wanglab/gogpt-training-data huggingface dataset:
Protein: L-gulonolactone oxidase 3 (AtGulLO3) (EC 1.1.3.8) (Q9LYD8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidation of L-gulono-1,4-lactone to ascorbic acid. L-gulono-1,4-lactone is oxidized to hydrogen peroxide and L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate (By similarity).
Subcellular location: Vacuole {ECO:0000305|PubMed:23738689}.
Interaction partners:
- L-galactono-1,4-lactone dehydrogenase, mitochondrial
- L-galactose dehydrogenase
- Monodehydroascorbate reductase 3
- GDP-mannose 3,5-epimerase
- Glutathione S-transferase DHAR2
- Putative F-box protein At1g65770
- GDP-L-galactose phosphorylase 1
- Ubiquitin carboxyl-terminal hydrolase 25
- Phosphomannomutase
- Glutathione S-transferase DHAR1, mitochondrial
Sequence:
MRYSHTLQQFSILSFFVTIWTVQSVPPQPPIRCDQTGCTVSNAYGTWPDRKTCHAANVTYPTTEEDLRKAVAYAAEHNLKVKTVTKFSHTIPKLACPSGSDALLISTSKYNSVIEIEPELLTVTADSGVSLRELIEKVEGAGFSIGTSPYWEGVSIGGLISTGSHGSSWSGRGGSVHDHVVGISLVVPANQSEGFAKVVRLEEGRDDTLLNAVKVSLGVLGVISKVKLSIEKAFKRSVTYNFTSDVALEDIFMEHGKKYEFGDITWYPSRKTAVYRYDIRAPVNVSGNGVNDFLGFQSNPILISKGVRALEKGFESSKNENGKCTTADTTLAYKKLIGNGLKNSGLIFTGYPVIGRQGKIQTSGSCLYSSSIRIDVACAWDPRYNGLFFYETTAIFPVSRFRDFLLDVKKLRDMKPERLCGIDIYNGIFIRFIKGSKAYLGQTEDSVVIDFNYYRADDELTPRLNQDVMEEMEQMAFVKHGAKPHWGKNRKVGFFGVKQKIGPNFDKFLEVKNKLDPKKMFSSEWSDEILLGTEASKYDGCALEGNCVCSEERHCNPSKGYFCKEGLVYTQARVCRFSPAQVIVM
Protein: Capsid protein (ORF2) (Q2V8W4)
Organism: Norovirus (isolate Mouse/NoV/United States/MNV1/2002/GV) (MNV-1) (Murine Norovirus 1)
Subcellular location: Host cytoplasm {ECO:0000256|ARBA:ARBA00004192}. Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MRMSDGAAPKANGSEASGQDLVPAAVEQAVPIQPVAGAALAAPAAGQINQIDPWIFQNFVQCPLGEFSISPRNTPGEILFDLALGPGLNPYLAHLSAMYTGWVGNMEVQLVLAGNAFTAGKVVVALVPPYFPKGSLTTAQITCFPHVMCDVRTLEPIQLPLLDVRRVLWHATQDQEESMRLVCMLYTPLRTNSPGDESFVVSGRLLSKPAADFNFVYLTPPIERTIYRMVDLPVIQPRLCTHARWPAPVYGLLVDPSLPSNPQWQNGRVHVDGTLLGTTPISGSWVSCFAAEAAYEFQSGTGEVATFTLIEQDGSAYVPGDRAAPLGYPDFSGQLEIEVQTETTKTGDKLKVTTFEMILGPTTNADQAPYQGRVFASVTAAASLDLVDGRVRAVPRSIYGFQDTIPEYNDGLLVPLAPPIGPFLPGEVLLRFRTYMRQIDTADAAAEAIDCALPQEFVSWFASNAFTVQSEALLLRYRNTLTGQLLFECKLYNEGYIALSYSGSGPLTFPTDGIFEVVSWVPRLYQLASVGSLATGRMLKQ
Protein: Uncharacterized protein Rv1289 (P9WM37)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable periplasmic iron-transport lipoprotein
Sequence:
MCVSVGESVAQSLQQWDRKLWDVAMLHACNAVDETGRKRYPTLGVGTRFRTALRDSLDIYGVMATPGVDLEKTRFPVGVRSDLLPDKRPDIADVLYGIHRWLHGHADESSVEFEVSPYVNASAALRIANDGKIQLPKSAILGLLAVAVFAPENKGEVIPPDYQLSWYDHVFFISVWWGWQDHFREIVNVDRASLVALDFGDLWNGWTPVG
Protein: Uncharacterized protein (Q584D0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTNNHVENNCIAHFLRQSGSGEVTGRVHMLLLAATKRLTSDIRELNKEVRPPPEKLGALERTTRKIKEIVAAAFSTRPLDVVDSTEKHSRGVVDVLCHGSHVYSTALADSALDITVITNDNPRARYYWRSLRDNVESMETVESLLLLPVKGTEAAALQPYPASLPVTLPLLERTDMLQYLSTVISKSSLSRVSINRHSHNTFERICLGGAADEIGMNLTVNQRDSVEACGVLRQFLRSNEPVRHVIILMKVILKQLHIHSSQLTPYVLTLMVVAFSRHCANEYPLCGSFHYPHRRNMVESGYLLLSFLSFFSPPPRGLFTPTDMLIVPMHPDGIIKRSTCVPAPSPGECVNSWKVMDPICHNQNVAASCSAIDQCPLFFERILNRLLCGYLDASVLPLQHVDVELADGSNKWEANHCHWMNAFTGCGRPLFALLKAWRAHKKTDLS
Protein: Copine-4 (Copine IV) (Copine-8) (Q96A23)
Organism: Homo sapiens (Human)
Function: Probable calcium-dependent phospholipid-binding protein that may play a role in calcium-mediated intracellular processes.
Interaction partners:
Sequence:
MKKMSNIYESAANTLGIFNSPCLTKVELRVACKGISDRDALSKPDPCVILKMQSHGQWFEVDRTEVIRTCINPVYSKLFTVDFYFEEVQRLRFEVHDISSNHNGLKEADFLGGMECTLGQIVSQRKLSKSLLKHGNTAGKSSITVIAEELSGNDDYVELAFNARKLDDKDFFSKSDPFLEIFRMNDDATQQLVHRTEVVMNNLSPAWKSFKVSVNSLCSGDPDRRLKCIVWDWDSNGKHDFIGEFTSTFKEMRGAMEGKQVQWECINPKYKAKKKNYKNSGTVILNLCKIHKMHSFLDYIMGGCQIQFTVAIDFTASNGDPRNSCSLHYIHPYQPNEYLKALVAVGEICQDYDSDKMFPAFGFGARIPPEYTVSHDFAINFNEDNPECAGIQGVVEAYQSCLPKLQLYGPTNIAPIIQKVAKSASEETNTKEASQYFILLILTDGVITDMADTREAIVHASHLPMSVIIVGVGNADFSDMQMLDGDDGILRSPKGEPVLRDIVQFVPFRNFKHASPAALAKSVLAEVPNQVVDYYNGKGIKPKCSSEMYESSRTLAP
Protein: AP-1 complex subunit gamma-1 (Adaptor protein complex AP-1 subunit gamma-1) (Adaptor-related protein complex 1 subunit gamma-1) (Clathrin assembly protein complex 1 gamma-1 large chain) (Gamma1-adaptin) (Golgi adaptor HA1/AP1 adaptin subunit gamma-1) (O43747)
Organism: Homo sapiens (Human)
Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. In association with AFTPH/aftiphilin in the aftiphilin/p200/gamma-synergin complex, involved in the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:12773381}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:12773381}; Peripheral membrane protein {ECO:0000269|PubMed:12773381}; Cytoplasmic side {ECO:0000269|PubMed:12773381}. Cytoplasm {ECO:0000269|PubMed:15758025}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15758025, ECO:0000269|PubMed:34102099}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15758025}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:34102099}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex (PubMed:12773381). Co-localizes with AFTPH/aftiphilin in the cytoplasm (PubMed:15758025). {ECO:0000269|PubMed:12773381, ECO:0000269|PubMed:15758025}.
Interaction partners:
- AP-1 complex subunit beta-1
- AP-1 complex subunit sigma-3
- AP-1 complex subunit mu-1
- AP-1 complex subunit sigma-1A
- AP-1 complex subunit sigma-2
- AP-1 complex subunit mu-2
- ADP-ribosylation factor 1
- AP-2 complex subunit beta
- AP-2 complex subunit mu
- Clathrin heavy chain 1
Sequence:
MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADCASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCIGEYGDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQQRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPTEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPVIPTAPTSKPSSAGGELLDLLGDINLTGAPAAAPAPASVPQISQPPFLLDGLSSQPLFNDIAAGIPSITAYSKNGLKIEFTFERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKVLNPQKQQLRMRIKLTYNHKGSAMQDLAEVNNFPPQSWQ
Protein: Hydroxyacylglutathione hydrolase, mitochondrial (EC 3.1.2.6) (Glyoxalase II) (Glx II) (Round spermatid protein RSP29) (O35952)
Organism: Rattus norvegicus (Rat)
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Subcellular location: [Isoform 1]: Mitochondrion matrix {ECO:0000250|UniProtKB:Q16775}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250|UniProtKB:Q16775}.
Interaction partners:
- Lactoylglutathione lyase
- D-lactate dehydrogenase
- L-gulonolactone oxidase
Sequence:
MVLGRGSLCLRSLSVLGAACARRGLGQALLGLSLCHTDFRKNLTVQQDMMKIELLPALTDNYMYLIIDEDTQEAAVVDPVQPQKVIETVKKHRVKLTTVLTTHHHWDHAGGNEKLVKLEPGLKVYGGDDRIGALTHKVTHLSTLEVGSLSVKCLSTPCHTSGHICYFVSKPGSSEPSAVFTGDTLFVAGCGKFYEGTADEMYKALLEVLGRLPPDTKVICGHEYTVNNLKFARHVEPGNTAVQEKLAWAKEKNAIGEPTVPSTLAEEFTYNPFMRVKEKTVQQHAGETDPVTTMRAIRREKDQFKVPRD
Protein: COP9 signalosome complex subunit 5 (Signalosome subunit 5) (EC 3.4.-.-) (Q6PC30)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Probable protease subunit of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of E3 ligase complexes, leading to modify the Ubl ligase activity. In the complex, it probably acts as the catalytic center that mediates the cleavage of nedd8 from cullins. It however has no metalloprotease activity by itself and requires the other subunits of the CSN complex.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q92905}. Nucleus {ECO:0000250|UniProtKB:Q92905}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q92905}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q92905}.
Interaction partners:
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 2
- G protein pathway suppressor 1.
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 3
- COP9 constitutive photomorphogenic homolog subunit 7A
- Ubiquitin-like protein NEDD8
- E3 ubiquitin-protein ligase RBX1
- 26S proteasome non-ATPase regulatory subunit 12
- S-phase kinase-associated protein 1
Sequence:
MAGSSIAMKTWELSNSMQEVQSIDEIYKYDKKQQQEILAAKPWTKDHHYFKYCKLSALALLKMVMHARSGGNLEVMGLMLGKVDGETMIIMDSFALPVEGTETRVNAQAAAYEYMAAYIENAKQVGRLENAIGWYHSHPGYGCWLSGIDVSTQMLNQQFQEPFVAVVIDPTRTISAGKVNLGAFRTYPKGYKPPDEGPSEYQTIPLNKIEDFGVHCKQYYALEVSYFKSSLDRKLLELLWNKYWVNTLSSSSLLTNADYTTGQVFDLSEKLEQAEAQLGRGSFMLGLDTHDRKSEDKLAKATRDSCKTTIEAIHGLMSQVIKDKLFNQVNTSAN
Protein: Oviduct-specific glycoprotein (Estrogen-dependent oviduct protein) (Mucin-9) (Oviductal glycoprotein) (Oviductin) (Q12889)
Organism: Homo sapiens (Human)
Function: Binds to oocyte zona pellucida in vivo. May play a role in the fertilization process and/or early embryonic development.
Subcellular location: Cytoplasmic vesicle, secretory vesicle. Note=Secretory granules.
Interaction partners:
- Zona pellucida sperm-binding protein 3
- Zona pellucida sperm-binding protein 4
- Zona pellucida sperm-binding protein 1
- Zona pellucida sperm-binding protein 2
- Platelet glycoprotein VI
Sequence:
MWKLLLWVGLVLVLKHHDGAAHKLVCYFTNWAHSRPGPASILPHDLDPFLCTHLIFAFASMNNNQIVAKDLQDEKILYPEFNKLKERNRELKTLLSIGGWNFGTSRFTTMLSTFANREKFIASVISLLRTHDFDGLDLFFLYPGLRGSPMHDRWTFLFLIEELLFAFRKEALLTMRPRLLLSAAVSGVPHIVQTSYDVRFLGRLLDFINVLSYDLHGSWERFTGHNSPLFSLPEDPKSSAYAMNYWRKLGAPSEKLIMGIPTYGRTFRLLKASKNGLQARAIGPASPGKYTKQEGFLAYFEICSFVWGAKKHWIDYQYVPYANKGKEWVGYDNAISFSYKAWFIRREHFGGAMVWTLDMDDVRGTFCGTGPFPLVYVLNDILVRAEFSSTSLPQFWLSSAVNSSSTDPERLAVTTAWTTDSKILPPGGEAGVTEIHGKCENMTITPRGTTVTPTKETVSLGKHTVALGEKTEITGAMTMTSVGHQSMTPGEKALTPVGHQSVTTGQKTLTSVGYQSVTPGEKTLTPVGHQSVTPVSHQSVSPGGTTMTPVHFQTETLRQNTVAPRRKAVAREKVTVPSRNISVTPEGQTMPLRGENLTSEVGTHPRMGNLGLQMEAENRMMLSSSPVIQLPEQTPLAFDNRFVPIYGNHSSVNSVTPQTSPLSLKKEIPENSAVDEEA
Protein: Coiled coil domain containing 88A (A0A8I6A5W7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MENEIFTPLLEQFMTSPLVTWVKTFGPLAAGNGTNLDEYVALVDGVFLNQVMLQINPKTESQRVNKKVNNDASLRIHNLSILVKQIKFYYQDTLQQLIMMSLPNILVIGKNPFSEQGTEEVKKLLLLLLGCAVQCQKKEEFIEKIQGLDFDTKAAVAAHIQEVTHNQENVFDLQWMEVTDMSQEDTEPLLKSMASHLRRLIDERDEHSETIIELSEERDGVHFLPHASSSAQSPCGSPGMKRTESRQHLSVELADAKAKIRRLRQELEEKTEQLLDCKQELEQMEVELKRLQQENMNLLSDARSARMYRDELDALREKAVRVDKLESELCRYKERLHDIEFYKARVEELKEDNQVLLETKTMLEDQLEGTRARSDKLHELEKENLQLKAKLHDMEMERDMDRKKIEELMEENMTLEMAQKQSMDESLHLGWELEQISRTSELAEAPQKSLGHEVNELTSSKLLKLEMENQSLTKTVEELRSTMDSAEGSTSKILKVEKENQRLSKKVEILENEIIQEKQSLQNCQNLSKDLMKEKAQLEKTIETLRENSERQIKILEQENEHLNQTVSSLRQRSQISAEARVKDIEKENKILHESIKETSGKLSKIEFEKRQMKKELELYKEKGERAEELENELNRLGKENELLQKKITNLKITCEKLETLEQENSELERENRKFKKTLDSFKNLTFQLESLEKENSQLDEENLELRRSVESLKCASMKMAQLQLENKELESEKEQLKKGLELMKASFKKTERLEVSYQGLDTENQRLQKALENSNKKIQQLESELQDLEMENQTLQKNLEELKISSKRLEQLEKENKSLEQETSQLEKDKKQLEKENKRLRQQAEIKDTTLEENNVKIGNLEKENKTLFKEISVYKESCVRLKELEKENKELVKRATIDIKTLVTLREDLVSEKLKTQQMNNDLEKLTHELEKIGLNKERLLQDEQSTDDSRYKLLESKLESTLKKSLEIKEEKIAALEARLEESTNYNQQLRHELKTVKKNYEALKQRQDEERMVQSSLPISGEDDKWGRESQEATRELLKVKDRLIEVERNNATLQAEKQALKTQLKQLETQNNNLQAQILALQRQTVSLQEQNTTLQTQNAKLQVENSTLNSQSTSLMNQNAQLLIQQSSLENENESIMKEREDLKSLYDALIKDHEKLELLHERQASEYESLISKHGTLKSAHKNLEVEHKDLEDRYNQLLKQKGQLEDLEKMIKVEQEKMLLESKNHEMVAAEYKKLCGDNDRLNHTYSQLLKETEILQTDHKNLKSVLNNSKLEQTRLEAEFSKLKEQYQQLDITSTKLNNQCELLSQLKGNLEEENRHLLDQIQTLMLQNRTLLEQNMESKDLFHVEQRQYIDKLNELRRQKEKLEEKIMDQYKFYDPSPPRRRGNWITLKMRKLIKSKKDINRERQKSLTLTPTRSDSSEGFLQLPHQDSQDSSSVGSNSLEDGQTLGTKKSSMVALKRLPFLRNRPKDKDKMKACYRRSMSMNDLVQSMVLAGGQWTGSTENLEVPDDISTGKRRKELGAMAFSTTAINFSTVNSSAAFRSKQLVNNKDTTSFEDVSPQGISDDSSTGSRVHASRPASLDSGRTSTSNSNNNASLHEVKAGAANIQSRPQSHSSGDFSLLHDHETWSSSGSSPVQYLKRQTRSSPMLQHKMSETVDSQAHHKMNAGSPGSEVVTLQQFLEESNKLTSIQLKSSSQENLLDEVMKSLSVSSDFLGKDKPVSCTLARSVSGKAPGDFYDRRTAKPEFLRTGPQKTEDAYSISSAGKPTPSTQGKIKLVKETSVLRQSKDSNPYATLPRASSVISTAEGTTRRTSIHDFLSKDSRLPVSVEPAPPPAGGSSTAASNVNKVQESRNSKSRSREQQSS
Protein: DDT domain-containing protein DDR4 (A0A178UG69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MVTLRQRTMVVTGEPEQKKEEERLCEDLTILSSDSDNDSSSDSAVKHLRGRWELASVLNFFNVFGPLVSEKLKFTAEEIEMGLIESNTTNAQLHIALLKGIPPVNKTLDDANAWITVLCKKLAPWWPWIAKGEIHITVNKGEEISEYQGLDSINRLKILKALCELRVQQDDARSYIQENTKEGDWDSSLRKRKLGGDGKKTSYWFDGNDIQGYRLYREVNGISKKNAGSDLSCLSWETEATNLDEFQSVARELSSSKASSLAATGQMIETEAIPVVEKYHKKRERAIKKKMKEEMVVNVNFSRPLRTTRSCRNHMPATYTFDEYDKMISDAVEETEDTDGDEVEGRDQQSASLDSNDKSTEVEAAEIHNDDDKENEISKEDAEPKEEFGAKNRLRQRVTRNSAIC
Protein: Protein tesmin/TSO1-like CXC 4 (AtTCX4) (Q84JZ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in development of both male and female reproductive tissues.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Proline-rich spliceosome-associated
- Retinoblastoma-related protein 1
- Ras-related protein RABG3d
- F-box associated ubiquitination effector family protein
- Protein ALWAYS EARLY 3
- Protein ALWAYS EARLY 1
- Protein ALWAYS EARLY 2
Sequence:
MDTPDKNRISAVSFCNFEDSPVFQYINDLSPIEPVKPGRPENILHSLVFTSPSSSSSLFCSPQLNSYRDSRFFIKRHRSLDLSSPVVLIGETLKNSPDALWEEKLKCRPEKLENVSEPKPFKEQISLAIELANSLKHGRDGCDIQMVSCDEVPMDADDEIGSGGGSRELSDELCRQSFDPLDFDADSDGVLHTDEMEAESGFGKEVIMFDVADIQNYEQQIPRTTDPRFYSLASEPQQFSIYCNNSNYVEEREGSCSVQVAAGAPDINLSCSSKVAAIDSTAEAEDKEDKDLQPSGKQRSVRRRCLTFDMGGSHKRIPLRDSTNDLPLDSTSINKAPSPQNCLDTSKQDTDEILPIPRTIGLHLNGFVNPSVSSGRKKKKIKDGQAFPSTTFHYNIEDEFSTPVSTKRDLVVFSDVKIMEPPERSVEGECFDQLMAMENRQLSQGLDELGSCKRCKCRKSQCLKLYCECFSAGLFCGEPCSCQNCFNKPIHEDLVMKSREVIKARNPLAFAPKVVSTSDTVIDLWVENSKTPASARHKRGCNCRKSGCSKKYCECFMMGVGCSSNCRCMGCKNTFGHTNEQCAGDSDVVTINDEAKHYGDHGDASRQNEEILTSERNRLLLPGSVAFRSLTSLSNLSEL
Protein: Coactosin (Cyclic AMP-regulated protein p16) (Cytoskeletal protein p17) (P34121)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Binds to F-actin in a calcium independent manner. Binds to the filaments along their length.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Major actin
- Adenylyl cyclase-associated protein
Sequence:
MADVSSTELKAAYDEVLADSNDTNWCLFKYEGKNKIVLSGKGSGGFAELAQEINQPSERLYAYLRVVSGDDESKRSKFVFISWCGEEVGPLAKANVSVHKASVKQVIKNIGVEVHYTVADDLNEEELMTKVRKSSGADYSGNKSTN
Protein: Trans-3-hydroxy-L-proline dehydratase (EC 4.2.1.77) (Trans-L-3-hydroxyproline dehydratase) (Q96EM0)
Organism: Homo sapiens (Human)
Function: Catalyzes the dehydration of trans-3-hydroxy-L-proline to Delta(1)-pyrroline-2-carboxylate (Pyr2C). May be required to degrade trans-3-hydroxy-L-proline from the diet and originating from the degradation of proteins such as collagen-IV that contain it.
Interaction partners:
- D-amino-acid oxidase
- Ketimine reductase mu-crystallin
- Voltage-gated monoatomic cation channel TMEM109
- Pyrroline-5-carboxylate reductase 3
Sequence:
MESALAVPRLPPHDPGTPVLSVVDMHTGGEPLRIVLAGCPEVSGPTLLAKRRYMRQHLDHVRRRLMFEPRGHRDMYGAVLVPSELPDAHLGVLFLHNEGYSSMCGHAVLALGRFALDFGLVPAPPAGTREARVNIHCPCGLVTAFVACEDGRSHGPVRFHSVPAFVLATDLMVDVPGHGKVMVDIAYGGAFYAFVTAEKLGLDICSAKTRDLVDAASAVTEAVKAQFKINHPDSEDLAFLYGTILTDGKDAYTKEPTTNICVFADEQVDRSPTGSGVTARIALQYHKGLLELNQMRAFKSSATGSVFTGKAVREAKCGDFKAVIVEVSGQAHYTGTASFIIEDDDPLRDGFLLK
Protein: Zinc finger and BTB domain-containing 11 (Zinc finger and BTB domain-containing protein 11) (F1RAC1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSSEESYLAIQRYLTDEREPYAPGTHGNTKRKIRKAAACYIVRNGILYYQRRQKGLDEFTELEVVLTADRRKELITEAHITSGGEHLNQQQTWEIISQKYWWRGVLKQVKDCIKECIHCQTKQEKGRNNTEDAPKQTARQVRQKISSACASEEEDDEIHEDLEEEQSTTVDKHELVFVDSKGIVKQFLQKHGQTMLDKLNLQRMNNEFCDITLIIEGEEYRAHKAVLASCSDYFYELFVEKGAVSSHEAVVDLSGFSKASFLPLLDFAYTSNLTFNFCVMAEVATLARHLLMAEVLQICESVHKKVEEQKLMVYQRGDIHTVLPNQPASTQPITPTAAETYVVTMQSDGTAEAGQSLAVITSEIGTAESLALLAGATVDGETMTVVTHSGQAGSAESLAMVAHSGQAEEGETMTLVTHSGQAGSGESLAVVQACWSVEEPQVGDTPVVQSMQTGAFLISVDPGKTGASEIVHLAAAAPPAVQDEPQASKPIHQTEPPAAAPQPSPAPLKRRPGRPPKVKQQEPPPPLPSEDEPMEMEGVEDDEKQEDECIDPNKRYLRKRSVREGGYVRLHMGLETEEEEKITSPPAKIPQKGLAKRGRPVQSAKKNPETEFSETNLEAAPNAIVTSAKEPEPVIVEQPETVEEGALPGDPEGAVEGEHACNECGMVFQRRYTLIMHALKHEKARIFKCSICNKEFQYAASLRAHLARHKHQKSQRASLTRAMATEDSQGSDDQARFRTRREFVCDICGKTMPKLYSLRIHMLNHTGVRPHSCKVCGKSFATKHSLKMHRALHDSLKRFHCTVCEKSFVTKRSLEEHTSIHTGESKYLCTTCGASFHRASGLSKHLKKHQPKPEVRSFHCSHCDKSFFEAKDLQQHMNKHLGLKPFQCQVCGKCYSWKKDWYSHVKSHSVAEPFRCNVCGKEFFEKALFRRHVKKATHGKKGRVKQNLERECEHCGRKFTQLREYRRHMNNHQGVKPFECLTCGVAWADARSLKRHVRTHTGERPYVCPLCQEAHIDARTLRKHITKFHGDQLPGKIMLEKDTLQFHNQGTQVEHAVSILSSELPPELQPPQPPATEEIETVLITEETVEAVQAMNDGAAVTTLSDQSIMQVVNYVLAQQAAVKVEEAPEIIQTMEVEVAHVAEVE
Protein: Cell division cycle protein 27 homolog B (CDC27 homolog B) (Protein HOBBIT) (Q8LGU6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degradation of target proteins such as cyclins. The APC/C complex is required for the female gametophyte development and is involved in several aspect of development by controlling cell division and cell elongation. Involved in the control of endoreduplication. Functionally redundant with CDC27A in the control of gametophyte development.
Subcellular location: Nucleus {ECO:0000269|PubMed:17944809}.
Interaction partners:
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 7
- Anaphase-promoting complex subunit 1
- Cell division cycle 20.1, cofactor of APC complex
- Anaphase-promoting complex subunit 11
Sequence:
MEAMLVDCVNNSLRHFVYKNAIFMCERLCAEFPSEVNLQLLATSYLQNNQAYSAYHLLKGTQMAQSRYLFALSCFQMDLLNEAESALCPVNEPGAEIPNGAAGHYLLGLIYKYTDRRKNAAQQFKQSLTIDPLLWAAYEELCILGAAEEATAVFGETAALSIQKQYMQQLSTSLGLNTYNEERNSTSTKNTSSEDYSPRQSKHTQSHGLKDISGNFHSHGVNGGVSNMSFYNTPSPVAAQLSGIAPPPLFRNFQPAVANPNSLITDSSPKSTVNSTLQAPRRKFVDEGKLRKISGRLFSDSGPRRSSRLSADSGANINSSVATVSGNVNNASKYLGGSKLSSLALRSVTLRKGHSWANENMDEGVRGEPFDDSRPNTASTTGSMASNDQEDETMSIGGIAMSSQTITIGVSEILNLLRTLGEGCRLSYMYRCQEALDTYMKLPHKHYNTGWVLSQVGKAYFELIDYLEAEKAFRLARLASPYCLEGMDIYSTVLYHLKEDMKLSYLAQELISTDRLAPQSWCAMGNCYSLQKDHETALKNFLRAVQLNPRFAYAHTLCGHEYTTLEDFENGMKSYQNALRVDTRHYNAWYGLGMIYLRQEKLEFSEHHFRMAFLINPSSSVIMSYLGTSLHALKRSEEALEIMEQAIVADRKNPLPMYQKANILVCLERLDEALEVLEELKEYAPSESSVYALMGRIYKRRNMHDKAMLHFGLALDMKPPATDVAAIKAAMEKLHVPDEIDESP
Protein: EG:EG0003.2 protein (Fbgn0014870;psi protein) (O96828)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSDFQQQGGINQSQALAQAIQRAKQVSSHHLEEEEAEIAAKIQPSQPGGGTAGPSPPSSGGGPGFKRINDDGDSGPESKRSLGSPEYANNSSNMSSGSGGGGGGGGGPGGASITQAIAQAAAVAARLAASAGTSCEEQIRLPESVAGAFMGRSSNDTITHIQAESGVKVQVMQDQDRVIMLRGQRDTVTKGREMIQNMANRAGGGQVEVLLTINMPPPGPSGYPPYQEIMIPGAKVGLVIGKGGDTIKQLQEKTGAKMIIIQDGPNQELIKPLRISGEAQKIEHAKQMVLDLIAQKDAQGQQQGGRGGGGGGGGPGMGFNNFNNGNGGESTEVFVPKIAVGVVIGKGGDMIRKIQTECGCKLQFIQGKNDEMGDRRCVIQGTRQQVDDAKRTIDGLIENVMVSRKYFIKEANTLPMSDVIATKWHESKWQWRRRWPRRRLWQLQLRLWIVIGRGGETIKLINQQSGAHTEMDRNASNPPNEKLFKSKGTTDQVEAARQMISEKINMELNVISRKPIGGGPGGGGGNSGGGQNNSHHNQQQGGYGGQNQMQGGDPNSGAGYQQQPWGGPYGQQGWDPSGQQQQMAMANQGGSAAGGASGGQDYSAQWIEYYKQMGCHREAEMIEQQMKAKQAGGSSGPVQQQQPQQQQQSQQQTGGAGAGGADYSAQWAEYYRSVGKIEEAEAIEKTLKNKQQNGSGGQSSTPNPSQGGPGQQQPNPAAAAAAAAAAAAAAGGYGQSMTPTQYAQYSQYYAAAAAAGGQPQGAPQPGGGQSGGPPGNYPGNYPGAGYGGYPGAPGQQQQKSHKNDNH
Protein: 5830443L24Rik protein (Q66K09)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
ELLQKLETISEDQLDLKFREETNAFVSYIFNYAKIKTLKEGIKVTGNGLGILVTTYVDAINSGAVPCVDDAVTTLAQHENSVAVQRAADHYSEQMVQRLSLPTDTLQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNISTFSVPGGHRLYMDMREKIEHDYWQVPRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKEQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKNSGSIFDTIIREVASFIFSPISMIEKGIRSLF
Protein: Nuclear transcription factor Y subunit B-7 (AtNF-YB-7) (AtNF-YB7) (Q9SIT9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the NF-Y/HAP transcription factor complex (By similarity). The NF-Y complex stimulates the transcription of various genes by recognizing and binding to a CCAAT motif in promoters (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Nuclear transcription factor Y subunit C-1
- Nuclear transcription factor Y subunit C-2
- Nuclear transcription factor Y subunit A-1
- Nuclear transcription factor Y subunit C-9
- Nuclear transcription factor Y subunit A-2
- Nuclear transcription factor Y subunit C-7
- Nuclear transcription factor Y subunit A-3
- Nuclear transcription factor Y subunit A-5
- Nuclear transcription factor Y subunit A-9
- Nuclear transcription factor Y subunit A-10
Sequence:
MTEESPEEDHGSPGVAETNPGSPSSKTNNNNNNNKEQDRFLPIANVGRIMKKVLPGNGKISKDAKETVQECVSEFISFVTGEASDKCQREKRKTINGDDIIWAITTLGFEDYVAPLKVYLCKYRDTEGEKVNSPKQQQQRQQQQQIQQQNHHNYQFQEQDQNNNNMSCTSYISHHHPSPFLPVDHQPFPNIAFSPKSLQKQFPQQHDNNIDSIHW
Protein: Zinc finger family protein (Zinc finger-like protein) (Q9LX86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- HAT family dimerization domain-containing protein
- Ac-like transposase
- Uclacyanin-3
- RINT1-like protein MAG2
- RINT1-like protein MAG2L
Sequence:
MVAESDNRDLTVDTAASCLMLLSGIGEHDGRKKRVFRCKTCERDFDSFQALGGHRASHSKLTNSDDKSLPGSPKKKPKTTTTTTAHTCPICGLEFPMGQALGGHMRKHRNEKEREKASNVLVTHSFMPETTTVTTLKKSSSGKRVACLDFDLTSVESFVNTELELGRTMY
Protein: L-pipecolate oxidase (EC 1.5.3.7) (L-pipecolic acid oxidase) (O43029)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Oxidizes L-pipecolate and L-proline (6,7% of the activity for L-pipecolate).
Subcellular location: Secreted {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative glycine dehydrogenase
- Serine hydroxymethyltransferase, mitochondrial
- Probable serine hydroxymethyltransferase, cytosolic
- Probable low-specificity L-threonine aldolase
- D-amino-acid oxidase
- 5-aminolevulinate synthase, mitochondrial
Sequence:
MVKNTSVIIVGAGVFGLSAALELTKRGGYTIKILDRAPPPVIDGSSVDANRIIRSDYADAVYCSMGIDALEEWRTNPLFKEQFYGSGLMFVGRDNVEYRDMSLENLTKMGVSAAKFQTTEELRKLFPKWIGELNDGEAGYANFSSGWANAEQSVKSVVNYLAHAGVSFISGPEGTVEELITEENVVKGVRTTTGAYMAEKLIFATGAWTASLLPNDHTRFLATGQPVAYIKLTPEEYIRFLTNPVYLDFDTGFYIFPPTPDGYLKFARHGYGFTRMQNLKSGKVESVPPKKPLVSPILPKEAELDLRRNLQRTYGEEISQRPFYKTRICYYTDTADAEFVFDYHPDYENLFVCTGGSGHGFKFFPILGKYSIGCMFRELEEPLLKKWRWKKENLEFAALDHSRAGPSRQELS
Protein: Hydroperoxide resistance transcriptional regulator OhrR (Q8EI70)
Organism: Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1)
Interaction partners:
- Peroxiredoxin OhrA
- Glutathione peroxidase
- Transcriptional regulator of oxidative stress OxyR
- Thioredoxin
Sequence:
MPNTELSSAVNTLEKPENTLVDNVLCLENQVCFSLYSAANAMVRAYRPMLDKLDLTYPQYLVMLVLWQEQGISVKTLGDKLFLDSGTLTPLLKRLESKGLVSRGRSDQDERVRVLCLTPAGQALKREANEIPHLMRCKIGAELDDLKALKAMCDKALAQLHASID