wanglab/gogpt-training-data huggingface dataset:
Protein: Beta-alanyl-bioamine nonribosomal peptide synthetase (EC 6.3.2.-) (Nonribosomal peptide synthetase) (SmNRPS) (A0A3Q0KR05)
Organism: Schistosoma mansoni (Blood fluke)
Function: Catalyzes the condensation of beta-alanine with tryptamine to form beta-alanyl-tryptamine (BATT). Beta-alanyl-tryptamine is an essential pheromone produced by the male that stimulates female sexual development during pairing.
Interaction partners:
- Acyl carrier protein
- Acyl-CoA dehydrogenase
- Uncharacterized protein
- Protein-cysteine N-palmitoyltransferase HHAT
- Putative dna double-strand break repair rad50 ATPase
- Mediator of RNA polymerase II transcription subunit 27
- SMB domain-containing protein
- Putative ffa transport protein.
- Very long-chain fatty acid transport protein
- Uncharacterized protein.
Sequence:
MPQSTAQLKSPLLHTLLENLTQSSICTSTAIWHVPNPVNFVCNHNENSFDNKNNSVTTITTTDVSTNNHKNTNYDYEQQEQWSNEEINSNQESNEIYTMTFLKLNNAANRVAMNLANYLERKWSSITNKINRTQLNQHSLSIDEPIELRNQSDTVIALFMPPGIDRIVVQIACMKLHLAYMPLDRNVPAGRITQILHKLKPILILIDKDYYDFIYDDDHNDNDKMSDLSSSIDNNNKSLLSRKLSSNDFIIGNLNQLKLTFQLFDVKVYEYIKLMKLSKYYSRSDIYTASIPIRVCLFPFESDPIVLVLFTSGSTSSGPKPVKLRTTQLFNRLEWQWDSTSDMDLPNFENATCNSNTSVKRIGLAKTAWGFVDAFTELFSCLLAGIPVVVPGGSACPSEKSITDVQQLINLTKHFKISHITTVPTQMNLWLKQLRLKPKEIVTSHLSSLRTVIVSGDIVHPKMACEFFQLFKNPEMRLINLYGTTEVAGDVTGLVFRGEIDVKKHTKVVPCGLERENNKSGKPVLSVGTVIQGTAIFIVQDDDDHHLHHEKDNENQPDKWSNPSLSIIGSVDRKPNWDKFPFKILPKGHIGHVCILGQQVSDSASRCQRIESLPEDLNCVDTNKCKSDVESCENNSSKEIRVFMPGDLGFIDPQTNHLYICGRTNELIKINGIRFHANDIDNLFIELKKNWKAKNMTNCTREELLVNKVSETVTLTIQTVHGRDLKLVCFYVLHMNENQNTMNIEPKENYDKLEDLPKQDDFIAVFSHYLPPYLSPTFINIDHIPLMRTSGKVDKEYLRQYYYSKHHCEISEITKVLQPGWVNDPVKHMTENNNSTSDQSFGKNSRDFKLSRGRERARKVLAEVLGIRGPNGDVIPGRPKDDEDFYLLGGDSLLTVLTTEQLRQLGFNVNLDVFTKTGKIGSILTSLQNTESDFLKTQEPFTSDSWTVKEISMNKVLKKSHTCNLINRIPLMEDECYLSPTICPQGSYEIFIEQWNDGNFSVTERHEIVDVLVNAFIEKDRLSHALKLDRTDLTEAIEVFLNAHKSNPGIVLTARYYYENPYEHTFVKNKLVGVIISLPAKHVPSLHLTPKLALVQRFFDECSNKDQFQDISMDNLLATQMVAITSQSPYSKSKYLQYMLSNWKKISLKLLTRLERDLLRIAAKQGYSGVITFNTNEVTEEVCSQLGYKVIQTTMLKSFMNKENLLLLPQYERIRCSYMIKELNPSS
Protein: Possible conserved transmembrane protein (O53731)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Amine oxidase domain-containing protein
- DUF1365 domain-containing protein
- Tuberculostearic acid methyltransferase UfaA1
- ECF RNA polymerase sigma factor SigK
Sequence:
MVTSVSALAVAVVHSVAFAIGRRIGRYNVVDVVWGLGFVAVAVAAATLGHGDPVRRWLLLALVSTWGLRLSWHMYRKTAGQGEDPRYADLLRGATPVQALRKVFGLQGLLTLFVSFPLQLSAVTGPTPKPLLAVGGVGLAVWLVGITFEAVGDWQLWVFKSDPANRGVIMDRGLWAWTRHPNYFGDACVWWGLWLITINDWAPLATVGSPLLMTYLLVDVSGARLTERYLKGRPGFAEYQRRTAYFVPRPPRSARR
Protein: Coiled-coil alpha-helical rod protein 1 (Alpha-helical coiled-coil rod protein) (Putative gene 8 protein) (Pg8) (Q8TD31)
Organism: Homo sapiens (Human)
Function: May be a regulator of keratinocyte proliferation or differentiation.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Corneodesmosin
- HLA class I histocompatibility antigen, C alpha chain
- Transcription factor 19
- Psoriasis susceptibility 1 candidate gene 2 protein
- Steroidogenic acute regulatory protein, mitochondrial
- IQ domain-containing protein C
- Keratin, type I cytoskeletal 16
Sequence:
MFPPSGSTGLIPPSHFQARPLSTLPRMAPTWLSDIPLVQPPGHQDVSERRLDTQRPQVTMWERDVSSDRQEPGRRGRSWGLEGSQALSQQAEVIVRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELEALARAEKAGRAEAEGLRAALAGAEVVRKNLEEGSQRELEEVQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLSSLETRRAGEAKELAEAQREAELLRKQLSKTQEDLEAQVTLVENLRKYVGEQVPSEVHSQTWELERQKLLETMQHLQEDRDSLHATAELLQVRVQSLTHILALQEEELTRKVQPSDSLEPEFTRKCQSLLNRWREKVFALMVQLKAQELEHSDSVKQLKGQVASLQEKVTSQSQEQAILQRSLQDKAAEVEVERMGAKGLQLELSRAQEARRRWQQQTASAEEQLRLVVNAVSSSQIWLETTMAKVEGAAAQLPSLNNRLSYAVRKVHTIRGLIARKLALAQLRQESCPLPPPVTDVSLELQQLREERNRLDAELQLSARLIQQEVGRAREQGEAERQQLSKVAQQLEQELQQTQESLASLGLQLEVARQGQQESTEEAASLRQELTQQQELYGQALQEKVAEVETRLREQLSDTERRLNEARREHAKAVVSLRQIQRRAAQEKERSQELRRLQEEARKEEGQRLARRLQELERDKNLMLATLQQEGLLSRYKQQRLLTVLPSLLDKKKSVVSSPRPPECSASAPVAAAVPTRESIKGSLSVLLDDLQDLSEAISKEEAVCQGDNLDRCSSSNPQMSS
Protein: Uncharacterized protein 9G6.050 (Q96UA9)
Organism: Neurospora crassa
Interaction partners:
Sequence:
MAGPGRPRRRRGSSASIDSTDDRRRRWTRELAILKPVTPGTSDDLWPYFAVLTDATIYQKDGKTLANPLHVDLEGPFIVRGKLEPVEDGDDEARECFHKPYNKATYIEISRSERYSIGYEPNTLWVSGASGWFEIIPSRKYETMYNEVMEAITLYYGIMGPYEEHKRLLKKADKKKRKDVKPPSLDEIFFSYALTAGDGAVTVKEEVEARCLKWAQFLLAHFPKESEIRWQDTGFAAWLQSARPDLQKKISDVAAGLLTKPAAEPEGLLARDDHSPQPQSLAIREPPKGGRTTRTSRQASELSDQRSDKGKGIARDSPVETPIPAPVSNRHLSSSSPRPRASPAVITGSDDLPDDPVDRLIVLLGEVAQRIDIKTVKMSKINSDLFYNCRIKYYNAARELCEHFAKDLLERLPPMWDNTPYRAWLEDVVENGRPAPVEFVVEDIPQYLTRRTRRQTHISRLSSALGPTPSVEAESKDEVRAGKQPRVGRPSGKVATLRVAGSKRLASDMIDEDELPPRRGRKALKRTVRVEEDEDSDANSVIIDMTDNTGVIPKDAVRIVVQAERLPTMSPAGPNGTWTCDQEGCNYVVRSADEPEGQDLISKHFKDHEEQAQKINLAMEESSHSHLLDKIQAMGKNALAKKRGSLNGEPLPLPIKRRLLI
Protein: Transmembrane protein with metallophosphoesterase domain (EC 3.1.-.-) (Q6ZT21)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAIFRQLSLGAKATLAAVTVFVSMIASRSYLAESLELRAWRWLLRLQLALFVNSLLLIGSLYIWRSTVSNLCHSPAAESTCFQLWKVVVLAFLALAHSSFFTMFFLVAEEPYLFSLAAYSCLGAYIIMLFFLFILSGMEQAYQLLAWRSGRVVGSLEKTRKLVLRPALAVGVTAVLSVAGILNAAQPPAVKTVEVPIHQLPASMNNLKIVLLSDIHLGPTVGRTKMEMFVRMVNVLEPDITVIVGDLSDSEASVLRTAVAPLGQLHSHLGAYFVTGNHEYYTSDVSNWFALLESLHVQPLHNENVKISATRAQRGGGGSGSGSEDEDWICLAGVDDIEADILHYSGHGMDLDKALEGCSPDHTIILLAHQPLAAKRALQARPDINLILSGHTHAGQIFPLNVAAYLLNPFFAGLYQVAQATFVYVSPGTAYYGIPMRLGSRAEITELILQRSP
Protein: FI02030p (Tejas) (A1Z9P1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Probable ATP-dependent RNA helicase spindle-E
- Protein aubergine
- Tudor domain-containing protein krimp
- Protein vreteno
- Protein piwi
- Chromo domain-containing protein rhino
- Probable RNA helicase armi
- Mitochondrial cardiolipin hydrolase
- Putative ATP-dependent RNA helicase BoYb
- Kotsubu
Sequence:
MDDGGELSLVKKVVHSLVVSSPGKLTVEQLMRDYRSEEGCTLPYSKLGFKDAESFLRSIPDTVTVTGHGQMAWITAVATAKSAHIQKLVRCQKKSKNRGSHKPKYCYASEPSNLVFINESVSKMKNRKAPFPTYQVPRNLKLPVSYPNYNRLLYPVHTPHIDQMISTGQQQSTLRTQRPSFPCNANSKSLKVNDWSQKDRKQEPSKERNNQKYPKITTENKQEKETEELAQAFENLSVDVAPTDHQEKLKCEIYEDNEDEFVRDPFIYGEVKEKEDEAVVLAFDAVSEDGFDLLSMTTTQQNAVKPLDPPEDCLHYASSDDGEDENAIPAYAVDHRVLDVDYPRDAVRSAFTLPARDIESIIELQQRIRVQLVSLVNPHNFNFWIYNDDFKDYEAQFANMQTFYESSESKNYTMPLFLITTDHLCVVRCTSGWERAKVLGYRSSNNKMTIEVELVDIGDIIRVSQQNVKFLIKPFALLPRQCLAGRLAFITQCKSPNWTAEVVNFFHDMILLRLLYAKVEAIKNNTAYLVLVDTESQGHTVNLNRSLIETGWVRRCTSA
Protein: Phage shock protein C (P0AFN2)
Organism: Escherichia coli (strain K12)
Function: The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspC is involved in transcription regulation.
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phage shock protein D
- Phage shock protein B
- Phage shock protein A
- Psp operon transcriptional activator
- Phage shock protein G
- Thiosulfate sulfurtransferase PspE
- Aerobic respiration control sensor protein ArcB
- Universal stress protein E
- Sensor histidine kinase GlrK
Sequence:
MAGINLNKKLWRIPQQGMVRGVCAGIANYFDVPVKLVRILVVLSIFFGLALFTLVAYIILSFALDPMPDNMAFGEQLPSSSELLDEVDRELAASETRLREMERYVTSDTFTLRSRFRQL
Protein: Hepatocyte nuclear factor 4-alpha (HNF-4-alpha) (Nuclear receptor subfamily 2 group A member 1) (Transcription factor 14) (TCF-14) (Transcription factor HNF-4) (P49698)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator which controls the expression of hepatic genes during the transition of endodermal cells to hepatic progenitor cells, facilitatating the recruitment of RNA pol II to the promoters of target genes (By similarity). Activates the transcription of CYP2C38. Represses the CLOCK-BMAL1 transcriptional activity and is essential for circadian rhythm maintenance and period regulation in the liver and colon cells.
Subcellular location: Nucleus.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Nuclear receptor subfamily 0 group B member 2
- Forkhead box protein O1
- Histone lysine acetyltransferase CREBBP
- Hepatocyte nuclear factor 1-alpha
- Nuclear receptor coactivator 1
- Sterol regulatory element-binding protein 1
- Bile acid receptor
- Nuclear receptor coactivator 2
- Hepatocyte nuclear factor 3-beta
Sequence:
MRLSKTLAGMDMADYSAALDPAYTTLEFENVQVLTMGNDTSPSEGANLNSSNSLGVSALCAICGDRATGKHYGASSCDGCKGFFRRSVRKNHMYSCRFSRQCVVDKDKRNQCRYCRLKKCFRAGMKKEAVQNERDRISTRRSSYEDSSLPSINALLQAEVLSQQITSPISGINGDIRAKKIANITDVCESMKEQLLVLVEWAKYIPAFCELLLDDQVALLRAHAGEHLLLGATKRSMVFKDVLLLGNDYIVPRHCPELAEMSRVSIRILDELVLPFQELQIDDNEYACLKAIIFFDPDAKGLSDPGKIKRLRSQVQVSLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFIKLFGMAKIDNLLQEMLLGGSASDAPHTHHPLHPHLMQEHMGTNVIVANTMPSHLSNGQMCEWPRPRGQAATPETPQPSPPSGSGSESYKLLPGAITTIVKPPSAIPQPTITKQEAI
Protein: Vacuolar amino acid transporter 2 (P39981)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable amino acid transporter of unknown specificity.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:11274162}; Multi-pass membrane protein {ECO:0000269|PubMed:11274162}.
Interaction partners:
- 5-oxoprolinase
Sequence:
MSELGEYSKLENKELRTEFELTNFPFPGTTDNDSDDGSQGQNSLNIITPDMDDTLVNDVLRENDKKSSMRMAFMNLANSILGAGIITQPFAIKNAGILGGLLSYVALGFIVDWTLRLIVINLTLAGKRTYQGTVEHVMGKKGKLLILFTNGLFAFGGCIGYCIIIGDTIPHVLRAIFSQNDGNVHFWLRRNVIIVMVTTFISFPLSMKRNIEALSKASFLAVISMIIIVLTVVIRGPMLPYDWKGHSLKLSDFFMKATIFRSLSVISFALVCHHNTSFIFFSMRNRSVAKFTRLTHISIIISVICCALMGYSGFAVFKEKTKGNVLNSFPGTDTAINIARLCFGFNMLTTFPMEIFVLRDVVGNLLHECNLIKNYDEHTQLSGKQHVVITSSLVFITMGISLTTCNLGALFELIGATTASTMAYILPPYTNLLLTSKKKSWKERLPFYLCICFGFMIMIISSTQTIIDAVNGSDGQHCQI
Protein: Rhoptry protein 4 (Q5Y808)
Organism: Toxoplasma gondii
Function: Thought to play a role in parasitophorous vacuole membrane function during the infection of host organisms.
Subcellular location: Secreted {ECO:0000269|PubMed:15470260}. Parasitophorous vacuole membrane {ECO:0000269|PubMed:15470260}. Note=Localized to rhoptries which are secretory organelles at the apical end of the parasite and secreted during host cell invasion when it becomes associated with the parasitophorous vacuole membrane.
Interaction partners:
Sequence:
MGHPTSFGQPSCLVWLAAAFLVLGLCLVQQGAGRQRPHQWKSSEAALSVSPAGDIVDKYSRDSTEGENTVSEGEAEGSRGGSWLEQEGVELRSPSQDSQTGTSTASPTGFRRLLRRLRFWRRGSTRGSDDAAEVSRRTRVPLHTRLLQHLRRVARIIRHGVSAAAGRLFGRVRQVEAERPQPVFTEGDPPDLETNSLYYRDKVPGQGIIQEILRQKPGIAHHPESFSVVAADERVSRTLWAEGGVVRVASELGQPGRVLVRGRRIGLFRPGMQFEATDQATGEPMTALVGHTVLEATARDVDSMRNEGLAVGLFQKVKNPYLANRYLRFLAPFDLVTIPGKPLVQKAKSRNEVGWVKNLLFLLPPTHVDMETFVDEIGRFPQEDRPLADAARLYLTVQAVRLVAHLQDEGVVHGKIMPDSFCLKREGGLYLRDFGSLVRAGAKVVVPAEYDEYTPPEGRAAARSRFGSGATTMTYAFDAWTLGSVIFLIWCSRAPDTKSGYEYSVEFFFSRCRRVPENVKLLVYKLINPSVEARLLALQAIETPEYREMEEQLSAASRLYSGDGTLTGGDDDMPPLET
Protein: Exosome complex component CSL4 (Exosome component 1) (Q9DAA6)
Organism: Mus musculus (Mouse)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC1 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC6 and EXOSC8 (By similarity).
Subcellular location: Nucleus, nucleolus. Nucleus {ECO:0000250|UniProtKB:Q9Y3B2}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y3B2}.
Interaction partners:
- Exosome complex component 10
- Exosome complex component RRP4
- Exosome complex component MTR3
- Exosome complex exonuclease RRP44
- Exosome complex component RRP40
- Exosome complex exonuclease RRP42
- Exosome complex component RRP41
- Exosome complex component RRP45
- Exosome complex component RRP46
- Exosome complex component RRP43
Sequence:
MAPPVRYCIPGERLCNLEEGSPGSGTYTRHGYIFSSLAGCLMKTSENGAVPVVSVMRETESQLLPDVGAVVTCKVSSINSRFAKVHILYVGSTPLKNAFRGTIRKEDIRATEKDKVEIYKSFRPGDIVLAKVISLGDAQSNYLLTTAENELGVVVAHSESGVQMVPISWCEMQCPKTHTKEFRKVARVQPEFLQT
Protein: Trafficking protein particle complex subunit 9 (A0A8I6AP83)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MSVPDYMQCAEDHQTLLVVVQAVGIVSEENFFRIYKRICSVSQLSVRDSQRALFIRYRHHYPPENNEWGDFQTHRKVVGLITITDCFSPKDWPQTFEKFHVQKEIYGSTLYDSRLFVFGLQGDVAEQPRPDVAFYPNYDDCDSVEKRIEDFIESLFIVLESKRLDRATDKSGDKIPLLCVPFEKKDFVGLDTDSRHYKKRCQGRMRKHVGDLCLQAGMLQDALVHYHMSVELLRSVNDFLWLGAALEGLCSASVIYHYPGGTGGKTGARRLPGNSLPSEAANRHRPGALTTNGINPDTSTEIGRAKNCLSPEDIIDKYKEAISYYSKYKNAGVIELEACVKAVRVLAIQKRGMEASEFLQNAVYINLRQLSEEEKIQRYSILSELYELIGFHRKSAFFKRVAAMQCVAPSIAEPGWRACYKLLLETLPGYSLSLDPKDFNKGTHDDLGLGWRLLYFHLACAFEQPLSSPSSALPTEPTFYFVSSSEKKDVTQSLENYTAKCPGTMEPITLPDGLTLPPVPFTKLPIVRCVKLLSLPTSLRPQKVKSLLGQSMSTKSPFIYSPIIAHNRGEERNKKIDFQWVQGDVCEVQLMVYNPMPFELRVENMGLLTSGVEFESLPAALSLPAESGLYPVTLVGVPQTTGMITVNGYHTTVFGVFSDCLLDNLPGLKTSGSTVEVIPALPRLQISTSLPRSAHSLQPSAGDEIATNVSVQLFNGETQQLAITLENIGLEPLEQLEVTSKLLTTKEKLYGDFLSWKLEETLAQFPLQPGKVATFTINIKAKLDFSCQENLLQDLSDDGISVSGFPLSSPFRQVVRPRVESRPTNPSEGSKTGDLGHVKVSPSVEVQAARVGSPGFCWSTFQLAFGVPF
Protein: Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase) (P15429)
Organism: Rattus norvegicus (Rat)
Function: Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. Appears to have a function in striated muscle development and regeneration.
Subcellular location: Cytoplasm. Note=Localized to the Z line. Some colocalization with CKM at M-band (By similarity). {ECO:0000250}.
Interaction partners:
- Phosphoglycerate mutase 2
- Pyruvate kinase PKM
- Pyruvate kinase PKLR
- Phosphoglycerate mutase 1
- Fructose-bisphosphate aldolase A
- Glucose-6-phosphate isomerase
- Phosphoenolpyruvate carboxykinase, cytosolic
- Fructose-bisphosphate aldolase C
- Fructose-bisphosphate aldolase
- Fructose-bisphosphate aldolase B
Sequence:
MAMQKIFAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKSRYLGKGVLKAVEHINKTLGPALLEKKLSVVDQEKVDKFMIELDGTENKSKFGANAILGVSLAVCKAGAAEKGVPLYRHIADLAGNPDLVLPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKEAMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKVVIGMDVAASEFYRNGKYDLDFKSPDDPARHISGEKLGELYKSFIKNYPVVSIEDPFDQDDWATWTSFLSGVDIQIVGDDLTVTNPKRIAQAVEKKACNCLLLKVNQIGSVTESIQACKLAQSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEALGDKAVFAGRKFRNPKAK
Protein: Metal cation symporter ZIP14 (Solute carrier family 39 member 14) (Zrt- and Irt-like protein 14) (ZIP-14) (A0A0G2KQY6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Broad-scope metal ion transporter with a preference for zinc uptake. Also mediates cellular uptake of nontransferrin-bound iron.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27231142}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Solute carrier family 30 member 10
- Zinc transporter ZIP1
- Solute carrier family 39 member 8.
- Solute carrier family 30 member 1b
- Solute carrier family 30
- Zinc transporter ZIP9
- Probable proton-coupled zinc antiporter SLC30A3
- Solute carrier family 30
- Solute carrier family 11 member 2.
- Zinc transporter 6
Sequence:
MTLRRASGCRQLTLTIGLALTLGLLQWPIGDVRGQDGASPAQVLQELLTRYGDNASISVPQLRSLLVRLNGGQSEDHDSKTQPTRTNASKCLAADTLAVYGMSEQSRIDERGLQQICPTMIQQLDSQACKTQPNQESESSPRPTEAEVWGYGLLCVTVISLCSLVGASVVPFMRKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFDPMEDYYVPKSAVVFGGFYLFFFTEKILKMILKPKDTGGHGHGHSHFPAERYANSNGDLEDGVMEKLQNGEAGGAALPRAEADGRGVGEDDKMLSTGQTVQDTQSSGGGGTGGCYWLKGRAYSDIGTLAWMITLSDGLHNFIDGLAIGASFTASVFQGISTSVAILCEEFPHELGDFVILLNAGMSIQQALFFNFLSACCCYLGMGFGILAGNNFSPNWIFALAGGMFLYIALADMFPEMNEVSREEEEAGGSGFLLTFALQNAGLLTGFAIMLVLTIYSGQIQLG
Protein: Inhibitor-2, isoform B (A8JNP7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine/threonine-protein phosphatase beta isoform
- Serine/threonine-protein phosphatase alpha-1 isoform
- Serine/threonine-protein phosphatase alpha-3 isoform
- Serine/threonine-protein phosphatase alpha-2 isoform
Sequence:
MEAVVQAEADDNNASDVQRGVGGALLAVVATQWAAMATPPRARGFAATCAIIIWRTSRFQCLFGYCRRDSRLSSSNSGSSNRNNNHKIYEIINDSQPPDVTQIARMQNNPSPQLPCKGILKTSRSFDKSGASFRKSAKFDELNVMQTFHPADKDYGHMKIDEPKTPYNYTEGFDENRDELDTELLVEKLRIAANTQPSTESIEDDGSSGDDQPLSEEERQRRREFERRRKAHYREFEAVKLARKLIQEEDDDDDDEDKGADSRPSGSSQGASSSGRFASSSTKRSSSQADSTTSPSTSAGQNMDLEPSNN
Protein: ARF GTPase-activating protein GIT2a (G protein-coupled receptor kinase-interacting ArfGAP 2a) (A2BG45)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Paxillin
- Paxillin
- G protein-coupled receptor kinase
- Rho guanine nucleotide exchange factor
- Rac/Cdc42 guanine nucleotide exchange factor
- Corrinoid adenosyltransferase MMAB
- G protein-coupled receptor kinase
- Non-specific serine/threonine protein kinase.
- Adenylosuccinate lyase
Sequence:
MVIPTLTETRMSKRLRNSEVCADCSTSDPRWASVNRGVLICDECCSVHRSLGRHNSQVRHLSNTSWPPTQLQMVQTLYNNGANAIWEHTLLDPSSIMSSKRKPNHQDKLHPNKADFIKAKYQMLAYVHRLPCRDDDSTAAADLSKQLHSSVRTGNLETCLRLLSLGAQANYFHPEKGNTPLHIAAKAGQVCQAELLCVYGADPGAPDSSGKTPINYARQAGHQDLADRLVEIQYELTDRLAFYLCGRKPDHKSGQHFIIPQMADSSVELTEFAKAAKRKLQSLSDHLFEELAMDVYDEVDRRETDAVWLATQNHSTLVTETTVVPFLPVNPEYSSTRNQGRQKLARFNAHEFATLVIDILSDAKRRQHGNPVPSPKDNVDVFFKSGGSRHGSESQEIDQPDYDSVASDEDTDTDLRMGKADRTKSLDSDLSDGPVSVQEFLEVKNALSASEAKIQELMKANSNLNEELRLMQKKLQSLQSENSSLRRQVSAQQPYQAPGGPDHPNPSSPSSCSSSSSSSSALKRHLSARASRPMSMYETGSGLKPFLPKGETPYPEETFPTLQPFPAYASKFDKQSSVSDGDYDNTVNESDLDDSGFGRRCRLRSSGWMGESGSIPELEDHECELDPSLPSTEDVIRKTEQITKNIQELLRAAQENKHESFVPCAERIHVAVNEMAALFPKRPRSETVRNSLRLLTSSANRLQTECKKASPLESSQASDMQLVTQQVIQCAYDIAKAAKQLVTITTKENN
Protein: Pumilio homolog 3 (HBV X-transactivated gene 5 protein) (HBV XAg-transactivated protein 5) (Minor histocompatibility antigen HA-8) (HLA-HA8) (Q15397)
Organism: Homo sapiens (Human)
Function: Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress. Binds to double-stranded RNA or DNA without sequence specificity. Involved in development of the eye and of primordial germ cells (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:21266351, ECO:0000269|Ref.6}. Nucleus, nucleoplasm {ECO:0000269|PubMed:21266351}. Chromosome {ECO:0000269|PubMed:20813266}. Note=Localizes predominantly in the nucleolus with minor punctate signals in the nucleoplasm. {ECO:0000269|PubMed:21266351}.
Interaction partners:
- Probable rRNA-processing protein EBP2
- Ribosome production factor 2 homolog
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- GTP-binding protein 4
- Ribosome biogenesis protein BRX1 homolog
- ATP-dependent RNA helicase DDX18
- 28S rRNA
- RNA-binding protein 28
- CCAAT/enhancer-binding protein zeta
- pre-rRNA 2'-O-ribose RNA methyltransferase FTSJ3
Sequence:
MEVKGKKQFTGKSTKTAQEKNRFHKNSDSGSSKTFPTRKVAKEGGPKVTSRNFEKSITKLGKKGVKQFKNKQQGDKSPKNKFQPANKFNKKRKFQPDGRSDESAAKKPKWDDFKKKKKELKQSRQLSDKTNYDIVVRAKQMWEILRRKDCDKEKRVKLMSDLQKLIQGKIKTIAFAHDSTRVIQCYIQYGNEEQRKQAFEELRDDLVELSKAKYSRNIVKKFLMYGSKPQIAEIIRSFKGHVRKMLRHAEASAIVEYAYNDKAILEQRNMLTEELYGNTFQLYKSADHRTLDKVLEVQPEKLELIMDEMKQILTPMAQKEAVIKHSLVHKVFLDFFTYAPPKLRSEMIEAIREAVVYLAHTHDGARVAMHCLWHGTPKDRKVIVKTMKTYVEKVANGQYSHLVLLAAFDCIDDTKLVKQIIISEIISSLPSIVNDKYGRKVLLYLLSPRDPAHTVREIIEVLQKGDGNAHSKKDTEVRRRELLESISPALLSYLQEHAQEVVLDKSACVLVSDILGSATGDVQPTMNAIASLAATGLHPGGKDGELHIAEHPAGHLVLKWLIEQDKKMKENGREGCFAKTLVEHVGMKNLKSWASVNRGAIILSSLLQSCDLEVANKVKAALKSLIPTLEKTKSTSKGIEILLEKLST
Protein: 3'-5' ssDNA/RNA exonuclease TatD (EC 3.1.11.-) (EC 3.1.13.-) (DNase TatD) (P27859)
Organism: Escherichia coli (strain K12)
Function: 3'-5' exonuclease that prefers single-stranded DNA and RNA. May play a role in the H(2)O(2)-induced DNA damage repair.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00901, ECO:0000269|PubMed:10747959, ECO:0000269|PubMed:25114049}.
Interaction partners:
- Sec-independent protein translocase protein TatC
- Sec-independent protein translocase protein TatB
- Sec-independent protein translocase protein TatA
- Sec-independent protein translocase protein TatE
Sequence:
MFDIGVNLTSSQFAKDRDDVVACAFDAGVNGLLITGTNLRESQQAQKLARQYSSCWSTAGVHPHDSSQWQAATEEAIIELAAQPEVVAIGECGLDFNRNFSTPEEQERAFVAQLRIAADLNMPVFMHCRDAHERFMTLLEPWLDKLPGAVLHCFTGTREEMQACVAHGIYIGITGWVCDERRGLELRELLPLIPAEKLLIETDAPYLLPRDLTPKPSSRRNEPAHLPHILQRIAHWRGEDAAWLAATTDANVKTLFGIAF
Protein: F-box/kelch-repeat protein At5g49000 (Q9FI70)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box protein SKIP22
- Thioredoxin-like 3-2, chloroplastic
- Probable protein S-acyltransferase 15
- Nucleic acid-binding, OB-fold-like protein
- Alpha carbonic anhydrase 3
- F-box protein SKIP31
- F-box protein SKIP24
- Metal-independent phosphoserine phosphatase
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 9
- Synaptotagmin-3
Sequence:
MSSPERKRKKRSLEPSPESTPNPSLPDDLIVSILARVSRLYYPILSLVSKSSRTLVTSPELYKTRSFFNRTESCLYVCLDFPPDPNPRWFTLYRKPNQNITEKTKNSSGFVLAPIPNHHSHSSSIVAIGSNIYAIGGSIENAPSSKVSILDCRSHTWHEAPSMRMKRNYPAANVVDGKIYVAGGLEEFDSSKWMEVFDIKTQTWEFVLSPLAERFIYRSLVIEGEIYIFGDKVVTYKPKEDRWGGVGEHQSMDLGLFFHSYCVIDNVLYCYRPGGIKWYESEKRSWRKLRGLKGLSKLASSCVKLADYGGKMALLWDKYIPCSGNKSHSISCAVVSLERCKNQGIRGKVEWFDDMLTVPSSYNFVGALAATL
Protein: Urea transporter 2 (Solute carrier family 14 member 2) (Urea transporter, kidney) (Q15849)
Organism: Homo sapiens (Human)
Function: Mediates the transport of urea driven by a concentration gradient across the cell membrane of the renal inner medullary collecting duct which is critical to the urinary concentrating mechanism.
Subcellular location: [Isoform 1]: Apical cell membrane {ECO:0000269|PubMed:17702749}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:17702749}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSDPHSSPLLPEPLSSRYKLYEAEFTSPSWPSTSPDTHPALPLLEMPEEKDLRSSNEDSHIVKIEKLNERSKRKDDGVAHRDSAGQRCICLSKAVGYLTGDMKEYRIWLKDKHLALQFIDWVLRGTAQVMFINNPLSGLIIFIGLLIQNPWWTITGGLGTVVSTLTALALGQDRSAIASGLHGYNGMLVGLLMAVFSEKLDYYWWLLFPVTFTAMSCPVLSSALNSIFSKWDLPVFTLPFNIAVTLYLAATGHYNLFFPTTLVEPVSSVPNITWTEMEMPLLLQAIPVGVGQVYGCDNPWTGGVFLVALFISSPLICLHAAIGSIVGLLAALSVATPFETIYTGLWSYNCVLSCIAIGGMFYALTWQTHLLALICALFCAYMEAAISNIMSVVGVPPGTWAFCLATIIFLLLTTNNPAIFRLPLSKVTYPEANRIYYLTVKSGEEEKAPSGGGGEHPPTAGPKVEEGSEAVLSKHRSVFHIEWSSIRRRSKVFGKGEHQERQNKDPFPYRYRKPTVELLDLDTMEESSEIKVETNISKTSWIRSSMAASGKRVSKALSYITGEMKECGEGLKDKSPVFQFFDWVLRGTSQVMFVNNPLSGILIILGLFIQNPWWAISGCLGTIMSTLTALILSQDKSAIAAGFHGYNGVLVGLLMAVFSDKGDYYWWLLLPVIIMSMSCPILSSALGTIFSKWDLPVFTLPFNITVTLYLAATGHYNLFFPTTLLQPASAMPNITWSEVQVPLLLRAIPVGIGQVYGCDNPWTGGIFLIALFISSPLICLHAAIGSTMGMLAALTIATPFDSIYFGLCGFNSTLACIAIGGMFYVITWQTHLLAIACALFAAYLGAALANMLSVFGLPPCTWPFCLSALTFLLLTTNNPAIYKLPLSKVTYPEANRIYYLSQERNRRASIITKYQAYDVS