wanglab/gogpt-training-data huggingface dataset:
Protein: Leukemia inhibitory factor receptor (LIF receptor) (LIF-R) (CD antigen CD118) (P42702)
Organism: Homo sapiens (Human)
Function: Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
Interaction partners:
- Leukemia inhibitory factor
- Oncostatin-M
- Ciliary neurotrophic factor receptor subunit alpha
- Ciliary neurotrophic factor
- Cardiotrophin-1
- Interleukin-6 receptor subunit beta
- Cardiotrophin-like cytokine factor 1
- Tyrosine-protein kinase JAK2
- Tyrosine-protein kinase JAK1
- Interleukin-6
Sequence:
MMDIYVCLKRPSWMVDNKRMRTASNFQWLLSTFILLYLMNQVNSQKKGAPHDLKCVTNNLQVWNCSWKAPSGTGRGTDYEVCIENRSRSCYQLEKTSIKIPALSHGDYEITINSLHDFGSSTSKFTLNEQNVSLIPDTPEILNLSADFSTSTLYLKWNDRGSVFPHRSNVIWEIKVLRKESMELVKLVTHNTTLNGKDTLHHWSWASDMPLECAIHFVEIRCYIDNLHFSGLEEWSDWSPVKNISWIPDSQTKVFPQDKVILVGSDITFCCVSQEKVLSALIGHTNCPLIHLDGENVAIKIRNISVSASSGTNVVFTTEDNIFGTVIFAGYPPDTPQQLNCETHDLKEIICSWNPGRVTALVGPRATSYTLVESFSGKYVRLKRAEAPTNESYQLLFQMLPNQEIYNFTLNAHNPLGRSQSTILVNITEKVYPHTPTSFKVKDINSTAVKLSWHLPGNFAKINFLCEIEIKKSNSVQEQRNVTIKGVENSSYLVALDKLNPYTLYTFRIRCSTETFWKWSKWSNKKQHLTTEASPSKGPDTWREWSSDGKNLIIYWKPLPINEANGKILSYNVSCSSDEETQSLSEIPDPQHKAEIRLDKNDYIISVVAKNSVGSSPPSKIASMEIPNDDLKIEQVVGMGKGILLTWHYDPNMTCDYVIKWCNSSRSEPCLMDWRKVPSNSTETVIESDEFRPGIRYNFFLYGCRNQGYQLLRSMIGYIEELAPIVAPNFTVEDTSADSILVKWEDIPVEELRGFLRGYLFYFGKGERDTSKMRVLESGRSDIKVKNITDISQKTLRIADLQGKTSYHLVLRAYTDGGVGPEKSMYVVTKENSVGLIIAILIPVAVAVIVGVVTSILCYRKREWIKETFYPDIPNPENCKALQFQKSVCEGSSALKTLEMNPCTPNNVEVLETRSAFPKIEDTEIISPVAERPEDRSDAEPENHVVVSYCPPIIEEEIPNPAADEAGGTAQVIYIDVQSMYQPQAKPEEEQENDPVGGAGYKPQMHLPINSTVEDIAAEEDLDKTAGYRPQANVNTWNLVSPDSPRSIDSNSEIVSFGSPCSINSRQFLIPPKDEDSPKSNGGGWSFTNFFQNKPND
Protein: Gamma-glutamyl hydrolase (EC 3.4.19.9) (Conjugase) (FGPH) (Folylpolyglutamate hydrolase) (GH) (Gamma-Glu-x carboxypeptidase) (Q9Z0L8)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates.
Subcellular location: Secreted, extracellular space {ECO:0000250|UniProtKB:Q92820}. Lysosome {ECO:0000250|UniProtKB:Q92820}. Melanosome {ECO:0000250|UniProtKB:Q92820}. Note=While its intracellular location is primarily the lysosome, most of the enzyme activity is secreted. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250|UniProtKB:Q92820}.
Interaction partners:
- Folylpolyglutamate synthase, mitochondrial
- Dihydrofolate reductase
- Lipid droplet-regulating VLDL assembly factor AUP1
- Reduced folate transporter
- SUMO-conjugating enzyme UBC9
Sequence:
MANLGYLLCLLGLLLCGLSSPGMSRPYNHGSERPIIGVVMQECFGKMAKLGNYYIAASYVKYIESAGARVVPIRPDLSDAEYEELFRSINGVLLPGGGANLTDSGYSRVAKIFFSKALESFDNGDHFPVWGTCLGFEELSVLVSGENLLTSTDTKSKKLPLNFTEGARKSRMFKHFPTELLDSLALENLTANFHKWSLSVKNFTENEKLKKFFNILTTNTDGKTEFISSMEGFKYPVYAVQWHPEKAAFEWKNLGGISHAPNAVKTSFYLAEFLVSEARKNSHHFENVVKETASLIYKFNPIYTGNISSFQQAYMFD
Protein: Homeobox protein caupolican (P54269)
Organism: Drosophila melanogaster (Fruit fly)
Function: Controls proneural and vein forming genes. Positive transcriptional controler of ac-sc (achaete-scute). May act as an activator that interacts with the transcriptional complex assembled on the ac and sc promoters and participates in transcription initiation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeobox protein araucan
- Homeobox protein slou
Sequence:
MAAYAQFGYAGYPTANQLTTANTDSQSGHGGGSPLSGTNEASLSPSGGSTATGLTAGPLSPGAVSQSSHHAGHKGLSTSPAEDVVGGDVPVGLSSAAQDLPSRGSCCENGRPIITDPVSGQTVCSCQYDPARLAIGGYSRMALPSGGVGVGVYGGPYPSNEQNPYPSIGVDNSAFYAPLSNPYGIKDTSPSTEMSAWTSASLQSTTGYYSYDPTLAAYGYGPNYDLAARRKNATRESTATLKAWLSEHKKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKMTWEPKNKTEDDDDGMMSDDEKEKDAGDGGKLSTEAFDPGNQLIKSELGKAEKEVDSSGDQKLDLDREPHNLVAMRGLAPYATPPGAHPMHAAYSSYAQSHNTHTHPHPQQMQHHQQQQQQQQNQQQLQHHQMDQPYYHPGGYGQEESGEFAAQKNPLSRDCGIPVPASKPKIWSVADTAACKTPPPTAAYLGQNFYPPSSADQQLPHQPLQQHQQQQLQQLQQQQQHHHHPHHHHPHHSMELGSPLSMMSSYAGGSPYSRIPTAYTEAMGMHLPSSSSSSSSTGKLPPTHIHPAPQRVGFPEIQPDTPPQTPPTMKLNSSGGSSSSSGSSHSSSMHSVTPVTVASMVNILYSNTDSGYGHGHSHGHGHGHGHGLGHGHGLGHGHGHMGVTSNAYLTEGGRSGS
Protein: Aldehyde dehydrogenase 1A1 (EC 1.2.1.19) (EC 1.2.1.28) (EC 1.2.1.3) (EC 1.2.1.36) (3-deoxyglucosone dehydrogenase) (ALDH-E1) (ALHDII) (Aldehyde dehydrogenase family 1 member A1) (Aldehyde dehydrogenase, cytosolic) (Retinal dehydrogenase 1) (RALDH 1) (RalDH1) (Q8MI17)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid. Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vitamin A into retinoic acid. This pathway is crucial to control the levels of retinol and retinoic acid, two important molecules which excess can be teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE, malonaldehyde and hexanal that form protein adducts and are highly cytotoxic. By participating for instance to the clearance of (E)-4-hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of HNE-protein adducts and lens opacification. Functions also downstream of fructosamine-3-kinase in the fructosamine degradation pathway by catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product of fructosamine 3-phosphate decomposition, which is itself a potent glycating agent that may react with lysine and arginine side-chains of proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase activity and is probably part of an alternative pathway for the biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a role in GABAergic synaptic transmission (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12941160}. Cell projection, axon {ECO:0000250|UniProtKB:P24549}.
Interaction partners:
- Retinol dehydrogenase 10
- CD44 antigen
- Hydroxysteroid dehydrogenase-like protein 2
- Cytochrome P450 26B1
- Delta-1-pyrroline-5-carboxylate synthase
- Cytochrome P450 26A1
- Homeobox protein NANOG
Sequence:
MADLPTPLTNLKIQYTKIFINNEWHDSVSGKKFPVLNPATEEQICLIEEGDKADVDKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESLNAGKLFPNAYLMDLGGCIKTLRYCAGWADKIQGRTMPMDGDFFCYTRHEPVGVCGQIIPWNFPLVMLIWKIGPALSCGNTVIVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVFADADLDNAVEFAHQGVFYHQGQCCIAASRLFVEESIYDEFVRRSVERAKKYVLGNPLAPEVNQGPQIDKEQYNKILDLIESGKKEGAKLECGGGPWGNKGYFIQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKRANNTTYGLSAGIFTKDLDKAVTVSSALQAGTVWVNCYSVVSAQVPFGGFKMSGNGRELGEYGLQQYTEVKTVTVKISQKNS
Protein: Zinc finger protein 282 (HTLV-I U5RE-binding protein 1) (HUB-1) (Q9UDV7)
Organism: Homo sapiens (Human)
Function: Binds to the U5 repressive element (U5RE) of the human T cell leukemia virus type I long terminal repeat. It recognizes the 5'-TCCACCCC-3' sequence as a core motif and exerts a strong repressive effect on HTLV-I LTR-mediated expression.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Zinc finger protein 212
- Zinc finger protein 398
- Bromo adjacent homology domain-containing 1 protein
- ELAV-like protein 1
- Transcription intermediary factor 1-beta
Sequence:
MQFVSTRPQPQQLGIQGLGLDSGSWSWAQALPPEEVCHQEPALRGEMAEGMPPMQAQEWDMDARRPMPFQFPPFPDRAPVFPDRMMREPQLPTAEISLWTVVAAIQAVERKVDAQASQLLNLEGRTGTAEKKLADCEKTAVEFGNHMESKWAVLGTLLQEYGLLQRRLENLENLLRNRNFWVLRLPPGSKGEAPKVPVTFVDIAVYFSEDEWKNLDEWQKELYNNLVKENYKTLMSLDAEGSVPKPDAPVQAEPREEPCVWEQRHPEEREIPMDPEAGAEPLVPAQDASSQVKREDTLCVRGQRGLEERAIPTESITDSPISAQDLLSRIKQEEHQCVWDQQDLADRDIPTDPNSESLISAHDILSWIKQEEQPYPWGPRDSMDGELGLDSGPSDSLLMVKNPPPAPPQPQPQPQPPQPQLQSQPQPQSLPPIAVAENPGGPPSRGLLDDGFQVLPGERGSGEAPPGGDRSTGGGGGDGGGGGGGAEAGTGAGGGCGSCCPGGLRRSLLLHGARSKPYSCPECGKSFGVRKSLIIHHRSHTKERPYECAECEKSFNCHSGLIRHQMTHRGERPYKCSECEKTYSRKEHLQNHQRLHTGERPFQCALCGKSFIRKQNLLKHQRIHTGERPYTCGECGKSFRYKESLKDHLRVHSGGPGPGAPRQLPPPPERD
Protein: Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein homolog) (GRP-78 homolog) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein) (HSP70 family protein) (Luminal-binding protein) (allergen Cor a 10.0101) (Q9FSY7)
Organism: Corylus avellana (European hazel) (Corylus maxima)
Function: Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q6Z7B0}.
Interaction partners:
Sequence:
MAGSWRARGSLVVLAILLFGCLFAISIAKEEATKLGTVIGIDLGTTYSCVGVYKNGHVEIIANDQGNRITPSWVGFTDGERLIGEAAKNQAAVNPERTIFDVKRLIGRKFEDKEVQKDMKLVPYKIVNKDGKPYIQVKIKDGETKVFSPEEISAMILIKMKETAEAFLGKKIKDAVVTVPAYFNDAQRQATKDAGIIAGLNVARIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLSTNGDTHLGGEDFDMRIMEYFIKLIKKKHGKDISKDNRAIGKLRREAERAKRALSSQHQVRVEIESLFDGVDFSEPLTRARFEELNNDFVQKDHGTREEAMEDAGLAKNQIDEIVLVGGSTRIPKVQQLLKDYFDGKEPNKGVNPDEAVAYGAAVQGSILSGEGGEETKDILLLDVAPLTLGIETVGGVMTKLIPRNTVIPTKKSQVFTTYQDQQTTVSIQVFEGERSLTKDCRNLGKFDLTGVPPAPRGTPQIEVTFEVDANGILNVKAEDKGTGKSEKITITNDKGRLSQEEIDRMVQEAEEFAEEDKKVKERIDARNTLETYVYNMKNQVNDKDKLADKLESDEKDKIESAVKDALEWLDDNQSAEKEDYDEKLKEVEAVCNPIITAVYQRSGGAPGGGSGEEDEDSESHDEL
Protein: Msb2p (A0A1D8PGF8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- SWR1-complex protein 4
- RuvB-like helicase 1
- Histone H2A.Z
- Vps72/YL1 C-terminal domain-containing protein
- High osmolarity signaling protein SHO1
- RuvB-like helicase 2
- HIT-type domain-containing protein
- Actin-like protein ARP6
- Chromatin modification-related protein EAF7
- SWR1-complex protein 5
Sequence:
MLANVKLNLVTALYVLSYVSVVNAYQQENEITPADNIDKRAGAIGNFFRDFTNSIFGNDNSEVNQPSTNGATSTGHFFGPSIPSTSTHQQTPGETSNNVNTKSSSQNQSPSTSPTSTVAAAAATSSSPVASTRPASTSEQKQQEETTARQSTSPATTATTSNTPPSPSTSKETPTSNTAQTSSANNNQQSSNTAAPSTSVIQPSTSEVHVQSQQTSTTPNTPTSSPNTPTTSEAAPTTSAAPTTSEAPVTPSTSEVVPNTPTTSKAPNTPTTSEAPVTPSTSEVVPNTPTTSKAPNTPTTSEAPATPTTSEAPNTPTTSEAPVTPTTSEVVPTTSTQGDAVSTSSTSVTEQTTLTSSTQLPPTTASTTQTSTPEASDSPKPSSTSIETPSTSTFEQDPTTTSSVGTPSSEQPQPTTTSESAVTSNSPTQESTSLVEPTTSSLESSNTPTPNPSTSEAQPSTSASQAPPDTTSSAPAPELSSSNADFSNSVLHSSETTSLVNPTDSQIDSSSTTDAVSQATTEPTSENTPTAASSVTANDINSAQSSAPTSNADAETASSPVSEQSLATGSQTSLDTTAGASSTASEATAENLSTFGTDGSSDASQTIAETTSNSPDQSVVTPSASASPDVSTLPTGSESGTSLVSGSETSIDTNTVASGSTVIPESSNIPTQSPSQSVVSSDAAASNVSTGSATTDSLAGSETGVQPISSSATGTSEPVFSSEYNSSEGTTSLVVPTNSELSSTVTGSSETAATAINSESVLTGSSDTAATVTGSESILTGNTETSATAIASESTLTGSTTGATDSAATTIASESVLTGTSDASATVIPSESALTGSTTTPIASESVLTGTTSADVSGATTIGSESIFTGTTESTGTPLPTASGTESLDTTVATGTSVSEQSGVETALSTQPTTGTEATVTSGVSQSEQTGTSAVTGVTESSEQIQSGATTPATTTASDATAVTNASEASAESQATTTAASEATTGSQVTTAASEAATESQATTAASEAATESQATTAASEAATESQATTPASEPATGSQVTSEVTPATVPSSVTAADTAATSIITSPPASAEPSSEVTAVAPSAATTSSTKNWLPSSLVIAETPSSNASKSTESIVQASATGASTSGLPRAITPETTTTPGFDYQVITVGFKSALNYPFVVENSISSAQIFQYLPRVLKYPFNGDKSLQNVSVRRLIPYTASNIDYTITVAEVYFPKDSVKALGSFITTPGSAIYRNPDSVLQALASLIDSRIPLTGLVTDDQQVSGSSSDSNPSTNSYGSMDIVSNTKVADKGRIAGITIGAAAGCGLYMTLMVLLFRKFRKSNKALELPITDSESNLGFSDEDSSMLESSSGFSAIFSRINHGGVLTGDPNGGGDDMMMMNNNNNNLRPNNISEPVQASNSLGWYH
Protein: LD30065p (Protein tyrosine phosphatase Meg2, isoform C (EC 3.1.3.-, EC 3.1.3.48)) (Q8IRM7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEAEQQEFAVKQFIDLCNNLGANCSTTTATSPSTSSSSASSTQNLIAVVPPQLQQLQVQLPAPGGGGGAGAGGGGGGGGGAAPVRRHISHTTAVKFLYARKFDIPRAVSLYEQHEQIRLKEYLYNIDPDVEPLRSELQTGKFTILPARTSSGAAIALFTANRHSPLSVSHTTTLQGIVYQLDSALQDSETQRAGLVFIYDMSGSKYSNFDYDLSQKILTLLKGGYPARLKKVLIVTAPLWFKAPFKILRLFVREKLRERVFTVSVPQLALHVPRKALPIHLGGTLEVDHATWLLSCRQSMTNREDELLANIVGVGGGSGSGSAAGSAAIVSTNGTETEAATTAATIISAVHQLGDNNTTVVTVSNGVGPAGSASGGATTAASAATEPNENITINGLSPSHRQAANNSSSSSSSAATVANPLKLNTSGSADNNSTITNATTAAGAAGAAAGTTTNGGGEFWSENPPSSASSGFSDDDSLAGQEGDPKPIDQIVQMVKQRGRHGLIKEYADIRNRAPEGTFLHARMRANLTKNRYTDVLCYDHSRVVLAHEDGDEPSDYINANFVDGYKQKNAYISTQGPLPKTSQDFWRMIWEQHCLVIVMTTRVMERGRVKCGQYWEPTEESSLEFGDYHVRTISVECNEDYMVASLELRNIKTDEIRNVSHWQFTSWPDYGVPSSAMAMLNFLQKVREKQAQLVQGLGDTWAGHPRGPPIVVHCSAGIGRTGTFITLDICISRLEDVGTADIRGTVEKIRSQRAYSIQMPDQYVFCHLALIEYAYSRGMLQTVDLAGFDEREPDSE
Protein: TPR domain protein (Q726A1)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- YkgJ family cysteine cluster protein
- Uncharacterized protein
- Chaperone protein HtpG
- Uncharacterized protein
- Alanine--tRNA ligase
- Chaperone protein DnaK
- Protein DsvD
- Nitrogen regulatory protein P-II
- DNA-directed RNA polymerase subunit alpha
Sequence:
MKARYEDLDEYIADLRAEIAQSENCANHHYNLGLALLSKRDFVAAEESFLNAVRNSPRLAEAYVQLGGICLQRGDLEGCLRYNEEAAQSRPKFPVAWSNIGFVHLQRGEPEKAIAALKKALKWQPDFIQAMATMGAAFYMEGDYEACINISNEAIKKEPSFGPAYNNLALAYFELGDFAKSVKFADLAMENGFEVRPEFLKELEAHR
Protein: Angiotensin-converting enzyme 2 (EC 3.4.17.23) (ACE-related carboxypeptidase) (EC 3.4.17.-) [Cleaved into: Processed angiotensin-converting enzyme 2] (Q8R0I0)
Organism: Mus musculus (Mouse)
Function: Essential counter-regulatory carboxypeptidase of the renin-angiotensin hormone system that is a critical regulator of blood volume, systemic vascular resistance, and thus cardiovascular homeostasis. Converts angiotensin I to angiotensin 1-9, a nine-amino acid peptide with anti-hypertrophic effects in cardiomyocytes, and angiotensin II to angiotensin 1-7, which then acts as a beneficial vasodilator and anti-proliferation agent, counterbalancing the actions of the vasoconstrictor angiotensin II. Also removes the C-terminal residue from three other vasoactive peptides, neurotensin, kinetensin, and des-Arg bradykinin, but is not active on bradykinin. Also cleaves other biological peptides, such as apelins, casomorphins and dynorphin A (By similarity). By cleavage of angiotensin II, may be an important regulator of heart function. By cleavage of angiotensin II, may also have a protective role in acute lung injury. Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19, regulating its trafficking on the cell surface and its activity.
Subcellular location: [Processed angiotensin-converting enzyme 2]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23535237}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:23535237}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9BYF1}. Apical cell membrane {ECO:0000250|UniProtKB:Q9BYF1}. Note=Detected in both cell membrane and cytoplasm in neurons. {ECO:0000269|PubMed:23535237}.
Interaction partners:
- Sodium-dependent neutral amino acid transporter B
- Dipeptidyl peptidase 4
- Transmembrane protease serine 2
- Angiotensinogen
- Sodium- and chloride-dependent transporter XTRP3A
- Proto-oncogene Mas
- Vitronectin
- Neprilysin
- Sodium- and chloride-dependent transporter XTRP3B
- Type-1 angiotensin II receptor A
Sequence:
MSSSSWLLLSLVAVTTAQSLTEENAKTFLNNFNQEAEDLSYQSSLASWNYNTNITEENAQKMSEAAAKWSAFYEEQSKTAQSFSLQEIQTPIIKRQLQALQQSGSSALSADKNKQLNTILNTMSTIYSTGKVCNPKNPQECLLLEPGLDEIMATSTDYNSRLWAWEGWRAEVGKQLRPLYEEYVVLKNEMARANNYNDYGDYWRGDYEAEGADGYNYNRNQLIEDVERTFAEIKPLYEHLHAYVRRKLMDTYPSYISPTGCLPAHLLGDMWGRFWTNLYPLTVPFAQKPNIDVTDAMMNQGWDAERIFQEAEKFFVSVGLPHMTQGFWANSMLTEPADGRKVVCHPTAWDLGHGDFRIKMCTKVTMDNFLTAHHEMGHIQYDMAYARQPFLLRNGANEGFHEAVGEIMSLSAATPKHLKSIGLLPSDFQEDSETEINFLLKQALTIVGTLPFTYMLEKWRWMVFRGEIPKEQWMKKWWEMKREIVGVVEPLPHDETYCDPASLFHVSNDYSFIRYYTRTIYQFQFQEALCQAAKYNGSLHKCDISNSTEAGQKLLKMLSLGNSEPWTKALENVVGARNMDVKPLLNYFQPLFDWLKEQNRNSFVGWNTEWSPYADQSIKVRISLKSALGANAYEWTNNEMFLFRSSVAYAMRKYFSIIKNQTVPFLEEDVRVSDLKPRVSFYFFVTSPQNVSDVIPRSEVEDAIRMSRGRINDVFGLNDNSLEFLGIHPTLEPPYQPPVTIWLIIFGVVMALVVVGIIILIVTGIKGRKKKNETKREENPYDSMDIGKGESNAGFQNSDDAQTSF
Protein: C-type lectin domain family 19 member A (Q6UXS0)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Synaptotagmin-17
Sequence:
MQRWTLWAAAFLTLHSAQAFPQTDISISPALPELPLPSLCPLFWMEFKGHCYRFFPLNKTWAEADLYCSEFSVGRKSAKLASIHSWEENVFVYDLVNSCVPGIPADVWTGLHDHRQEGQFEWTDGSSYDYSYWDGSQPDDGVHADPEEEDCVQIWYRPTSALRSWNDNTCSRKFPFVCKIPSLTIH
Protein: WW and C2 domain containing 1 (F1M6U0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Merlin
- non-specific serine/threonine protein kinase
- FERM domain-containing protein 6
- non-specific serine/threonine protein kinase
Sequence:
MPRPELPLPEGWEEARDFDGKVYYIDHRNRTTSWIDPRDRYTKPLTFADCISDELPLGWEEAYDPQVGDYFIDHNTKTTQIEDPRVQWRREQEHMLKDYLVVAQEALSAQKEIYQVKQQRLELAQQEYQQLHAVWEHKLGSQVSLVSGSSSSSKYDPEILKAEIATAKSRVNKLKREMVHLQHELQFKERGFQTLKKIDERMSDAQGGYKLDEAQAVLRETKAIKKAITCGEKEKQDLIKSLAMLKDGFRTDRGSHSDLWSSSSSLESSSFPVPKQFLDVSSQTDISGSFSTSSSNQLAEKVRLRLRYEEAKRRIANLKIQLAKLDSEAWPGVLDSERDRLILINEKEELLKEMRFISPRKWTQGEVEQLEMARRRLEKDLQAARDTQSKALTERLKLNSKRNQLVRELEEATRQVAALHSQLKSLSSSMQSLSSGSSPGSLTSSRGSLAASSLDSSTSASFTDLYYDPFEQLDSELPSKVELLFLEGATGFRPSGCITTIHEDEVAKTQKAEGGSRLQALRSLSGTPRSMTSLSPRSSLSSPSPPCSPLIADPLLAGDAFLTPLEFEDTELSPTLCELSLGTDGARERFRLEEPGPEGKPLGQAASVAPGCGLKVACVSAAVSDESVAGDSGVYEASMQRLGTSEAAAFDSDESEAVGVTQVQIALKYDEKSKQFAILVIQLSNLSALLLQQDQKVNIRVAILPCSESSTCLFRTRPLDSADSLVFNEAFWVSMSYPALHQKTLRVDVCTTDRSHTEECLGGAQISLAEVCRSGERSTRWYNLLSYKYLKKQGREPQPAEAPGPDHVDAVSALLEQTAVELEKRQEGRSSSQTLEGSWTYEEEASENEAVAEEEEREEEEGEEDVFAEKVSPEAEECPALKVDRETNTDSVTPSPTVVRPKDRRVGAPSPGPFLRGNTIIRSKTFSPGPQSQYVCRLNRSDSDSSTLSKKPPFVRNSLERRSVRMKRPSSVKSLRTERLIRTSLDLELDLQATRTWHSQLTQEISVLKELKEHLEQAKNHGEKELPQWLREDERFRLLLRMLEKRVDRGEHKSELQADKMMRAAAKDVHRLRGQSCKEPPEVQSFREKMAFFTRPRMNIPALSADDV
Protein: Cell division cycle protein 16 homolog (Anaphase-promoting complex subunit 6) (APC6) (Cyclosome subunit 6) (Q8R349)
Organism: Mus musculus (Mouse)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).
Interaction partners:
- Cell division cycle protein 23 homolog
- Anaphase-promoting complex subunit 5
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 2
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit CDC26
Sequence:
MNLEPLRKRVRQYLDQQQYQSALFWADKVASLSHEEPQDVYWLAQCLYLTAQYHRAAHALRSRKLDKLYEACRYLAARCHYAAKEHQQALDILDMEEPINRRLFEKYLKDDNGSRDPSSDWEMSQSSIKSSICLLRGKIYDALDNRTLATYSYKEALKLDVYCFEAFDLLTSHHMLTAQEEKELLDSLPLNKLCAEEQELLRFVFENKLKKYNKPSETVIPESVDGLQENLDVVVSLAERHYYNCDFKMCYKLTSTVMEKDPFHANCLPVHIGTLVELNKANELFYLSHKLVDLYPSNPVSWFAVGCYYLMVGHKNEHARRYLSKATTLEKTYGPAWIAYGHSFAVESEHDQAMAAYFTAAQLMKGCHLPMLYIGLEYGLTNNSKLAERFFGQALSIAPEDPFVIHEVGVVAFQNGEWKTAEKWFLDALEKIKAIGNEVTVDKWEPLLNNLGHVCRKLKKYAEALDYHRQALVLIPQNASTYSAIGYIHSLMGNFENAVDYFHTALGLRRDDTFSVTMLGHCIEMYIGDSEAYIGADIKDKLKCYDFDVHTMKTLKNIISPPWDFRDFEVEKQNTEEAGLAPLQNSTKAPESRPNLEETFEIEMNESDMMLETSMSDHST
Protein: Zinc phosphodiesterase ELAC protein 2 (EC 3.1.26.11) (ElaC homolog protein 2) (Ribonuclease Z 2) (tRNA 3 endonuclease 2) (tRNase Z 2) (A0A0S2Z5M8)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000256|ARBA:ARBA00004436}.
Interaction partners:
Sequence:
MWALCSLLRSAAGRTMSQGRTISQAPARRERPRKDPLRHLRTREKRGPSGCSGGPNTVYLQVVAAGSRDSGAALYVFSEFNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLSGMILTLKETGLPKCVLSGPPQLEKYLEAIKIFSGPLKGIELAVRPHSAPEYEDETMTVYQIPIHSEQRRGKHQPWQSPERPLSRLSPERSSDSESNENEPHLPHGVSQRRGVRDSSLVVAFICKLHLKRGNFLVLKAKEMGLPVGTAAIAPIIAAVKDGKSITHEGREILAEELCTPPDPGAAFVVVECPDESFIQPICENATFQRYQGKADAPVALVVHMAPASVLVDSRYQQWMERFGPDTQHLVLNENCASVHNLRSHKIQTQLNLIHPDIFPLLTSFRCKKEGPTLSVPMVQGECLLKYQLRPRREWQRDAIITCNPEEFIVEALQLPNFQQSVQEYRRSAQDGPAPAEKRSQYPEIIFLGTGSAIPMKIRNVSATLVNISPDTSLLLDCGEGTFGQLCRHYGDQVDRVLGTLAAVFVSHLHADHHTGLPSILLQRERALASLGKPLHPLLVVAPNQLKAWLQQYHNQCQEVLHHISMIPAKCLQEGAEISSPAVERLISSLLRTCDLEEFQTCLVRHCKHAFGCALVHTSGWKVVYSGDTMPCEALVRMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAISVGMRMNAEFIMLNHFSQRYAKVPLFSPNFSEKVGVAFDHMKVCFGDFPTMPKLIPPLKALFAGDIEEMEERREKRELRQVRAALLSRELAGGLEDGEPQQKRAHTEEPQAKKVRAQ
Protein: Lethal(3)malignant brain tumor-like protein 2 (H-l(3)mbt-like protein 2) (L(3)mbt-like protein 2) (Q969R5)
Organism: Homo sapiens (Human)
Function: Putative Polycomb group (PcG) protein. PcG proteins maintain the transcriptionally repressive state of genes, probably via a modification of chromatin, rendering it heritably changed in its expressibility. Its association with a chromatin-remodeling complex suggests that it may contribute to prevent expression of genes that trigger the cell into mitosis. Binds to monomethylated and dimethylated 'Lys-20' on histone H4. Binds histone H3 peptides that are monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Polycomb group RING finger protein 6
- Chromobox protein homolog 3
- Transcription factor E2F6
- WD repeat-containing protein 5
- YY1-associated factor 2
- E3 ubiquitin-protein ligase RING2
- RING1 and YY1-binding protein
- E3 ubiquitin-protein ligase RING1
- MAX gene-associated protein
- Transcription factor Dp-1
Sequence:
MEKPRSIEETPSSEPMEEEEDDDLELFGGYDSFRSYNSSVGSESSSYLEESSEAENEDREAGELPTSPLHLLSPGTPRSLDGSGSEPAVCEMCGIVGTREAFFSKTKRFCSVSCSRSYSSNSKKASILARLQGKPPTKKAKVLHKAAWSAKIGAFLHSQGTGQLADGTPTGQDALVLGFDWGKFLKDHSYKAAPVSCFKHVPLYDQWEDVMKGMKVEVLNSDAVLPSRVYWIASVIQTAGYRVLLRYEGFENDASHDFWCNLGTVDVHPIGWCAINSKILVPPRTIHAKFTDWKGYLMKRLVGSRTLPVDFHIKMVESMKYPFRQGMRLEVVDKSQVSRTRMAVVDTVIGGRLRLLYEDGDSDDDFWCHMWSPLIHPVGWSRRVGHGIKMSERRSDMAHHPTFRKIYCDAVPYLFKKVRAVYTEGGWFEEGMKLEAIDPLNLGNICVATVCKVLLDGYLMICVDGGPSTDGLDWFCYHASSHAIFPATFCQKNDIELTPPKGYEAQTFNWENYLEKTKSKAAPSRLFNMDCPNHGFKVGMKLEAVDLMEPRLICVATVKRVVHRLLSIHFDGWDSEYDQWVDCESPDIYPVGWCELTGYQLQPPVAAEPATPLKAKEATKKKKKQFGKKRKRIPPTKTRPLRQGSKKPLLEDDPQGARKISSEPVPGEIIAVRVKEEHLDVASPDKASSPELPVSVENIKQETDD
Protein: 26S proteasome non-ATPase regulatory subunit 13 (26S proteasome regulatory subunit RPN9) (26S proteasome regulatory subunit S11) (26S proteasome regulatory subunit p40.5) (Q22253)
Organism: Caenorhabditis elegans
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 8
- Probable 26S proteasome regulatory subunit 10B
- Probable 26S proteasome regulatory subunit 6B
- Probable 26S proteasome regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 7
Sequence:
MTAQDYLNGKLAAANGPLADDWKNLKELWEKKLWHQLTVLTRSLVKKPQFVASTDMHEFYRLFVAEWELRVNPLQLVEICISIAQNIATKDKQKSMEFLSKIGNVINKDKIAVARLHTGEIEARLENKDKNGQIIDLKSIRTQIDSTQHEVDSLVGVTEVHAPFYRVSSLYLREVGDFAGYYREALRYLGVEDANNLTTEQKQVHAVLLGFAALLGENVHNFGELLAHPILKSLEGTRERWIVDVLLAFNSGDLTRFFSLEGDWGGWDDLKKQKDFLTAKIRLMAVMELAVSRPTKARSVSFKEIATKCQIPFDEVEFLVMKALSKDLIRGDINQVEQVVYVTWVQPRVLDNPQIMQMATRISAWRNDVNSMEGIVSKEAREILTQN