wanglab/gogpt-training-data huggingface dataset:
Protein: Dachshund homolog dac-1 (H2KY91)
Organism: Caenorhabditis elegans
Function: Transcription factor (By similarity). Plays a role in the thermotactic response.
Subcellular location: Nucleus {ECO:0000269|PubMed:15620651}.
Interaction partners:
- Protein phosphatase eya-1
- Homeobox protein ceh-33
- Homeobox protein ceh-34
Sequence:
MQELSQLGGYFQKLAAGGFVINPSSSSSSSNNSSSNTSSSNFLSPYEYQESSTSPRDTTDSSGESSLSSSGSSSSLNGSCNVAAKLIKFRGHNVAAFDINGKEMICLPQVYEVFLKNMVGGLHTVYTKLKRLYIHPMVCNVEQVRALRSLGAIQPGVNRCKLLKTSDFEKLYDDCTSTCTRPGRPSKRSFDDWNNGAVIIKKDKTDSEPVNGPVFNQLMQPQMTPQQILMQHFVALSQKTKNSFERADDDDQNQRDADDITPLNLSKSGGNSENDSDSLENMRKEDSSPNTSVSDRGGSNSNSLSMSMEAGSSSSSGKNDEASMMNKVMSLIELASQQFKHEREELWKERSEIQVLRESFHKIVQEERDLRKKLETQNKKCTAFEKRYKYVKKQLLLANADLRRYKEKEEQSSDGNSVEL
Protein: Zinc finger protein 111 (Zinc finger protein ZFP111) (Q9R164)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MCLPSQEAVTFRDVAVVFSEEELGLLDAAQRKLYHDVMLENFRNLLAVGGQSPNKMEIVDATGLRCLSLGQLLCWGETSHNINKLARALEAVINTQGKCSHSLEQCHSSCHRVSEEPPRDSEDSSSPDLTNDHSSITENQEFLSGRAQGSWGKRRLRKRQNHQKNCLQTLMKNKPQLLAQHSPVHSTQEDTRHSFSVPVQESIYPGRKRYRCQECGKAFRQSSALQTHQRVHTGEKPYRGNSRGKNFSRSSDLNIHRQVHTREKPYTCKVCKKRFMQCSLLQAHKRIHTGEKPYKCGDCGKRFSCISNFHIHQRVHTKSKPSKCDYGKPFNLRCNFHSHQRVHTGEKPYKCEECGKGFTSASSFQRHQRVHTGEKPFVCSVCGKGFSRTSYLQTHQRVHSGDKPYQCDSCGKGFTQLSHLQAHERIHTDQKPYKCGDCGKRFSCSSNLHTHQRVHTGEKPYKCEECGKGFSLVSGLQAHQRVETGKKPFKCNACQKRFSQAWNLHAHQRVHTGEKPYKCDTCGKAFGQRSGLQIHQRIHTGEKPFKCEECGKEFSLNSGLIAHRRVHTGEKPYECKDCGKGFSLASSLRTHQRVHTGEKPFQCNECQKRFSQVSHLQSHQRVHTGEKPYKCDRCGKAFSQKSGLQVHKRIHTGEKPFKCEECGKEFIWSSGLSAHRKVHTGEKPYRRRQYGKGLIRPHTSD
Protein: Neuronal membrane glycoprotein M6-a (Q8UUT1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGCSECCLKCLSGIPYASLIATILLYAGVALFCGCGHEALSGTVTILQTYFDVVRSPVDALDVFTMIDIFKYVIYGVAAAFFVYGILLMVEGFFTTGAIRDLYGDFKITTCGRCVSAWFIMLTYIFMLAWLGVTAFTSLPVFMYFNIWNTCQNMTLLEGSLSSANSANLCFDLRQYGIVSIGEEKRLCADNENFKKMCESNELDLTFHLFVCALAGAGAAVIAMVHYLMVLSANWAYVKDACRMQKYEDIKSKEEQELHDIHSTRSKERLNAYT
Protein: Minor histocompatibility protein HB-1 [Cleaved into: Minor histocompatibility antigen HB-1 (mHag HB-1)] (O97980)
Organism: Homo sapiens (Human)
Function: Precursor of the histocomplatibility antigen HB-1. More generally, minor histocomplatibility antigens (mHags) refer to immunogenic peptide which, when complexed with MHC, can generate an immune response after recognition by specific T-cells. The peptides are derived from polymorphic intracellular proteins, which are cleaved by normal pathways of antigen processing. The binding of these peptides to MHC class I or class II molecules and its expression on the cell surface can stimulate T-cell responses and thereby trigger graft rejection or graft-versus-host disease (GVHD) after hematopoietic stem cell transplantation from HLA-identical sibling donor. GVHD is a frequent complication after bone marrow transplantation (BMT), due to mismatch of minor histocomplatibility antigen in HLA-matched sibling marrow transplants. HB-1 is presented on the cell surface by MHC class I HLA-B44. This complex specifically elicits donor-cytotoxic T lymphocyte (CTL) reactivity in B-cell acute lymphoblastic leukemia (B-ALL) after treatment by HLA-identical allogenic bone marrow transplantation (BMT). It induces cell recognition and lysis by CTL. However, HB-1 restricted expression in B-ALL cells and not in normal tissues may allow a specific CTL reactivity against B-ALL without the risk of evoking graft-versus-host disease.
Interaction partners:
Sequence:
MEEQPECREEKRGSLHVWKSELVEVEDDVYLRHSSSLTYRL
Protein: E3 ubiquitin-protein ligase pep5 (EC 2.3.2.27) (Carboxypeptidase Y-deficient protein 5) (Histone E3 ligase pep5) (RING-type E3 ubiquitin transferase pep5) (Vacuolar protein sorting-associated protein 11) (Q9P6N4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for vacuolar biogenesis and for trafficking of hydrolase precursors to the vacuole. Mediates transport at the vacuolar membrane where it may be responsible for tethering transport vesicles on the target membranes. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase ypt7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion. Acts as component of the CORVET complex that is required for transport between endosome and vacuole. CORVET is an effector for the endosomal Rab GTPase ypt5. Probable ubiquitin-protein ligase involved in the degradation-related ubiquitination of histones. Contributes to the post-translational regulation of histone protein levels by polyubiquitination of excess histones for subsequent degradation.
Subcellular location: Vacuole membrane {ECO:0000250|UniProtKB:P12868}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12868}; Cytoplasmic side {ECO:0000250|UniProtKB:P12868}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable vacuolar protein sorting-associated protein 16 homolog
- Vacuolar membrane protein pep3
- Vacuolar protein sorting-associated protein 33
- Vacuolar protein sorting-associated protein 8
- Vacuolar morphogenesis protein 6
- Vacuolar protein sorting-associated protein 41
- Vacuolar protein sorting-associated protein 3
- Ypt/Rab-type GTPase ypt7
- Syntaxin pep12
- Vesicle transport v-SNARE protein vti1
Sequence:
MSTFIKNWKRITLFQVKAIEENIDRLTSSFSSNGELVVFATAFGDVSIYNSSFKSLQSIKVEDESSIQQILWLDNKTFLLFSNVEGGTGTNSTVIIYAFSQADENEPPQFVLVTTHKFSINESPYPIIAVSQSPIDKTIACGFGGGLVSCYHGNPLRERGIKNSYSHNLGEPITGLTYLDDQSSVLFIATTNKTYSLSGKSLSCLDNTGVSLNCSSSCKTTPLQSREKNSSSFVCTRSSGLTFYDSKREKICFTFPGEKHYMTVMGSILALCYTPTLGTDSSTNEGLKKSFSSSSSIRKADASRNPAFPPRLLLVDLSRNLIVWEGHLKDVAVSILPLKHGFLVVTADDNVFELKRITLQEEISLLCQKMMYNLAISLAKKENMDIEFRESLMRDYASFLFRRGDFSASMDWYIRSIKSIDIPSVCLEFLKAQEIKQLIRLLEELIKTGLATSDHRLLLLSCYVEIHDSPSIRKLIDIGEIDFDQAFKICYDSNLLDEAKHLAIRFNNNERVLDVLVESEQYSEALRFFESLPPSNLLPLLLKYGRVLLDKLPEKTTNIFIQFYSNSHRGDLSTSESKGELKTAKSLRQTYLSLLPYAQVANFSLPPSLYEISPSQEENQRAALFSEDVSYTAPSPQTCFHIFLNHNSELISFLEGILPNASPNYKTLINTCLFEAYIRESFASSNVEKQEFWQEKSNSLLKKVEKNVDLNAVFLISQILGFDDGVRFVQGKSGQTLDIFRSFCQQNDIERALKMVRVHGPDQQELYIMMLNCFASLENVDSWYQDINEIVNIIVSQRLISPTQLLDILGKSVNIKLEHISDSMQSVLDNYRESISKQNEAIEMGKRDIEEITSQLSILRTRAFVVQESKCSTCGIDLELPMVHFRCGHSYHQRCVEDECIRCRWL
Protein: Histone-lysine N-methyltransferase SETMAR (SET domain and mariner transposase fusion protein) (Metnase) [Includes: Histone-lysine N-methyltransferase (EC 2.1.1.357); Transposon Hsmar1 transposase (EC 3.1.-.-)] (Q53H47)
Organism: Homo sapiens (Human)
Function: Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double-strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Has also kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity. In parallel, has a histone methyltransferase activity and methylates 'Lys-4' and 'Lys-36' of histone H3. Specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining. Also regulates replication fork processing, promoting replication fork restart and regulating DNA decatenation through stimulation of the topoisomerase activity of TOP2A.
Subcellular location: Nucleus {ECO:0000269|PubMed:18263876}. Chromosome {ECO:0000269|PubMed:18790802, ECO:0000269|PubMed:22231448}. Note=Recruited on damaged DNA at sites of double-strand breaks. {ECO:0000269|PubMed:18263876}.
Interaction partners:
- Pre-mRNA-processing factor 19
- Protein BANP
- Calmodulin-lysine N-methyltransferase
- Histone H3.3
- Histone H3.1
- Histone H3.2
- Histone H3.1t
- Histone H3-7
- Histone H3.3C
- Actin-histidine N-methyltransferase
Sequence:
MFAEAAKTTRPCGMAEFKEKPEAPTEQLDVACGQENLPVGAWPPGAAPAPFQYTPDHVVGPGADIDPTQITFPGCICVKTPCLPGTCSCLRHGENYDDNSCLRDIGSGGKYAEPVFECNVLCRCSDHCRNRVVQKGLQFHFQVFKTHKKGWGLRTLEFIPKGRFVCEYAGEVLGFSEVQRRIHLQTKSDSNYIIAIREHVYNGQVMETFVDPTYIGNIGRFLNHSCEPNLLMIPVRIDSMVPKLALFAAKDIVPEEELSYDYSGRYLNLTVSEDKERLDHGKLRKPCYCGAKSCTAFLPFDSSLYCPVEKSNISCGNEKEPSMCGSAPSVFPSCKRLTLETMKMMLDKKQIRAIFLFEFKMGRKAAETTRNINNAFGPGTANERTVQWWFKKFCKGDESLEDEERSGRPSEVDNDQLRAIIEADPLTTTREVAEELNVNHSTVVRHLKQIGKVKKLDKWVPHELTENQKNRRFEVSSSLILRNHNEPFLDRIVTCDEKWILYDNRRRSAQWLDQEEAPKHFPKPILHPKKVMVTIWWSAAGLIHYSFLNPGETITSEKYAQEIDEMNQKLQRLQLALVNRKGPILLHDNARPHVAQPTLQKLNELGYEVLPHPPYSPDLLPTNYHVFKHLNNFLQGKRFHNQQDAENAFQEFVESQSTDFYATGINQLISRWQKCVDCNGSYFD
Protein: Flavin-dependent halogenase armH2 (EC 1.14.19.-) (G3FLZ8)
Organism: Armillaria mellea (Honey mushroom) (Agaricus melleus)
Function: Flavin-dependent halogenase involved in the biosynthesis of melleolides, a range of antifungal and phytotoxic polyketide derivatives composed of an orsellinic acid (OA) moiety esterified to various sesquiterpene alcohols. The halogenase catalyzes the transfer of a single chlorine atom to the melleolide backbone, resulting in a 6'-chloromelleolide product. The enzyme acts on free substrate and does not depend on carrier-protein-dependent acceptor molecules.
Interaction partners:
Sequence:
MVTQVPSSTNILVIGGGPAGAYAAGVLVREGFEVTLLEKDFFPRYHIGESMLPSWRQFLRFIDMEEKMKNYGFLPKPGGAIKLNQDKREGYTDFIANNPENSAWNVVRSEFDQLLLNHVAEQGVKVYEGTRVDEIHFSPEEPTRPVSLTWSKDDKTRGDISFNWLVDASGRNGLMSTKYLKNRTFNRSLKNVAVWGYWTGTNRYAPGTNRENAPWFEALTDETGWVWFIPLHDGTTNVGVVLVEEDSKRKKAEYRAKHEGKSLAEVQYDRYMEDIQLAPGLIGLLGDGKFDGKLQAAGDYSYHASGYAGPHFRIAGDAGAFIDPFFSSGIHLAFTGGLSAACTIAASIRGHCTEEEASEFHSSKIKTAFTRFLFVVLGIYKQLRAQQSQILYEADEESLDRAILSLRPVIQGAADADADLTKEELENTLDFCKSVLEDEPQANGNGAAKQDAVPAPIPVALSSGAGPEKDAKRREIEAESLRSLQEMDDCKRNFGTEVINGFFVKMEQGVLGLVRA
Protein: CCN family member 4 (WNT1-inducible-signaling pathway protein 1) (WISP-1) (Wnt-1-induced secreted protein) (O95388)
Organism: Homo sapiens (Human)
Function: Downstream regulator in the Wnt/Frizzled-signaling pathway. Associated with cell survival. Attenuates p53-mediated apoptosis in response to DNA damage through activation of AKT kinase. Up-regulates the anti-apoptotic Bcl-X(L) protein. Adheres to skin and melanoma fibroblasts. In vitro binding to skin fibroblasts occurs through the proteoglycans, decorin and biglycan.
Subcellular location: Secreted.
Interaction partners:
- Biglycan
- Protein NDRG1
- Proto-oncogene Wnt-1
- Decorin
Sequence:
MRWFLPWTLAAVTAAAASTVLATALSPAPTTMDFTPAPLEDTSSRPQFCKWPCECPPSPPRCPLGVSLITDGCECCKMCAQQLGDNCTEAAICDPHRGLYCDYSGDRPRYAIGVCAQVVGVGCVLDGVRYNNGQSFQPNCKYNCTCIDGAVGCTPLCLRVRPPRLWCPHPRRVSIPGHCCEQWVCEDDAKRPRKTAPRDTGAFDAVGEVEAWHRNCIAYTSPWSPCSTSCGLGVSTRISNVNAQCWPEQESRLCNLRPCDVDIHTLIKAGKKCLAVYQPEASMNFTLAGCISTRSYQPKYCGVCMDNRCCIPYKSKTIDVSFQCPDGLGFSRQVLWINACFCNLSCRNPNDIFADLESYPDFSEIAN
Protein: Protein SIEL (Protein SHORT-ROOT INTERACTING EMBRYONIC LETHAL) (Q8VZA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Intracellular shuttle that promotes movement of SHR from the stele into the endodermis. Required for SHR association to endosomes and localization, and for intercellular movement of SHR.
Subcellular location: Nucleus {ECO:0000269|PubMed:21924907}. Endosome {ECO:0000269|PubMed:21924907, ECO:0000269|PubMed:23294290}. Cytoplasm, cell cortex {ECO:0000269|PubMed:23294290}. Note=Intact microtubules promote the localization to endosomes and the cell cortex. {ECO:0000269|PubMed:23294290}.
Interaction partners:
- Embryo defective 2739
- Cleavage and polyadenylation specificity factor subunit 3-II
- ARM repeat superfamily protein
- Integrator complex subunit
- Cleavage and polyadenylation specificity factor subunit 3-I
- DNA-directed RNA polymerase II subunit 4
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA cross-link repair protein SNM1
- Cleavage and polyadenylation specificity factor subunit 2
- DNA-directed RNA polymerases II, IV and V subunit 6A
Sequence:
MTSSMEEDDSISPESISLDTLASIRSLIINADTSDSVISSVFDFLTGLLSRGNSAILHHVLKLLSDLAFRRKELAPQIFDSILSNLLRLHNTVAEASHERAAVESLAVLASLSERTPSIAAALSKIDDEVFASICLGAPISSRLWLLRNADRFNVPSSVLFTLFLGFSKDPYPYIRKVALDGLINICNAGDFNHTHAVEGCYTRAVELLSDAEDSVRSSAVRAVSVWGKVMIASKEEEMNRRDCTDAVFLQLCSVVRDMSVDVRVEVFKAFGIIGTASESIILQTLSKKVLGAGKGKKPQNLLSNGSADVSSAAGVYIHGFEDEFYEVREAAVDSFHSLSVNSIKFPDEAVYLLMDMLYDDYMVVRLKALKALHHIADLGNLKIQETYMPAFLDAIVDTSENIRVEARNILKLAKLPDLKLVNKCIDGVLKSLEMYPQDEPDILSALFHFGQNHTNFLVSMVKRFSEKLGTASGSKAEFNSRQLSASLTLIISAPLSNKQSITSIPPLAFSYSLAMLGKFSSGLHDMMDQDMLLAYLTHCAILSSSSGTEFNKGDVFFHAYRDSNADLAGNPVLLPGKDIPAESKYMACKAELEIGNQALKFVNHILLKIKAAWLLSQSGCSKEALRALRACKQELATLTADSSISKGTLDFICQYVHVIELLVQVWPHFNYSRHISTCSSVEVELLMEEVEIKLMEIRCRFTGLSTEESLVLELVIFGCLLRLYKFEICCRLSCMEKLSSTISQLELHHEQQCTKPSDFLTETKKSLEEFGSSDDINSCRLLDLIKIFKCFSPEQFTFSVNLQCVSAEVEVPGNGPYSPISFVPGLPVAIPCEITLLNVPRDTCLWLRISRNDETCQFVYLDPNLYNGNGREKRFMFTAVTYMTPRAVVFTLRVSIGIECLFEDICYRKQRHGPKHPVAYLCKEREIHLSLVSRT
Protein: Beta-1,3-N-acetylglucosaminyltransferase manic fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) (O09008)
Organism: Mus musculus (Mouse)
Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 4
- Neurogenic locus notch homolog protein 3
- Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe
- Beta-1,3-N-acetylglucosaminyltransferase radical fringe
- GDP-fucose protein O-fucosyltransferase 1
Sequence:
MHCRLFRGMAGALFTLLCVGLLSLRYHSSLSQRMIQGALRLNQRNPGPLELQLGDIFIAVKTTWAFHRSRLDLLLDTWVSRIRQQTFIFTDSPDERLQERLGPHLVVTNCSAEHSHPALSCKMAAEFDAFLVSGLRWFCHVDDDNYVNPKALLQLLKTFPQDRDVYVGKPSLNRPIHASELQSKNRTKLVRFWFATGGAGFCINRQLALKMVPWASGSHFVDTSALIRLPDDCTVGYIIECKLGGRLQPSPLFHSHLETLQLLGAAQLPEQVTLSYGVFEGKLNVIKLPGPFSHEEDPSRFRSLHCLLYPDTPWCPLLAAP
Protein: Mannan endo-1,4-beta-mannosidase 2 (EC 3.2.1.78) (Beta-mannanase 2) (Endo-beta-1,4-mannanase 2) (AtMAN2) (Q7Y223)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- At1g75700
- Bifunctional fucokinase/GDP-fucose pyrophosphorylase
- PLATZ transcription factor family protein
- Putative pectinesterase/pectinesterase inhibitor 43
- At1g21000/F9H16_1
- DEAD-box ATP-dependent RNA helicase 40
- Transcription initiation factor IIF subunit alpha
- Putative pectinesterase/pectinesterase inhibitor 45
Sequence:
MAAPTGNGPVIPILGFLTCVAFIYLSFGDLWFGLKTEGELAFVKRNGTQFVVDGKALYVNGWNSYWFMDHAVNDHSRHRVSAMLEAGAKMGLTVCRTWAFNDGGYNALQISPGRFDERVFKALDHVIAEAKTHGVRLLLSLVNNLQAYGGKTQYVNWAWQEGVGLSSSNDSFFFDPSIRRYFKNYLTVLLTRKNSLTGIEYRNDPTIFAWELINEPRCMSDVSGDTLQDWINEMTAFIKSIDNKHLLTVGLEGFYGPSSPKKLTVNPERWASELGSDFVRNSDSPNIDFASVHIYPDHWFHDQGFEEKLKFVVKWMLSHIEDGDKELKKPVLFTEFGLSNLNKDYDPSQRDRFYRTIFDVIYKSAKRKRSGAGTLVWQFLIEGMEGFNDDFGIVPWEQDSIQRLMIEQSCRLSRITGRHLLDKKSIEMCSHRP
Protein: Extragenic suppressor of kinetochore protein 1 (O74511)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:12773390}. Note=Associated with chromatin.
Interaction partners:
- Serine/threonine-protein phosphatase ppe1
Sequence:
MFWRLGQGFGFQSSSAIEAILDKPEDEINLKELLEENGVLDECKSHNPKLLEYLCKPEVLSQLIDYILEVDETEIPSADGGYEEPEHTRLSYIASEILSSDVWSICEACVENKTLMVKLWSFLDSEGPLNPLQASYFAKVNEHFLDKKTEETVAFIQSIDNFVEKILRHAETSAIMDLLLKFISMDRCNTAIGIADWLYSQGLIQSLLRLLSPYVDPDVQFTVADVIKAIIAISANSNEPGVIGPNSLSRELVSRQTITTLTDYMTDSKAPHSATSLINGVSIVIELIRKNNSDYDVTPVLQMPLDTHPPTTRDPIYLGTMLRLFAEKIPVFQKILLKPSTESDLMPTSFGKIKPLGFERFRICELYAELLHCSNMSLLSDPNGEAMVMQRDHLRDYLFRHNSCARDLVMSDEDDDDSTFSDKNSKDFKETEDMNGAEDMHGRAPQITKDNLNLTTTDSPMSEAEPVSEEEYKDVMETAKALHHGDDDAASDTSYEPLPESVIEDAKKLPVIGDFLKIEFIQNNVIPTILDHFFDYPWNNFLHNVVYDVVQQVLNAPMDKDQNYALAVDMFKQGKITEKIVYGQELNDKKVAKPSGFRAGYMGHLTIIADEVVKFVEHYSSTFDQELLNLINDEKWQNFVNKTLVETRNRDNQLLGGLEPSMVGYLEDMDEGEMLDANNLPEMQFALEQELESNSSDDDVVEVHRELSHNSSSNDEDDGNDEDPLSREMSRRLSFESANDSDQDNRDHFAQYMSQQISDNNANQFSSSDEDDDDDDEVVEWVSRGNENKYPRSNFFINGSDREDFSDSEEEDGNDSSDDDRGFAEEEYSDGLVLNHGK
Protein: P-type Cu(+) transporter (EC 7.2.2.8) (G5EE14)
Organism: Caenorhabditis elegans
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004166}. Membrane {ECO:0000256|RuleBase:RU362081}.
Interaction partners:
- Copper transport protein ATOX1
- Multicopper oxidase
- Copper homeostasis protein cutC homolog
- Cytochrome c oxidase subunit 1
- Yip1 domain-containing protein
- Mitochondrial chaperone BCS1
- Nuclear hormone receptor family member nhr-115
- Probable delta-1-pyrroline-5-carboxylate synthase
- BED-type domain-containing protein
Sequence:
MSENVSLLDGSPLPSRPSTSSIPRPSPSKNIQLLVDFGAPKTDGNVQETMLEIKGMTCNSCVKNIQDVIGAKPGIHSIQVNLKEENAKCSFDTTKWTAEKVAEAVDDMGFDCKVLKKEPPTQMAEKPKIRRAIVSIEGMTCHACVNNIQDTVGSKDGIVKIVVSLEQKQGTVDYNSEKWNGESVAESIDDMGFDCKLITDQEIAAVEPQKASTTKLSISPLKTVDLSDGKVELQLNGVKYSKEGSSDHLEKCTFAVEGMTCASCVQYIERNISKIEGVHSIVVALIAAKAEVIYDGRVTSSDAIREHMTGELGYKATLLDSMGANPNYSKIRLIIGNLSTESDANRIESHVLSKSGIDSCNVSIATSMALVEFSPQVIGPRDIINVVESLGFTADLATRDDQMKRLDHSDDVKKWRNTFFIALIFGVPVMIIMIIFHWILRTPMHPDKQTPIFTPALSLDNFLLLCLCTPVQIFGGRYFYVASWKAIKHGNANMDVLIMLSTTIAYTYSIVVLLLAIIFKWPSSPMTFFDVPPMLIVFIALGRMLEHKAKGKTSEALSKLMSLQAKEATLVTMDSEGRLTSEKGINIELVQRNDLIKVVPGAKVPVDGVVVDGKSSVDESFITGESMPVVKKPGSTVIGGSVNQKGVLIVKATHVGNDSTLSQIVRLVEEAQTNRAPIQQLADKIAGYFVPFVIVLSLFTLGVWIYIEYNSARNANLPPGLRFEEALKIAFEAAITVLAIACPCSLGLATPTAVMVGTGVGAANGILIKGGEPLESVHKVTTIVFDKTGTITEGRPRVVQIASFVNPSTMSLKLITFLSGATEALSEHPIGNAVAAFAKQLLNEPTWPNTSRFHVSAGHGVTCRIDSIRQSFSSLALSGSTCEIPRLPDGQTITIPGTEVNLLQVSSKEVSQPNPDTANIVIGTERMMERHGIPVSEVVKMTLSEEQRKGHISVICAINAEVVAVISIADQVKKEASLAIYTLREMGLRVVLLTGDNSKTAESTAKQVGIDEVFAEVLPNQKQQKIKQLKGYKNKVAMVGDGVNDSPALAEANVGIAIAAGSDVAIESAGIVLVRNDLVDVVGAIKLSKMTTRRIRLNFLFAIIYNAIGIPIAAGVFRPFGFMLQPWMAAAAMALSSVSVVSSSLLLKNFRKPTIANLYTTSFKRHQKFLESGSFQVQVHRGLDDSAVFRGAASSKLSILSSKVGSLLGSTTSIVSSGSSKKQRLLDNVGSDLEDLIV
Protein: Fructose-bisphosphate aldolase, chloroplastic (EC 4.1.2.13) (P16096)
Organism: Spinacia oleracea (Spinach)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MASASLLKTSPVLDNPEFLKGQTLRIPSVAGVRFTPSGSSSLTVRASSYADELVKTAKTVASPGRGILAMDESNATCGKRLASIGLENTEANRQAYRTLLISAPGLGQYVSGAILFEETLYQSTTDGKKMVDVLIEQGIVPGIKVDKGWLPLPGSNDESWCQGLDGLACRSAAYYQQGARFAKWRTVVSIPNGPSALAVKEAAWGLARYAAITQDNGLDPILEPEIMLDGEHGIDRTFRVAQQVWAEVFFNLAENNVLLEGSSLKPSMVGPGALSARKGPPEQVADYPLKLLHRRRGPVVPGIMVLSGGQSEVEATLNLNAMNQSPNPWHVSFSYARALQNTCLKTWVEGQENVKAQDFACAKSNSLAQLGKYTGEGESEERKKDMFVKATLTY
Protein: Uncharacterized protein (Q4FKF6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- NADH dehydrogenase subunit NI8M
- Uncharacterized protein
- Adrenodoxin reductase, putative
- NB-ARC domain-containing protein
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase complex I subunit
- NADH-ubiquinone oxidoreductase complex I subunit
Sequence:
MVRYAKRPWYSPLGFMSHSPQSYAPLLMVVGVTATFPLRYKISDYFERQRDGPHVELRRKAVLYYNEVERMHRRQALQNQANVKDDDSSHRISSTLQAEALRLGHMDQEYNYWHAHQRDALRAEKLLAEVRELQERLNSAQMEQLAEA
Protein: S-phase kinase-associated protein 1 (Cyclin-A/CDK2-associated protein p19) (S-phase kinase-associated protein 1A) (p19A) (p19skp1) (Q6PEC4)
Organism: Rattus norvegicus (Rat)
Function: Essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription. In the SCF complex, serves as an adapter that links the F-box protein to CUL1. The functional specificity of the SCF complex depends on the F-box protein as substrate recognition component. SCF(BTRC) and SCF(FBXW11) direct ubiquitination of CTNNB1 and participate in Wnt signaling. SCF(FBXW11) directs ubiquitination of phosphorylated NFKBIA. SCF(BTRC) directs ubiquitination of NFKBIB, NFKBIE, ATF4, SMAD3, SMAD4, CDC25A, FBXO5, CEP68 and probably NFKB2. SCF(SKP2) directs ubiquitination of phosphorylated CDKN1B/p27kip and is involved in regulation of G1/S transition. SCF(SKP2) directs ubiquitination of ORC1, CDT1, RBL2, ELF4, CDKN1A, RAG2, FOXO1A, and probably MYC and TAL1. SCF(FBXW7) directs ubiquitination of cyclin E, NOTCH1 released notch intracellular domain (NICD), and probably PSEN1. SCF(FBXW2) directs ubiquitination of GCM1. SCF(FBXO32) directs ubiquitination of MYOD1. SCF(FBXO7) directs ubiquitination of BIRC2 and DLGAP5. SCF(FBXO33) directs ubiquitination of YBX1. SCF(FBXO11) directs ubiquitination of BCL6 and DTL but does not seem to direct ubiquitination of TP53. SCF(BTRC) mediates the ubiquitination of NFKBIA at 'Lys-21' and 'Lys-22'; the degradation frees the associated NFKB1-RELA dimer to translocate into the nucleus and to activate transcription. SCF(CCNF) directs ubiquitination of CCP110. SCF(FBXL3) and SCF(FBXL21) direct ubiquitination of CRY1 and CRY2. SCF(FBXO9) directs ubiquitination of TTI1 and TELO2. SCF(FBXO10) direct ubiquitination of BCL2.
Interaction partners:
- E3 ubiquitin-protein ligase RBX1
- Beta-transducin repeat containing E3 ubiquitin protein ligase
- S-phase kinase-associated protein 2
- Cullin-1
- F-box/WD repeat-containing protein 7
- F-box/WD repeat-containing protein 8
- Cullin-7
- F-box and leucine-rich repeat protein 3
- F-box/LRR-repeat protein 5
- F-box and WD repeat domain containing 11
Sequence:
MPTIKLQSSDGEIFEVDVEIAKQSVTIKTMLEDLGMDDEGDDDPVPLPNVNAAILKKVIQWCTHHKDDPPPPEDDENKEKRTDDIPVWDQEFLKVDQGTLFELILAANYLDIKGLLDVTCKTVANMIKGKTPEEIRKTFNIKNDFTEEEEAQVRKENQWCEEK
Protein: Neuroendocrine secretory protein 55 (NESP55) [Cleaved into: LHAL tetrapeptide; GPIPIRRH peptide] (Q9Z0F1)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Secreted {ECO:0000250}. Note=Neuroendocrine secretory granules. {ECO:0000250}.
Interaction partners:
Sequence:
MDRRSRAQQWRRARHNYNDLCPPIGRRAATALLWLSCSIALLRALASSNARAQQRAAQRRSFLNAHHRSAAAAAAAQVLPESSESESDHEHEEVEPELARPECLEYDQDDYETETDSETEPESDIESETEIETEPETEPETAPTTEPETEPEDERGPRGATFNQSLTQRLHALKLQSADASPRRAQPTTQEPESASEGEEPQRGPLDQDPRDPEEEPEERKEENRQPRRCKTRRPARRRDQSPESPPRKGPIPIRRH
Protein: Aquaporin TIP2-3 (Tonoplast intrinsic protein 2-3) (AtTIP2;3) (Q9FGL2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transports methylammonium or ammonium in yeast cells, preferentially at high medium pH. May participate in vacuolar compartmentation and detoxification of ammonium.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:15665250}; Multi-pass membrane protein {ECO:0000269|PubMed:15665250}. Note=Tonoplast.
Interaction partners:
- Probable aquaporin SIP1-2
- Probable aquaporin SIP2-1
- Protein kinase superfamily protein
- Aquaporin SIP1-1
- NAC domain-containing protein 91
- Protein S-acyltransferase 24
Sequence:
MVKIEVGSVGDSFSVSSLKAYLSEFIATLLFVFAGVGSAVAFAKLTSDGALDPAGLVAIAIAHAFALFVGVSIAANISGGHLNPAVTLGLAIGGNITLITGFFYWIAQCLGSIVACLLLVFVTNGKSVPTHGVSAGLGAVEGVVMEIVVTFALVYTVYATAADPKKGSLGTIAPIAIGFIVGANILAAGPFSGGSMNPARSFGPAVVSGDLSQIWIYWVGPLVGGALAGLIYGDVFIGSYEAVETREIRV