wanglab/gogpt-training-data huggingface dataset:
Protein: Leukocyte immunoglobulin-like receptor subfamily B member 3 (LIR-3) (Leukocyte immunoglobulin-like receptor 3) (CD85 antigen-like family member A) (Immunoglobulin-like transcript 5) (ILT-5) (Monocyte inhibitory receptor HL9) (CD antigen CD85a) (O75022)
Organism: Homo sapiens (Human)
Function: May act as receptor for class I MHC antigens. Becomes activated upon coligation of LILRB3 and immune receptors, such as FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-cell activation by recruiting phosphatases to its immunoreceptor tyrosine-based inhibitor motifs (ITIM).
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 6
- Tyrosine-protein kinase SYK
- CMRF35-like molecule 6
- HLA class I histocompatibility antigen, alpha chain F
- Leukocyte immunoglobulin-like receptor subfamily B member 2
- HLA class I histocompatibility antigen, alpha chain E
- Leukocyte immunoglobulin-like receptor subfamily A member 6
- TYRO protein tyrosine kinase-binding protein
Sequence:
MTPALTALLCLGLSLGPRTRVQAGPFPKPTLWAEPGSVISWGSPVTIWCQGSQEAQEYRLHKEGSPEPLDRNNPLEPKNKARFSIPSMTEHHAGRYRCHYYSSAGWSEPSDPLEMVMTGAYSKPTLSALPSPVVASGGNMTLRCGSQKGYHHFVLMKEGEHQLPRTLDSQQLHSRGFQALFPVGPVTPSHRWRFTCYYYYTNTPWVWSHPSDPLEILPSGVSRKPSLLTLQGPVLAPGQSLTLQCGSDVGYNRFVLYKEGERDFLQRPGQQPQAGLSQANFTLGPVSPSNGGQYRCYGAHNLSSEWSAPSDPLNILMAGQIYDTVSLSAQPGPTVASGENVTLLCQSWWQFDTFLLTKEGAAHPPLRLRSMYGAHKYQAEFPMSPVTSAHAGTYRCYGSYSSNPHLLSHPSEPLELVVSGHSGGSSLPPTGPPSTPGLGRYLEVLIGVSVAFVLLLFLLLFLLLRRQRHSKHRTSDQRKTDFQRPAGAAETEPKDRGLLRRSSPAADVQEENLYAAVKDTQSEDRVELDSQSPHDEDPQAVTYAPVKHSSPRREMASPPSSLSGEFLDTKDRQVEEDRQMDTEAAASEASQDVTYAQLHSLTLRRKATEPPPSQEGEPPAEPSIYATLAIH
Protein: Platelet-activating factor acetylhydrolase IB subunit alpha2 (EC 3.1.1.47) (PAF acetylhydrolase 30 kDa subunit) (PAF-AH 30 kDa subunit) (PAF-AH subunit beta) (PAFAH subunit beta) (Platelet-activating factor acetylhydrolase alpha 2 subunit) (PAF-AH alpha 2) (O35264)
Organism: Rattus norvegicus (Rat)
Function: Alpha2 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF. The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition. The alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2 homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE) more efficiently than 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA). In contrast, the alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes AAGPA more efficiently than PAF, but has little hydrolytic activity towards AAGPE (By similarity). May play a role in male germ cell meiosis during the late pachytenestage and meiotic divisions as well as early spermiogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Platelet-activating factor acetylhydrolase IB subunit alpha
- Platelet-activating factor acetylhydrolase IB subunit alpha1
- Platelet-activating factor acetylhydrolase 2, cytoplasmic
- Platelet-activating factor acetylhydrolase.
- Lysophosphatidylcholine acyltransferase 2
- Lysophosphatidylcholine acyltransferase 1
- Lysophosphatidylcholine acyltransferase 2B
- Lysophosphatidylcholine acyltransferase 4
- Choline/ethanolaminephosphotransferase 1
- Cholinephosphotransferase 1
Sequence:
MSQGDSNPAAIPHAAEDIQGDDRWMSQHNRFVLDCKDKEPDVLFVGDSMVQLMQQYEIWRELFSPLHALNFGIGGDTTRHVLWRLKNGELENIKPKVIVVWVGTNNHENTAEEVAGGIEAIVQLINTRQPQAKIIVLGLLPRGEKPNPLRQKNAKVNQLLKVSLPKLANVQLLDIDGGFVHSDGAISCHDMFDFLHLTGGGYAKICKPLHELIMQLLEETPEEKQTTIA
Protein: WW domain-containing protein A (Q54T86)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in regulation of actin cytoskeleton organization and cytokinesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:14595117}. Nucleus, nucleolus {ECO:0000269|PubMed:14595117}. Cytoplasm, cell cortex {ECO:0000269|PubMed:14595117}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14595117}. Note=In living cells localizes to the cell cortex and nucleus. In formaldehyde fixed cells localizes to the nucleolus. {ECO:0000269|PubMed:14595117}.
Interaction partners:
- Arrestin domain-containing protein F
- Probable serine/threonine-protein kinase DDB_G0290859
- Ras-interacting protein RIP3
- Probable serine/threonine-protein kinase ndrA
Sequence:
MSNKNPLNNSNGSNSSTIVNSDKFLVKIHSLSVSHTSKSSNIYLVGDFDQFKQFKTETKKSSSTHGSCIYNEFAMEFQYETKYIHKLDHKHFKICVYKKKSIGSDKYIGSFGVDLYTLATGPISHDVVFQKDNTGVGRLQFRLEMNHITDIQISFKSILLSNLMKQSNYQIDYSLNKINPLKSSIIENTICPSWYNQSSILMNISLKDLVDGSIFFNLKDTKSSKVIGELKLPVKSIFSFVEGDIKIVKTLLYNEKQNKICDACIEIQFNNIPQLAQLRGGIQTEQGIRGAESFFSGVPLPKIIGEISNASTSDGYSKEAQLQHVKLPDGWESRIDPVSGKVFYLNHNNKTTSWISPLEHAPVKKRTPTVVISNTTILDNNNNNNNNNNNNNNNNNNNNNNINNTNNIQQKQQAQQQPVQPPPQPVQQQVQQPQQKEKEKEKEINAEDYKISRPKKTPATPEEAAVIIQRTFRNHKKQSYNKTIRNSKTIIPPNNVQQQQPQQTEKPSIYQVFGQQIDQGLPNGWEVRQDQFGRVFYVDHINRATTWTRPTVKHPKQHQQATLVQQRK
Protein: Aldehyde-alcohol dehydrogenase (AAD) [Includes: Alcohol dehydrogenase (ADH) (EC 1.1.1.1); Aldehyde dehydrogenase (ALDH) (EC 1.2.1.3)] (P33744)
Organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)
Function: Has both aldehyde and alcohol dehydrogenase activities. Can use acetaldehyde, butyraldehyde, butanol and ethanol.
Interaction partners:
Sequence:
MKVTTVKELDEKLKVIKEAQKKFSCYSQEMVDEIFRNAAMAAIDARIELAKAAVLETGMGLVEDKVIKNHFAGEYIYNKYKDEKTCGIIERNEPYGITKIAEPIGVVAAIIPVTNPTSTTIFKSLISLKTRNGIFFSPHPRAKKSTILAAKTILDAAVKSGAPENIIGWIDEPSIELTQYLMQKADITLATGGPSLVKSAYSSGKPAIGVGPGNTPVIIDESAHIKMAVSSIILSKTYDNGVICASEQSVIVLKSIYNKVKDEFQERGAYIIKKNELDKVREVIFKDGSVNPKIVGQSAYTIAAMAGIKVPKTTRILIGEVTSLGEEEPFAHEKLSPVLAMYEADNFDDALKKAVTLINLGGLGHTSGIYADEIKARDKIDRFSSAMKTVRTFVNIPTSQGASGDLYNFRIPPSFTLGCGFWGGNSVSENVGPKHLLNIKTVAERRENMLWFRVPHKVYFKFGCLQFALKDLKDLKKKRAFIVTDSDPYNLNYVDSIIKILEHLDIDFKVFNKVGREADLKTIKKATEEMSSFMPDTIIALGGTPEMSSAKLMWVLYEHPEVKFEDLAIKFMDIRKRIYTFPKLGKKAMLVAITTSAGSGSEVTPFALVTDNNTGNKYMLADYEMTPNMAIVDAELMMKMPKGLTAYSGIDALVNSIEAYTSVYASEYTNGLALEAIRLIFKYLPEAYKNGRTNEKAREKMAHASTMAGMASANAFLGLCHSMAIKLSSEHNIPSGIANALLIEEVIKFNAVDNPVKQAPCPQYKYPNTIFRYARIADYIKLGGNTDEEKVDLLINKIHELKKALNIPTSIKDAGVLEENFYSSLDRISELALDDQCTGANPRFPLTSEIKEMYINCFKKQP
Protein: TATA box-binding protein-like 1 (TBP-like factor) (M9PHD8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSAVKKGDGSPTRILEEYQVARDLRNEDLFPEHPVEHPDEDSDKENQSPNQSPNPRAIGDCEQGPDIGKDTLNPNEADQFSSEEVEKNEANSSCNESGGDARNSRDRLSSSHSEDEQLNQEYSTSSSGSTIGNREQGSDVGKDTSSRNEADQFSNEEVEKNEANSSGNESYGDACNSNRLSSSNSEDEQLHQEYSTSSRGRTREYAQSDLNPGYQDLNIGNQDLNQVNREYQESNNEYQVSNQEYQHLNTEYQELNHGDQDSNDEYQELNHGNQDSNDEYQESNHGNQDSNDEYQELNHSNQDSNDEYQELNHGDQDSSDEYQDLNHVNQDSNHEYQAWNHEYQDSNHEYQALNREYQYPESDEEEAARKRNIYTRLRSYACQVHLPRLGESEVDSDDRRHNPINQPFNQPINRPNQKSDSSLESSSPERQDSESESRQASDEESSSGDSDYLIDPVTGWLSRRRETSTEREEKSDQSQQESSEEITDEQKEESDDVEQQSPAEHTSSDRRDHSPDKQQNKRKSLGTGNSSYSKKPLLDGDKGDPRSHLSSLGSRRSLKRKWPFDCTDSKKFKPNLQSEEDKSEEEKREDTESECSDEEDSDSSSFDTDSNSDSDSNLDLDSDSDSHSDFESSSSSEESAQDPAPEGETDQDPAPEGEADQDPAPEGGVDQDPAPEGGVDQDPAPEGEVDQDPAPEGESDQDLAPEGGVDQDPAPEFGTDQDPHPYYNDQDPAPYYDDQDPASYYDDHICDSEEDYKPFIFSKERKFLKFVTNPLGDDKSSLDLSIQLYKVFGAYKLEDVYSSIDEEGQPEQDLQLKQQQKHLKKYQKLQLVVFWHQEKFFSKEQLLLYEYLKLLLQKFFPQEQQEKRLQQEKLLQQEKLLQQEKRLQQEKRLQQEKRLQQEKRLQQEKRLQQQKLLQQQKLLQQEKLLQQQKLLQQEKLLQQEKLLQQEKQLQQEKHLPQERQLQQDKVFLQLRQLQQKKELEEQRERKRHLFEQQKQFVLEKLRQQKEQHRRQQNRVKRERKLRQKKEKQRLEYERFLKEYREDCKRQLRLQREHYLIKIKQLEKASQRSLKGNRKHKLMQNDMVSIPVANLNGGLKAASSGSGVGVVTSGGVVSSAVLANAPRVYLTPSSTFMTNRQMAGVASTGRMSGQVVGGSSGTASTAGTVRYFSQFSKMQTAGGPSLQRKLANGDTIVLATGSKNMFLTSSENKANLPTVASNGNGLITAKMDLLEEEVMQSITVIDDDDEEKKEVAEDEEESSNNAKPIDLHQPIADNEHELDIVINNVVCSFSVGCHLKLREIALQGSNVEYRRENGMVTMKLRHPYTTASIWSSGRITCTGATSESMAKVAARRYARCLGKLGFPTRFLNFRIVNVLGTCSMPWAIKIVNFSERHRENASYEPELHPGVTYKMRDPDPKATLKIFSTGSVTVTAASVNHVESAIQHIYPLVFDFRKQRSAEELQHLRQKQRLQAGGDPHELEKNVLADNKTASLDNIFVNTTAAHSKSSSNDQTSAPATILSSTVDSMPRLKQMVNYHQMMKQTQEERRHIMFNGEKANPASTSSAAAAPSTSSSSSSSGDNICANARRRATECWATKLQNKRPRYNDPGTTGTINAASSTASAATSSLASQATHLRNPLKTAALANARMLGAKVTTCTRNSIIVQQPQRIQMQQQQQQLQPQQQQTSFSPSEFDVDDLIEEEENNELDMPF
Protein: Centrosomal protein CCDC61 (Coiled-coil domain-containing protein 61) (VFL3 homolog) (Q08CF3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Microtubule-binding centrosomal protein required for centriole cohesion, independently of the centrosome-associated protein/CEP250 and rootletin/CROCC linker. In interphase, required for anchoring microtubule at the mother centriole subdistal appendages and for centrosome positioning. During mitosis, may be involved in spindle assembly and chromatin alignment by regulating the organization of spindle microtubules into a symmetrical structure. Plays a non-essential role in ciliogenesis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y6R9}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q9Y6R9}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9Y6R9}. Note=Localization at the centriolar satellite is dependent on intact microtubule network. Localizes at the centriole subdistal appendages and proximal ends. Localized to centrosomal/satellite-like structures with the onset of centrosome separation in early G2. {ECO:0000250|UniProtKB:Q9Y6R9}.
Interaction partners:
- Inhibitor of growth protein
- Inhibitor of growth protein
- Bromodomain-containing protein 9
- Tissue factor pathway inhibitor
- FACT complex subunit
Sequence:
MEVGTVVQEEMKFRGSEFAVKVEMAERLLIVEISDVVTADQWRGEFGPAYIEDLTRKTGNFKQFPVFCSMLESAVHKSSDSVTLDLLTYSDLELLRNRKAGVVGRPRAQPQSPALSAKRYLILIYTVEFDRIHYPLPLPYLGKPDPAELQKEIRALRSELKTLGLRGDHKVSDQETRKLRTELALVRDEKEALAKALDRLQMVGSGSAPGARGLREAVHSLEEQLLKERAKSQRSAIKKSQEQRLLVEQLEELRASERALRIRVKSLTTELALLRRGRATPVLSDRGGLRGDGVVHRSLSRERSLTRVGIRARSGSRERIEDRGRRSEERVRRADSSGSRNCITRPSPSPTGSRVPRFDPTAYIQDRQRRQKEAELKSQRKIRRDMLASPSLMERGRSRSREPVPQLMRAGSAGRGRSVSVESRRSRCSSEGSVAEFEELAKPLNSRGRKLMSNGPAVSRGRHINKKPMCSTPAQRMRAGDTSMDTGADLSEIDARLQALQDYMRDLDTGH
Protein: Terpene cyclase/mutase family member (EC 5.4.99.-) (A7BJ35)
Organism: Rhizophora stylosa (Bakau) (Red mangrove)
Interaction partners:
Sequence:
MWRLKIAEGGDPWLRTINNHVGRQVWEFDPSLVGSPEDIADIENARRNFTINRFHHRHSADLLMRLQFAKENRLPPVLPKVAVKDDEDVTEQAVTVTLRRALDYFSTIQAHDGHWPGDYGGPMFLMPGLVIALSVTGALNAILSREHQREICRYLYNHQNEDGGWGLHIEGPSTMFGSVLNYVTLRLIGEGANDGEGAMERGRNWILNHGGATHITSWGKMWLSVLGVFEWRGNNPLPPETWPLPYLLPVHPGRMWCHCRMVYLPMSYLYGKRFVGPITPTVLSLRKELFTVPYHDIDWNDARNLCAKEDLYYPHPLVQDLLWAFLDKAIEPFLMRWPGKKLRERAFQSVMEHVHYEDENTRYICIGPVNKVLNMLCCWVEDPNSEAFKLHLPRIHDYLWIAEDGMKMQGYNGSQLWDLSFAVQAIAATNLVEEYGPTLKKAHSFVKSSQVPEDCPGVLNSWYRHISKGAWPSSTADHGWPISDCTAEGLKAARLLSKISSVIVGEPLSANRLYDAVNILLSLQNVDGGYATYELTRSYSWLEVINPAETFGDIVIDYPYVECTSSAIQGLVSFKKSYPGHRREEIERCIRKAATFIESIQKADGSWYGSWGVCFTYATWFGIKGLVAAGKNFNNCSSIRKACDFLLSRQCASGGWGESYLSCQEKVYSNLEGNRSHIVNTAWAMLALIGAGQAERDPTPLHRSARYLINSQMDNGDFPQQEIMGVFNRNCMISYSAYKDIFPIWALGEYRCRVLQAS
Protein: Enolase 1-1 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 1-1) (2-phosphoglycerate dehydratase 1-1) (P40370)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Pyruvate kinase
- Phosphoglycerate kinase
- Triosephosphate isomerase
- ATP-dependent 6-phosphofructokinase
- Probable transketolase
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Glyceraldehyde-3-phosphate dehydrogenase 1
Sequence:
MAIQKVFARQIYDSRGNPTVEVDLTTETGIHRAIVPSGASTGIWEALEMRDGDKTKWGGKGVLKAVGNVNNIIAPAVVKANLDVTDQKAADEFLLKLDGTENKSKLGANAILGVSMAICRAGAAQKKLPLWKYIAENFGTKGPYVLPVPSFNVLNGGSHAGGDLAFQEFMILPTGAPSFSEAMRWGAETYHTLKSIAKKRYGSSAGNVGDEGGIAPDLQTPQEALDLIVEAINKAGYEGKIKIGLDVASSEFYVDGKYDLDIKAAKPKPENKLTYQQLTDLYVELSKKYPIVSIEDPFDQDDWSAWTHMKAETDFQIVGDDLTVTNVKRLRTAIDKKCANALLLKVNQIGSVTESLNAVRMSYEAGWGVMVSHRSGETADTFISHLTVGIGAGQLKSGAPCRSERLAKYNELLRIEEELGSEGVYAGAHAGKYIKAAKF
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I5ZYP2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MANDSPAKSLVDIDLSSLRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSITDLVKNTKGNTLKEDWIAYISREILRGLAHLHIHHVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDLWSCGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFFSFIEGCLVKNYMQRPSTEQLLKHPFIRDQPNERQVRIQLKDHIDRTRKKRGEKDETEYEYSGSEEEEEEVPEQEGEPSSIVNVPGESTLRRDFLRLQQENKERSEALRRQQLLQEQQLREQEEYKRQLLAERQKRIEQQKEQRRRLEEQQRREREARRQQEREQRRREQEEKRRLEELERRRKEEEERRRAEDEKRRVEREQEYIRRQLEEEQRHLEILQQQLLQEQAMLLECRWREMEEHRQAERLQRQLQQEQAYLLSLQHDHRRPHAQQPPPPQQQDRSKPSYHAPEPKPHYDPADRAREVQWSHLASLKNNVSPVSRSHSFSDPSPKFAHHHLRSQDPCPPSRSEGLSQSSDSKSEVPEPTQKAWSRSDSDEVPPRVPVRTTSRSPVLSRRDSPLQGSGQQNSQAGQRNSTSSIEPRLLWERVEKLVPRPGSGSSSGSSNSGSQPGSHPGSQSGSGERFRVRSSSKSEGSPSQRLENAAKKPEDKKEVFRPLKPADLTALAKELRAVEDVRPPHKVTDYSSSSEESGTTDEEEEDVEQEGADDSTSGPEDTRAASSLNLSNGETESVKTMIVHDDVESEPAMTPSKEGTLIVRQSTVDQKRASHHESNGFAGRIHLLPDLLQQSHSSSTSSTSSSPSSSQPTPTMSPQTPQDKLTANETQSASSTLQKHKSSSSFTPFIDPRLLQISPSSGTTVTSVVGFSCDGLRPEAIRQDPTRKGSVVNVNPTNTRPQSDTPEIRKYKKRFNSEILCAALWGVNLLVGTESGLMLLDRSGQGKVYPLISRRRFQQMDVLEGLNVLVTISGKKDKLRVYYLSWLRNKILHNDPEVEKKQGWTTVGDLEGCVHYKVVKYERIKFLVIALKSSVEVYAWAPKPYHKFMAFKSFGELVHKPLLVDLTVEEGQRLKVIYGSCAGFHAVDVDSGSVYDIYLPTHIQCTIKPHAIIILPNTDGMELLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIRSNQTMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVYFMTLGRTSLLSW
Protein: Cyclin-Y (P34624)
Organism: Caenorhabditis elegans
Function: In association with pct-1, regulates the trafficking of synaptic vesicle precursors in DA motor neurons by promoting anterograde trafficking to the axon and preventing dynein-dependent trafficking to the dendrite. May also regulate synaptic vesicle trafficking in DD motor neurons and in RIA interneurons. Involved in synapse formation during DD motor neuron remodeling by disassembling ventral presynaptic structures. May activate cdk-5.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20510931}. Cell projection, dendrite {ECO:0000269|PubMed:20510931}. Cell projection, axon {ECO:0000269|PubMed:20510931}. Note=Enriched in the dendrite and the proximal axon of the DA motor neuron. {ECO:0000269|PubMed:20510931}.
Interaction partners:
- Cyclin-dependent kinase 17
- Cyclin-dependent-like kinase 5
- PITH domain-containing protein ZK353.9
Sequence:
MGNSSCCLRTRSSSGEDKSYNNDGQYIRTNQVEFQYVNQVFPRDETSTNFLPHISEREVTEGYEEDPSTNPTARPTFMERSKSEMKLKDNRRSCYMLDALAAGGHHPGILPRSLRKSSSCSTIYIDDSTVSQPHLKNTIKCISLAIYYHISNRKNRGHERLMEIFEERLHPIFRDPIPPEQMTRDPDHRNIYRFVRNLFSSAQLTAECAIITLVYIERLLNYAEMDLCPSNWRRVVLGSIMLASKVWDDQAVWNVDYCQILRDTNVDDMNELERRFLECLDFNIEVPSSVYAKYYFDLRTLALANDLQLPIQPLYKERAQRLEALSRVFEDKIQSSSLPKRARSAEHLVFEHPAVLS
Protein: Tenomodulin (TeM) (mTeM) (Chondromodulin-1-like protein) (ChM1L) (mChM1L) (Chondromodulin-I-like protein) (Myodulin) (Tendin) (Q9EP64)
Organism: Mus musculus (Mouse)
Function: May be an angiogenesis inhibitor.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}.
Interaction partners:
- Basic helix-loop-helix transcription factor scleraxis
- Homeobox protein Mohawk
- Fibromodulin
- Decorin
- Thrombospondin-4
- Collagen alpha-1
Sequence:
MAKNPPENCEGCHILNAEALKSKKICKSLKICGLVFGILALTLIVLFWGSKHFWPEVSKKTYDMEHTFYSNGEKKKIYMEIDPITRTEIFRSGNGTDETLEVHDFKNGYTGIYFVGLQKCFIKTQIKVIPEFSEPEEEIDENEEITTTFFEQSVIWVPAEKPIENRDFLKNSKILEICDNVTMYWINPTLIAVSELQDFEEDGEDLHFPTSEKKGIDQNEQWVVPQVKVEKTRHTRQASEEDLPINDYTENGIEFDPMLDERGYCCIYCRRGNRYCRRVCEPLLGYYPYPYCYQGGRVICRVIMPCNWWVARMLGRV
Protein: Palmdelphin (Paralemmin-like protein) (Q9NP74)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11707320}. Cell projection, dendrite {ECO:0000269|PubMed:11707320}. Cell projection, dendritic spine {ECO:0000250}.
Interaction partners:
Sequence:
MEEAELVKGRLQAITDKRKIQEEISQKRLKIEEDKLKHQHLKKKALREKWLLDGISSGKEQEEMKKQNQQDQHQIQVLEQSILRLEKEIQDLEKAELQISTKEEAILKKLKSIERTTEDIIRSVKVEREERAEESIEDIYANIPDLPKSYIPSRLRKEINEEKEDDEQNRKALYAMEIKVEKDLKTGESTVLSSIPLPSDDFKGTGIKVYDDGQKSVYAVSSNHSAAYNGTDGLAPVEVEELLRQASERNSKSPTEYHEPVYANPFYRPTTPQRETVTPGPNFQERIKIKTNGLGIGVNESIHNMGNGLSEERGNNFNHISPIPPVPHPRSVIQQAEEKLHTPQKRLMTPWEESNVMQDKDAPSPKPRLSPRETIFGKSEHQNSSPTCQEDEEDVRYNIVHSLPPDINDTEPVTMIFMGYQQAEDSEEDKKFLTGYDGIIHAELVVIDDEEEEDEGEAEKPSYHPIAPHSQVYQPAKPTPLPRKRSEASPHENTNHKSPHKNSISLKEQEESLGSPVHHSPFDAQTTGDGTEDPSLTALRMRMAKLGKKVI
Protein: Adenylate cyclase (Q9HTS8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Cyclic AMP
- CyaB
- cAMP-activated global transcriptional regulator Vfr
- GTP pyrophosphokinase
- Pyruvate kinase
- Pyruvate kinase
- guanosine-3',5'-bis
- Nucleoside diphosphate kinase
- Nucleoside triphosphate pyrophosphohydrolase
- Class III
Sequence:
MNRHPALSLDLDDGIDRKVLGQLRQRFLAVNAGRLQRARQALSSRQERVLRLLPLLFHINHPLLPGYLSASTPAGLSGFEADDEVLAEAQRLARSFVYKPRRQEPAQQPIHGLFLMGSLGSLAQEEQSDLDLWVCHAPELEPGARQELRRKCALIEDWARSQGSEVHCFLIDVARFGQDEREDRKEPGGDGNTQHFLLLDEFYRSAIWLGGRTPLWWLVPPAHERRYDEYCRTLLGKRFIRAEEVLDLGHLAHIPAREFIGAGLWQLSKAIDSPYKSLLKLLLTEAYASEHPRVRCVALRFKEQVFAGQLDLDELDPYVLVYRHLERYLREQQAPERLELVRRCLYLKVGRKLGGRQRQAQKGWQHLSMERLVAEWQWEPRRLALLDSRSQWKMRQVMEERRTVVNELTYSYRLLFQIARQQGADSGIDSRDLGLLGRRLYAAFERKAGKVENINPGIAPDLGEDVLTLVQLPADDGREQAQWAIFPGALGAHQWPDYAPLKRSLRLVELLAWCHRNGVIDSATRLSLHPGQSDLGDAELDNLLGSLRQFLPVPLATVDDADLLQPRRLKSVLLLVNVGVDPLRHHSQMNLHMATGRTDVLGYAGVRDNLVLTLDQLSLNSWNELTVRHYAGPQALPECLAEFLDAVREKPGSPPQPPELMVRCFCRNRAAAIAVRVEELFRETYGQLLGGQPSRYLLQIRQQYHLLEMSPEAVSHESLPDLPSLLQHLGRERDGYSALKLDRHALEGEDLGLILSMGRPDCIQVFYRRDFDSAEISLLDERNALWRQRQALRDERSLLAPLQRFLQSLLYRRNALSLAEQVPAALDIRYYELLSNDGRVHVEPREAPEALAGPALYELQALLERGERKRVQVTLYCDHQEFSELEYGAGLFKAVARHILAHRAESEPYPCYLTDLDLSRLFADEQPQTLHYLRYKSVLETALNQALLEQ
Protein: Protein isy-1 (Q20716)
Organism: Caenorhabditis elegans
Function: Regulates the processing of the mir-60 microRNA (miRNA), which in turn negatively regulates the expression of the transcription factor zip-10. Does not affect the splicing of zip-10.
Subcellular location: Nucleus {ECO:0000269|PubMed:29664006}.
Interaction partners:
- TPR_REGION domain-containing protein
- Protein BUD31 homolog
- Pre-mRNA-splicing factor syf-2
- Pre-mRNA-splicing factor SYF1
- Cell division cycle 5-like protein
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor 8 homolog
- Pre-mRNA-splicing factor RBM22
- Tr-type G domain-containing protein
- Pleiotropic regulator 1
Sequence:
MARNAEKAMTALARWRRMKEEEERGPIARRPHDVKDCRNLSDAERFRREIVRDASKKITAIQNPGLGEFKLRDLNDEVNRLIKLKHAWEQRIRELGGTDYRKYAQKELDAIGRETGNSRGYKYFGAAKDLPGVRELFEKSTEGEEQRRHRADLLRNIDAHYFGYLDDEDGRLIPLEKLIEEKNIERINKEFAEKQAQKQQTASDAAPENIYKVEEDDDDDLETQESTVIGEDGRPMTIRHVLLPTQQDIEEMLLEQKKQELMAKYLD
Protein: GTP-binding protein YPT32/YPT11 (Rab GTPase YPT32) (P51996)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for protein transport through the secretory pathway. Probably involved in regulation of secretory vesicle formation at the trans-Golgi compartment. Mediates the proper polarized localization of SEC2, a GEF for SEC4, but does not alter the exchange activity of SEC2 on SEC4. Plays a role in autophagy.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:9151665}; Lipid-anchor {ECO:0000269|PubMed:9151665}.
Interaction partners:
- Rab guanine nucleotide exchange factor SEC2
- GTPase-activating protein GYP1
- Vacuolar morphogenesis protein 6
- Myosin-2
- GTP-binding protein YPT31/YPT8
- Trafficking protein particle complex II-specific subunit 130
- Trafficking protein particle complex II-specific subunit 120
- Phosphatidylinositol 4-kinase PIK1
- Trafficking protein particle complex subunit BET3
- Trafficking protein particle complex subunit BET5
Sequence:
MSNEDYGYDYDYLFKIVLIGDSGVGKSNLLSRFTTDEFNIESKSTIGVEFATRTIEVENKKIKAQIWDTAGQERYRAITSAYYRGAVGALIVYDISKSSSYENCNHWLTELRENADDNVAVGLIGNKSDLAHLRAVPTDEAKNFAMENQMLFTETSALNSDNVDKAFRELIVAIFQMVSKHQVDLSGSGTNNMGSNGAPKGPTISLTPAPKEDKKKKSSNCC
Protein: Serine/threonine-protein kinase MPS1 (EC 2.7.12.2) (Monopolar spindle protein 1) (Regulatory cell proliferation kinase 1) (P54199)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the regulation of the onset of mitosis. Involved in a pathway that coordinates cell proliferation and differentiation. Implicated in spindle pole body (SPD) duplication. Dual specificity kinase that can phosphorylate serine, threonine and tyrosine residues. Phosphorylates the SPC29 and SPC110 spindle pole body components.
Interaction partners:
- Mitotic spindle checkpoint component MAD2
- Spindle assembly checkpoint serine/threonine-protein kinase BUB1
- Spindle assembly checkpoint component MAD1
- Spindle assembly checkpoint component MAD3
- Spindle assembly checkpoint protein BUB3
- Kinetochore protein NDC80
- Kinetochore protein NUF2
- Mitotic check point protein BUB2
- Mitotic check point protein BFA1
- Kinesin-like protein CIN8
Sequence:
MSTNSFHDYVDLKSRTNTRQFSDDEEFTTPPKLSNFGSALLSHTEKTSASEILSSHNNDKIANRLEEMDRSSSRSHPPPSMGNLTSGHTSTSSHSTLFGRYLRNNHQTSMTTMNTSDIEINVGNSLDKSFERIRNLRQNMKEDITAKYAERRSKRFLISNRTTKLGPAKRAMTLTNIFDEDVPNSPNQPINARETVELPLEDSHQTNFKETKRNTDYDSIDFGDLNPIQYIKKHNLPTSDLPLISQIYFDKQREENRQAALRKHSSRELLYKSRSSSSSLSSNNLLANKDNSITSNNGSQPRRKVSTGSSSSKSSIEIRRALKENIDTSNNSNFNSPIHKIYKGISRNKDSDSEKREVLRNISINANHADNLLQQENKRLKRSLDDAITNENINSKNLEVFYHRPAPKPPVTKKVEIVEPAKSASLSNNRNIITVNDSQYEKIELLGRGGSSRVYKVKGSGNRVYALKRVSFDAFDDSSIDGFKGEIELLEKLKDQKRVIQLLDYEMGDGLLYLIMECGDHDLSQILNQRSGMPLDFNFVRFYTKEMLLCIKVVHDAGIVHSDLKPANFVLVKGILKIIDFGIANAVPEHTVNIYRETQIGTPNYMAPEALVAMNYTQNSENQHEGNKWKVGRPSDMWSCGCIIYQMIYGKPPYGSFQGQNRLLAIMNPDVKIPFPEHTSNNEKIPKSAIELMKACLYRNPDKRWTVDKVLSSTFLQPFMISGSIMEDLIRNAVRYGSEKPHISQDDLNDVVDTVLRKFADYKI
Protein: ShKT domain-containing protein (Q9GYJ3)
Organism: Caenorhabditis elegans
Interaction partners:
- Helix-loop-helix protein 6
- ShKT domain-containing protein
- Ubiquitin-like domain-containing protein
- Prion-like-
- Nuclear Hormone Receptor family
- EB domain-containing protein
- Flo11 domain-containing protein
Sequence:
MFRQFIISFAIFSVAFACEASESEGPCDGGILVCQTQVCDVAAGQCCPITTAAAVTSTTAAVVTDSDGSTVTTTASSVTVTSTSTTTCADRVNPSTGVSDCSALAYLCNDSTYYTVMTQQCPRTCGRCNSTSTSSTSCVDRVNPSTGVSDCPARAALCNDSNYYTLMTTQCPRTCGRCSTSSSTTSSSTTCADRVNPTTGVSDCPARASLCNNSVYYDIMTTQCPRTCGRCTSSSTISATSSASTTVSSTCVDQVNAATGTSDCPNRRAFCTNSAYISLMRTQCPLTCGFCTAG
Protein: asparagine--tRNA ligase (EC 6.1.1.22) (Q8I408)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- asparagine--tRNA ligase
- Glutamyl-tRNA
- Glutamyl-tRNA
- Proline--tRNA ligase, putative
- Proline--tRNA ligase
- Isoleucine--tRNA ligase, putative
- isoleucine--tRNA ligase
- leucine--tRNA ligase
- leucine--tRNA ligase
- tRNA import protein tRIP
Sequence:
MRIYFITLIYFFTLLFLLTKCIKNKNRNKISNISCTYNLSRIRNRPVLTTGTKRRKLRNNFFFLNNYRKMISLCNKIDIKKRFLLPKLQGKYNLYCTTKNVERTRIKDLFKMDIKEAQHKNFKICGWIKSVRTVGKSYFVFVDINDGSYYKNLQVIIDDKIPDYEYILKTSTDDAIECFGELKGSIGKKQNVELCVYDISKNHYIKLFKQMNQDTVEEKEKINDSGNEKDNHNFNSNGHVNNYNDSNNNNNNNNNNYNNNNHVNNYHDSNNINDNIIFTKNSSGHINEDNKTKGAKHNKEDYYVISKKYHTKQYLRNYPHLRARTKLYSSLFRLKSDIIFETFNFLKKKKNYTYINTPILTSNDCEGAGKLFYATTLFDQQIKNEQREEDHMKKGITNEIAGNIKEKCYYQNEHLEYISRHKSISKMEGFDEMLLKNVSSNDCISPNNTESYNTRFENDFFKKACYLNVSSQLSLECLCCSIGDVFTLNPSFRAENSNTFRHLSEFLMLEVELAFSNLKDIIDISEEYIKEMITYALYKSEDVNYLNEYHDKDLKNKLENILNKKFVLITYDEAINILKKENVFYDFQWGKDFSFEEQKYLATNYFKAPVVIINYPTHIKPFYMKLNEDEKTVSCMDIIFPDVGEVVGGSEREINLKNLKKQMENKKLNMKLYDPYIQLRKHGNIPHAGFGIGMDRLIMFLSSINNIRDVVTFPRYPGSLFM