWRREDGNEIVLKDNVGTKTLAPSFRGEVLKLSKISRNEMGSYLCIASNGVPPSVSKRISLSIHFHPVIQVPNQLVGAPLGTDVQIECHVEASPKSINYWIKDTGEMIVTSGKYHVQESSQSMYETKMSMIVRKFQKDDVGSYRCIAKNSLGEVDSSIRLYEIPGPNRNKNPLNGGGKGGGAGGSLDADANDILKQKQQVKVTYQPEDEELQYGSVEDFEAEGGEGGGLTPLSPHVYYTSGNKPATHKPGNSGGNQHLHQQHHHHHHHNNNNNNQQHSGGPGGGPTGGDAGSLGGEMGGITRKPPPYYGGNTEVRGPIDNNEMSSGSGDSRLCRGHHLPILLLPFARLILVRSWHCRHTFLMGLSQACLPGLLLSLL
Protein: Kunitz-type serine protease inhibitor textilinin-1 (Txln-1) (Q90WA1)
Organism: Pseudonaja textilis textilis (Eastern brown snake)
Function: Strongly inhibits plasmin (Ki=0.44 nM) and trypsin (Ki=0.42 nM). Has little effect on plasma (Ki=1870 nM) and tissue (Ki=12900 nM) kallikreins. In vivo, reduces bleeding in a small animal model.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MSSGGLLLLLGLLTLWEVLTPVSSKDRPDFCELPADTGPCRVRFPSFYYNPDEKKCLEFIYGGCEGNANNFITKEECESTCAA
Protein: Receptor activity-modifying protein 2 (Q9WUP0)
Organism: Mus musculus (Mouse)
Function: Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O60895}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:O60895}.
Interaction partners:
- Calcitonin gene-related peptide type 1 receptor
- Pro-adrenomedullin
- Calcitonin receptor
- Receptor activity-modifying protein 3
- Islet amyloid polypeptide
- Receptor activity-modifying protein 1
- Calcitonin gene-related peptide 2
- Calcitonin
- Protein ADM2
- Vasoactive intestinal polypeptide receptor 1
Sequence:
MAPLRVERAPGGSRLGVTRAQRPTALCLPPLLLLLLLLLGAVSASPESLNQSLPESQNQSHPTEDSLVSKGKMEDYETHVLPCWYEYKSCMDSVKDWCNWTLISRHYSDLQNCLEYNADKFGLGFPNPLAENIILEAHLIHFANCSLVQPTFSDPPEDVLLAMIIAPICLIPFLVTLVVWRSKDSDAQA
Protein: Beta galactosidase, isoform B (EC 3.2.1.23) (M9PCA6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGCRRNRKLTMAVSGCLIIAVMALTVGLCVGLSGDTDAPEPRFTIDHEANTFMLDGQPFRYVSGSFHYFRAVPESWRSRLRTMRASGLNALDTYVEWSLHNPHDGEYNWEGIADVVKFLEIAQEEDFYIILRPGPYICAERDNGGLPHWLFTKYPSIKMRTNDPNYISEVGKWYAELMPRLQHLFVGNGGKIIMVQVENEYGDYACDHDYLNWLRDETEKYVSGKALLFTVDIPNEKMSCGKIENVFATTDFGIDRINEIDKIWAMLRALQPTGPLVNSEFYPGWLTHWQEQNQRRDGQEVANALRTILSYNASVNLYMFFGGTNFGFTAGANYNLDGGIGYAADITSYDYDAVMDEAGGVTTKYNLVKAVIGEFLPLPEITLNPAKRLAYGRVELTPKLTLLSTEGRAALSKGDPVESIKPKTFEELDLYSGLVLYETELPSMDLDPALLKIDQINDRAHVFVDQELVGTLSREAQIYSLPLSKGWGSTLQLLVENQGRVNFYISNDTKGIFGEVSLQLHNGGYLPLENWRSTAFPLEQSAVELWRREHTDEKALDPLLARQRILRNGPILYTGSLTVTEVGDTYLNMAGWGKGVAYVNGFNLGRYWPVAGPQVTLYVPNEILKVGENSLVILEYQRANKTATGEDLPAVQFDAVAQLDGESGDVPLK
Protein: Medium/long-chain-fatty-acid--CoA/3-oxocholest-4-en-26-oate--CoA ligase (FACL) (EC 6.2.1.2) (EC 6.2.1.3) (EC 6.2.1.42) (Acyl-CoA synthetase) (FACL19) (Steroid-CoA ligase) (Steroid-coenzyme A ligase) (P9WQ51)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension. Also involved in the degradation of cholesterol via the degradation of the side chains of C-24 branched-chain sterols. Catalyzes the ATP-dependent CoA thioesterification of the sterol 3-oxocholest-4-en-26-oate to yield 3-oxocholest-4-en-26-oyl-CoA. It can also use 3beta-hydroxy-5-cholesten-26-oate.
Interaction partners:
- Enoyl-CoA hydratase EchA19
- Possible lipid transfer protein or keto acyl-CoA thiolase Ltp4
- Probable lipid carrier protein or keto acyl-CoA thiolase Ltp3
- Acyl-CoA dehydrogenase FadE26
- Steroid C26-monooxygenase-3-oxocholest-4-en-26-oate forming])
- Steroid 3-ketoacyl-CoA thiolase
- Acyl-CoA dehydrogenase FadE27
- ChsH2 C-terminal OB-fold domain-containing protein
- Acyl-CoA dehydrogenase FadE34
- Steroid C26-monooxygenase-3-oxocholest-4-en-26-oate forming])
Sequence:
MAVALNIADLAEHAIDAVPDRVAVICGDEQLTYAQLEDKANRLAHHLIDQGVQKDDKVGLYCRNRIEIVIAMLGIVKAGAILVNVNFRYVEGELRYLFDNSDMVALVHERRYADRVANVLPDTPHVRTILVVEDGSDQDYRRYGGVEFYSAIAAGSPERDFGERSADAIYLLYTGGTTGFPKGVMWRHEDIYRVLFGGTDFATGEFVKDEYDLAKAAAANPPMIRYPIPPMIHGATQSATWMALFSGQTTVLAPEFNADEVWRTIHKHKVNLLFFTGDAMARPLVDALVKGNDYDLSSLFLLASTAALFSPSIKEKLLELLPNRVITDSIGSSETGFGGTSVVAAGQAHGGGPRVRIDHRTVVLDDDGNEVKPGSGMRGVIAKKGNIPVGYYKDEKKTAETFRTINGVRYAIPGDYAQVEEDGTVTMLGRGSVSINSGGEKVYPEEVEAALKGHPDVFDALVVGVPDPRYGQQVAAVVQARPGCRPSLAELDSFVRSEIAGYKVPRSLWFVDEVKRSPAGKPDYRWAKEQTEARPADDVHAGHVTSGG
Protein: Ras-related protein RABD2a (AtRABD2a) (Ras-related protein Ara-5) (Ras-related protein Rab1B) (AtRab1B) (P28188)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:19789181}. Golgi apparatus membrane {ECO:0000305|PubMed:19789181}; Lipid-anchor {ECO:0000305|PubMed:19789181}.
Interaction partners:
- Tetratricopeptide repeat
- Trafficking protein particle complex subunit
- Trafficking protein particle complex II-specific subunit 120 homolog
- Tetratricopeptide repeat
- Trafficking protein particle complex subunit
- small monomeric GTPase
- Trafficking protein particle complex subunit
- Transport protein particle
- Trafficking protein particle complex subunit
- SNARE-like superfamily protein
Sequence:
MNPEYDYLFKLLLIGDSGVGKSCLLLRFSDDSYVESYISTIGVDFKIRTVEQDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIIVYDVTDEESFNNVKQWLSEIDRYASDNVNKLLVGNKSDLTENRAIPYETAKAFADEIGIPFMETSAKDATNVEQAFMAMSASIKERMASQPAGNNARPPTVQIRGQPVAQKNGCCST