wanglab/gogpt-training-data huggingface dataset:
Protein: At1g67410 (Exostosin family protein) (Glycosyltransferase) (Q08AA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
Sequence:
MYGKTICTIVFFIFLVASFSIYMGTVDPRPYFYLLQSQPNGASSPCSSSGKPLRVFMYDLPRKFNIAMMDPHSSDVEPITGKNLPSWPQTSGIKRQHSVEYWLMASLLNGGEDENEAIRVFDPDLADVFYVPFFSSLSFNTHGKNMTDPDTEFDRLLQVELMEFLENSKYWNRSGGKDHVIPMTHPNAFRFLRQQVNASILIVVDFGRYSKDMARLSKDVVSPYVHVVESLNEEGDDGMGDPFEARTTLLYFRGNTVRKDEGKIRLRLEKLLAGNSDVHFEKSVATTQNIKVSTEGMRSSKFCLHPAGDTPSSCRLFDAIVSHCIPVIISDKIELPFEDEIDYSEFSLFFSIKESLEPGYILNNLRQFPKEKWLEMWKRLKNVSHHFEFQYPPKREDAVNMLWRQVKHKIPYVKLAVHRNRRLKVPDWWL
Protein: Cell surface glycoprotein CD200 receptor 4 (CD200 cell surface glycoprotein receptor-like 4) (CD200 receptor-like 4) (CD200 cell surface glycoprotein receptor-like a) (CD200RLa) (Cell surface glycoprotein OX2 receptor 4) (Q6XJV4)
Organism: Mus musculus (Mouse)
Function: Involved in the recruitment or surface expression of the TYROBP receptor.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- OX-2 membrane glycoprotein
Sequence:
MHALGRIPTLTLLIFINIFVSGSSCTDENQTIQNDSSSSLTQVNTTMSVQMDKKALLCCFSSPLINAVLITWIIKHRHLPSCTIAYNLDKKTNETSCLGRNITWASTPDHSPELQISAVALQHEGTYTCEIVTPEGNLEKVYDLQVLVPPEVTYFPGKNRTAVCEAMAGKPAAQISWTPDGDCVTKSESHSNGTVTVRSTCHWEQNNVSVVSCLVSHSTGNQSLSIELSQGTMTTPRSLLTILYVKMALLVIILLNVGFAFFQKRNFART
Protein: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, chloroplastic (MECDP-synthase) (MECPS) (MECS) (EC 4.6.1.12) (Q9CAK8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Enzyme of the plastid non-mevalonate pathway for isoprenoid biosynthesis that converts 4-diphosphocytidyl-2C-methyl-D-erythritol 2-phosphate into 2C-methyl-D-erythritol 2,4-cyclodiphosphate and CMP. Is essential for chloroplast development.
Subcellular location: Plastid, chloroplast stroma {ECO:0000305|PubMed:18236010}.
Interaction partners:
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase, chloroplastic
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase, chloroplastic
- 1-deoxy-D-xylulose-5-phosphate synthase, chloroplastic
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, chloroplastic
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- 1-deoxy-D-xylulose-5-phosphate synthase
- Hydroxymethylglutaryl-CoA synthase
- 1-deoxy-D-xylulose-5-phosphate synthase
- Phosphomevalonate kinase, peroxisomal
Sequence:
MATSSTQLLLSSSSLFHSQITKKPFLLPATKIGVWRPKKSLSLSCRPSASVSAASSAVDVNESVTSEKPTKTLPFRIGHGFDLHRLEPGYPLIIGGIVIPHDRGCEAHSDGDVLLHCVVDAILGALGLPDIGQIFPDSDPKWKGAASSVFIKEAVRLMDEAGYEIGNLDATLILQRPKISPHKETIRSNLSKLLGADPSVVNLKAKTHEKVDSLGENRSIAAHTVILLMKK
Protein: Nuclear pore complex protein (A1YK57)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|RuleBase:RU365072}. Nucleus membrane {ECO:0000256|RuleBase:RU365072}.
Interaction partners:
Sequence:
MADSPFPRSSRSGLLRTTLNSSMAPQNLSHSLLILEKSNAEQNERSLMEDTGDDLDRGKSRMDVLFPQFFDVLQAQGNGQEAFEVIQSLTQVCRGVVEQLELEIDHGMGGEQGARQRESMLTWLRQEINTWRLLHALFYDRILLQTDRQADDEMQDGPTLGGSEKEVIQQLYALNATLREYQLVVDWLEACYDRGEQQNPLHAHDRMMAWENTLFQLENLQGAAFGKGHKIVTRLDPDAPVREKRPLHALDEEDNLRLSRAIFELIRAGRVDDGLKLCKHFGQTWRAAILEGWRLHEDPNFEQNVSVLHEKLPIEGNPRRDIWKRCAWMLADSKNYDEYSRATAGVFSGHLGSLKTLLHSNWHDLLWAHLKVQIDIRVESEIRGCCLKNYQPMPDDYWNGRMTMEQIFEELNVAKDASVRDFAQSQLGIIQRHLILDTCGELIQHMVRWVEKDTSQQSPHQLRFMAHIVLFLRQIGRVEQERQAEKIVAAYVEALIARGEPQLIAYYTASLSNPLQVQLYSRFLEQVVQKRPRELAVDAALQAGLDVEQITRVTVQNIRLAHQPLGEFGEPQSGEISAIDQRKISALEWLIHLPEQRGELLWQANAMIRTYLASSKVECMRQTFRMVPADIVQQLVSLYGSVDNIPPREECCLKEYLCYKAYLSGVDSFVEWNRLQQNRPKKPQTSHAASSQDNFTERMASERKEQAHRSEVVRWEHKVXEQXXQTIELLYNVLMFPDKGWLVDPFIAKLPENAVQLNWDHRLLQMEKLRSICIPEIALFLNEVMFKSGDFAGCVRLADEISSENRQLYKVYTKHKLAELLAKIADASLELLNSKLDPWGYPITT
Protein: ADP ribosylation factor-like 4, isoform C (L0MN60)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGATMVKPLVKNGNILDALPSQATLHVVMLGLDSAGKTTALYRLKFDQYLNTVPTIGFNCEKVQCTLGKAKGVHFLVWDVGGQEKLRPLWRSYTRKNGRS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q38B11)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSTDAMIGRVCRTFGEAFAKDEATAKEQKKKYWIKRVLGSGATGTVLCAKRTSDGETFAVKVVDLEGMNEGDKNRAQAEVHCLMNCDFFSILKCHEDFAKKDPQNEVNVLMIALVLDYANAGDLRQEIKSRAKTSRAFREHEAGLLFIQVLLALHHVHSRHMIHRDIKSANILLCSNGLIKLGDFGFTKMYSATVSDDVGKTFCGTPYYVAPEIWRRKPYSKKADLFSLGVLLYELLTLRRPFDGESMRDVMNRTLSGQYDPLPPETSPEMAEIVSLLLSSDPKQRPCSGKLLDMPICKLFMSGLLEIVQTQPAFEGPLRDVIPSDIRNIKQLLRADKRSVVKQMDESYSTAISTAVLEGATPCSGLGDVTLYEGIIKKQSSDMSWKRRYLCIRAELENGEDLSVGKLPKFKSLHLVLAISKDTLQRQCIATPFTDLEDVFPVPSKYTGSNAPNVFAVAFKAGRRLLFQARSPAKRDAWMQKIQEVLGL
Protein: Transient receptor potential cation channel subfamily V member 2 (G1SNM3)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Insulin-like growth factor 1
- Transient receptor potential cation channel subfamily M member 8
- Transient receptor potential cation channel subfamily M member 3
- Transient receptor potential cation channel subfamily A member 1
- Short transient receptor potential channel 1
- Transient receptor potential cation channel subfamily C member 6
- Transient receptor potential cation channel subfamily C member 3
- Transient receptor potential cation channel subfamily C member 4
- Ankyrin 1
Sequence:
MAPALALGQSLALVPREEKTASPGPSHQAHPDLGAGRKEGPLTASSAQERPPCLRMTSPSSPPAFRLETSDGGQDGAEVDKAQLGYGAGPPPMESRFQDEDRNFPPQIKVNLNYRKGAGASQPDLNRFDRDRLFNVVARGNPEDLAGLLEYLRRTSKYLTDSEYTEGSTGKTCLMKAVLNLQDGVNACIQPLLEIDRDSGNPQPLVNAQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGANVHAKACGHFFQKNQDTCFYFGELPLSLAACTKQWDVVNYLLENPHQPASLQAQDSLGNTVLHALVMIADDSAENSALVVRMYDGLLQAGARLCPNVQLEGIPNLEGLTPLKLAAKEGKIEIFKHILQREFSAPCQSLSRKFTEWCYGPVRVSLYDLASVDSWEENSVLEIIAFHSRSPHRHRMVVLEPLNKLLQAKWDRLIPRFCFNFLCYLVYMLIFTAVAYHQPALEKQGFPPLKATAGNSMLLLGHILILLGGVYLLLGQLWYFWRRRLFIWISFMDSYFEILFLLQALLTVLSQVLCFLAIEWYLPLLVSSLVLGWLNLLYYTRGFQHTGIYSVMIQKVILRDLLRFLLVYLVFLFGFAVALVSLSREAQNSRTPAGPNATEVGQPGAGQEDEAPPYRSILDASLELFKFTIGMGELAFQEQLRFRGVVLLLLLAYVLLTYVLLLNMLIALMSETVNSVATDSWSIWKLQKAISVLEMENGYWWCRRKKQRAGVMLTVGTRPDGSPDERWCFRVGEMNWATWEQTLPRTLCEEPSGAAAPGVMKNPTPASQRGEDSASEEDHLPLQLLQSR
Protein: Protein grainyhead (DNA-binding protein ELF-1) (Element I-binding activity) (Protein grainy-head) (Transcription factor NTF-1) (P13002)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds a CNS-specific regulatory element of the Dopa decarboxylase (Ddc) gene. Also interacts with sequences adjacent to other transcription units, including Ultrabithorax (Ubx) and engrailed (en). Activity in vivo may be required only at high levels transiently to activate the expression of Ddc in the CNS.
Subcellular location: Nucleus {ECO:0000269|PubMed:20599892, ECO:0000269|PubMed:2792757}.
Interaction partners:
- Homeobox protein abdominal-A
- E3 ubiquitin-protein ligase RING1
Sequence:
MSTSTATTSVITSNELSLSGHAHGHGHAHQLHQHTHSRLGVGVGVGILSDASLSPIQQGSGGHSGGGNTNSSPLAPNGVPLLTTMHRSPDSPQPELATMTNVNVLDLHTDNSKLYDKEAVFIYETPKVVMPADGGGGNNSDEGHAIDARIAAQMGNQAQQQQQQQQQTEHQPLAKIEFDENQIIRVVGPNGEQQQIISREIINGEHHILSRNEAGEHILTRIVSDPSKLMPNDNAVATAMYNQAQKMNNDHGQAVYQTSPLPLDASVLHYSGGNDSNVIKTEADIYEDHKKHAAAAAAAAGGGSIIYTTSDPNGVNVKQLPHLTVPQKLDPDLYQADKHIDLIYNDGSKTVIYSTTDQKSLEIYSGGDIGSLVSDGQVVVQAGLPYATTTGAGGQPVYIVADGALPAGVEEHLQSGKLNGQTTPIDVSGLSQNEIQGFLLGSHPSSSATVSTTGVVSTTTISHHQQQQQQQQQQQQQQQQQHQQQQQHPGDIVSAAGVGSTGSIVSSAAQQQQQQQLISIKREPEDLRKDPKNGNIAGAATANGPGSVITQKILHVDAPTASEADRPSTPSSSINSTENTESDSQSVSGSESGSPGARTTATLEMYATTGGTQIYLQTSHPSTASGAGGGAGPAGAAGGGGVSMQAQSPSPGPYITANDYGMYTASRLPPGPPPTSTTTFIAEPSYYREYFAPDGQGGYVPASTRSLYGDVDVSVSQPGGVVTYEGRFAGSVPPPATTTVLTSVHHHQQQQQQQQQHQQQQQQQQHHQQQQHHSQDGKSNGGATPLYAKAITAAGLTVDLPSPDSGIGTDAITPRDQTNIQQSFDYTELCQPGTLIDANGSIPVSVNSIQQRTAVHGSQNSPTTSLVDTSTNGSTRSRPWHDFGRQNDADKIQIPKIFTNVGFRYHLESPISSSQRREDDRITYINKGQFYGITLEYVHDAEKPIKNTTVKSVIMLMFREEKSPEDEIKAWQFWHSRQHSVKQRILDADTKNSVGLVGCIEEVSHNAIAVYWNPLESSAKINIAVQCLSTDFSSQKGVKGLPLHVQIDTFEDPRDTAVFHRGYCQIKVFCDKGAERKTRDEERRAAKRKMTATGRKKLDELYHPVTDRSEFYGMQDFAKPPVLFSPAEDMEKVGQLGIGAATGMTFNPLSNGNSNSNSHSSLQSFYGHETDSPDLKGASPFLLHGQKVATPTLKFHNHFPPDMQTDKKDHILDQNMLTSTPLTDFGPPMKRGRMTPPTSERVMLYVRQENEEVYTPLHVVPPTTIGLLNAIENKYKISTTSINNIYRTNKKGITAKIDDDMISFYCNEDIFLLEVQQIEDDLYDVTLTELPNQ
Protein: Complement C5 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4) [Cleaved into: Complement C5 beta chain; Complement C5 alpha chain; C5a anaphylatoxin; Complement C5 alpha' chain] (P01031)
Organism: Homo sapiens (Human)
Function: Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled.
Subcellular location: Secreted.
Interaction partners:
- Complement component C8 alpha chain
- C5a anaphylatoxin chemotactic receptor 1
- Complement component C6
- Complement component C9
- Complement component C7
- Complement component C8 beta chain
- Complement component C8 gamma chain
- C5a anaphylatoxin chemotactic receptor 2
- Complement C3
- Prothrombin
Sequence:
MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETVLTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGEHLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVWLNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGLNNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC
Protein: Tissue factor pathway inhibitor (TFPI) (Extrinsic pathway inhibitor) (EPI) (Lipoprotein-associated coagulation inhibitor) (LACI) (Q02445)
Organism: Rattus norvegicus (Rat)
Function: Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Tissue factor
- Coagulation factor VII
- Coagulation factor X
- Thrombomodulin
- Antithrombin-III
- Prothrombin
- Heparin cofactor 2
- Tissue-type plasminogen activator
- Vitamin K-dependent protein C
- Endothelial protein C receptor
Sequence:
MTNKLKKDHAFWAAVCLLLSIVPELLNALPEEDDDTINTDSELRPMKPLHTFCAMKAEDGPCKAMIRSYYFNMNSHQCEEFIYGGCRGNKNRFDTLEECRKTCIPGYKKTTIKTTSGAEKPDFCFLEEDPGICRGFMTRYFYNNQSKQCEQFKYGGCLGNSNNFETLEECRNTCEDPVNEVQKGDYVTNQITVTDRTTVNNVVIPQATKAPSQWDYDGPSWCLEPADSGLCKASEKRFYYNPAIGKCRQFNYTGCGGNNNNFTTKQDCNRACKKDSSKKSSKRAKTQRRRKSFVKVMYENIH
Protein: AMP deaminase, isoform I (EC 3.5.4.6) (M9NDW2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQSYADALSAKGYRSFGFDTDMEMDMDMGCTTMRRIEKRKGGDLADSPVDEKAEADVEVTNEISAPYEVPQFPIEQIEKKLQIQRHLNEKQATGPRPVATAAVLATNRESSSSTEGRESAVTMERNDADINFQRVSISGEDTSGVPLEDLERASTLLIEALRLRSHYMAMSDQSFPSTTARFLKTVKLKDRINNLPVKEVSGEFLYSINPIPYSHKEECKAIFWSSLVQWYLQLMHGLGWFCGLNLNATLVYLIRCIL
Protein: Olfactory receptor 5K1 (HTPCRX10) (Olfactory receptor OR3-8) (Q8NHB7)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MAEENHTMKNEFILTGFTDHPELKTLLFVVFFAIYLITVVGNISLVALIFTHRRLHTPMYIFLGNLALVDSCCACAITPKMLENFFSENKRISLYECAVQFYFLCTVETADCFLLAAMAYDRYVAICNPLQYHIMMSKKLCIQMTTGAFIAGNLHSMIHVGLVFRLVFCGSNHINHFYCDILPLYRLSCVDPYINELVLFIFSGSVQVFTIGSVLISYLYILLTIFKMKSKEGRAKAFSTCASHFLSVSLFYGSLFFMYVRPNLLEEGDKDIPAAILFTIVVPLLNPFIYSLRNREVISVLRKILMKK
Protein: histidine kinase (EC 2.7.13.3) (Q1D948)
Organism: Myxococcus xanthus (strain DK1622)
Interaction partners:
- histidine kinase
- Response regulator FrzZ
- Conserved domain protein
- Response regulator
- PilZ domain-containing protein
- histidine kinase
- Sensory/regulatory protein RpfC
- histidine kinase
- Response regulator
- histidine kinase
Sequence:
MTVPAELASAPSAPDTPELSVRMLRSVMLYYERTYGRDRLVRVWQREELPLTLAYVETLTNFVSVGFTERLFDVLDKDSGDPDFMTKAGRSIASPEAVGFLYYMMKALATPRSVYERALELDHTYNRVGGFHIDTLTDSRVQVRYVSRIRERDRNFCRARQGNLSAFPAIWNLPLAEVKELRCQVDGADCCEYDIRWQSLPPLAWRYIVGGMAGMVAGLVSGTLNLAPPVFAVSSLGMVGVAAGAWLDTRAALLRKDEKLSEQHQGLQTSLEDLQRRNDEIFAANKALEDRVAERTQELSEANTKLEASLARQQELDRLKSEFFDNVSHELRTPLTLILLTLEALAKEAESLPPELPPLVTNMERSAQRLLRLINNLLDLAQLESGKARLRYQPLELFGFLSTVVPPFHTMAERQGVTLRLEGATVTPVHVDHERIEIVFQNLLGNALKFTQKGGVTVRVREDDSEVHVEVEDSGQGIAPQDIPVIFDRFSQADNSGTRRFGGSGIGLALVKETLELHAGGISVTSELGQGSVFHVRLPKGTAHIREDLRERRQAVMPVRRERRISGAFPSLEPTGTDVLGASPPPARDHAGPGPESPRIMVVEDDPEIRSFLARLLAQHYRVMEAINGDDGRQRALRERPDLILSDVMMPVMSGLQMLTALRNDPQTVDIPVILLTARQEVTAKVEGLGTGANDYLGKPFSPNELLARIETQLRLREAAVRAAENERLAAIGLLTSGFAHEVRNPLNGLMNALLPLKDMLTGGSADVELSKAMLEVVEECGQRIRHLAESLLSFTRTSESPVVLSLDSSLDSTLSVLAWKVPPGVKVERAYHCSEPIRGNPGALNQVWLNLLDNALRAVGDKGRVRISTANTAEEAIVTIGDDGVGIRPEDMERLFQPFFSTRAAGEGTGLGLALSRRIIIQHGGSIALSSVPGEGTQVEVRLPLRPVAPRVTGGLPDLASEPRVGRLG
Protein: Keratin, type I cytoskeletal 15 (Cytokeratin-15) (CK-15) (Keratin-15) (K15) (Q61414)
Organism: Mus musculus (Mouse)
Function: In the absence of KRT14, makes a bona fide, but ultrastructurally distinct keratin filament network with KRT5.
Interaction partners:
- Keratin, type II cytoskeletal 5
Sequence:
MATTFLQTSSTFGGSSTRGASLRAGGGSFGGGSLYGGGGSRSISASSARFVSSGAGGGFGGGMSCGFGGGFGGGFGGGFGGGFGDFGGGDGGLLSGNEKVTMQNLNDRLASYLDKVRALEQANTELEVKIRDWYQKQSPASPDRDYSHYFKTMEEIRDKILAATIDNSRVVLEIDNARLAADDFRLKYENELTLRQGVEADINGLRRVLDELTLARTDLEMQIEQLNEELAYLKKNHEEEMKEFSSQLAGQVNVEMDAAPGVDLTRMLAEMREQYEAIAEKNRRDVEAWFFSKTEELNKEVASNTEMIQTSKTEITDLRRTLQGLEIELQSQLSMKAGLENSLAEVECRYATQLQQIQGVITGLETQLSELRCEMEAQNQEYNMLLDIKTRLEQEIATYRNLLEGQDAKMAGIGVREGSSGGGGSSSSSSNFHISVEESVDGKVVSSRKREI
Protein: NAD(P)H-hydrate epimerase (EC 5.1.99.6) (NAD(P)HX epimerase) (Nicotinamide nucleotide repair protein 1) (P40165)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Subcellular location: Cytoplasm. Mitochondrion.
Interaction partners:
- ATP-dependent
- mRNA-decapping enzyme subunit 1
- Pyridoxamine 5'-phosphate oxidase
- ATP-dependent RNA helicase DHH1
- Carboxypeptidase Y inhibitor
- Glutamate decarboxylase
Sequence:
MSTLKVVSSKLAAEIDKELMGPQIGFTLQQLMELAGFSVAQAVCRQFPLRGKTETEKGKHVFVIAGPGNNGGDGLVCARHLKLFGYNPVVFYPKRSERTEFYKQLVHQLNFFKVPVLSQDEGNWLEYLKPEKTLCIVDAIFGFSFKPPMREPFKGIVEELCKVQNIIPIVSVDVPTGWDVDKGPISQPSINPAVLVSLTVPKPCSSHIRENQTTHYVGGRFIPRDFANKFGFEPFGYESTDQILKL
Protein: Far-red impaired responsive (FAR1) family protein (F4JRH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- ASI1-immunoprecipitated protein 2
- N6-adenosine-methyltransferase non-catalytic subunit MTB
- Mutator-like transposase
- Mutator-like transposase
- Chromatin remodeling 34
- Histone acetyltransferase subunit NuA4-domain protein
- Thioredoxin family protein
- ARM repeat superfamily protein
- Precursor of CEP13
- AAA-type ATPase family protein
Sequence:
MMTGDLKLDEPYVGLKFESEEEAKDFYVEYSKRLGFVVRMMQRRRSGIDGRTLARRLGCNKQGFGPNNQRSSSSSSSSREGCKATILVKMEKSGKWVVTRFIKEHNHSLQFIGSSSYDSFADKERKIKELTEEIECQDRLCDVYRDRLVSFIDNVEHYTEELSLKVRDIVENVKKLECQIQTRA
Protein: Spermatogenesis-associated protein 22 (Testis development protein NYD-SP20) (Q8NHS9)
Organism: Homo sapiens (Human)
Function: Meiosis-specific protein required for homologous recombination in meiosis I.
Subcellular location: Chromosome {ECO:0000250|UniProtKB:Q5SV06}. Note=Localizes on meiotic chromosome axes. Accumulates on resected DNA. Localization is dependent on MEIOB. {ECO:0000250|UniProtKB:Q5SV06}.
Interaction partners:
- Meiosis-specific with OB domain-containing protein
- Heat shock factor 2-binding protein
Sequence:
MKRSLNENSARSTAGCLPVPLFNQKKRNRQPLTSNPLKDDSGISTPSDNYDFPPLPTDWAWEAVNPELAPVMKTVDTGQIPHSVSRPLRSQDSVFNSIQSNTGRSQGGWSYRDGNKNTSLKTWNKNDFKPQCKRTNLVANDGKNSCPVSSGAQQQKQLRIPEPPNLSRNKETELLRQTHSSKISGCTMRGLDKNSALQTLKPNFQQNQYKKQMLDDIPEDNTLKETSLYQLQFKEKASSLRIISAVIESMKYWREHAQKTVLLFEVLAVLDSAVTPGPYYSKTFLMRDGKNTLPCVFYEIDRELPRLIRGRVHRCVGNYDQKKNIFQCVSVRPASVSEQKTFQAFVKIADVEMQYYINVMNET
Protein: Diphosphoinositol polyphosphate phosphohydrolase 3-beta (DIPP-3-beta) (DIPP3-beta) (hDIPP3beta) (EC 3.6.1.52) (Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-beta) (Diadenosine hexaphosphate hydrolase (AMP-forming)) (EC 3.6.1.60) (Nucleoside diphosphate-linked moiety X motif 11) (Nudix motif 11) (hAps1) (Q96G61)
Organism: Homo sapiens (Human)
Function: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12121577}.
Interaction partners:
- EH domain-binding protein 1
- Diphosphoinositol polyphosphate phosphohydrolase 3-alpha
Sequence:
MKCKPNQTRTYDPEGFKKRAACLCFRSEREDEVLLVSSSRYPDRWIVPGGGMEPEEEPGGAAVREVYEEAGVKGKLGRLLGVFEQNQDRKHRTYVYVLTVTELLEDWEDSVSIGRKREWFKVEDAIKVLQCHKPVHAEYLEKLKLGGSPTNGNSMAPSSPDSDP
Protein: Homeobox protein prophet of Pit-1 (PROP-1) (Pituitary-specific homeodomain factor) (O75360)
Organism: Homo sapiens (Human)
Function: Possibly involved in the ontogenesis of pituitary gonadotropes, as well as somatotropes, lactotropes and caudomedial thyrotropes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Pituitary-specific positive transcription factor 1
- Growth hormone-releasing hormone receptor
- Prolactin
- Catenin beta-1
- Somatoliberin
- Pro-opiomelanocortin
- Growth hormone receptor
- Somatotropin
Sequence:
MEAERRRQAEKPKKGRVGSNLLPERHPATGTPTTTVDSSAPPCRRLPGAGGGRSRFSPQGGQRGRPHSRRRHRTTFSPVQLEQLESAFGRNQYPDIWARESLARDTGLSEARIQVWFQNRRAKQRKQERSLLQPLAHLSPAAFSSFLPESTACPYSYAAPPPPVTCFPHPYSHALPSQPSTGGAFALSHQSEDWYPTLHPAPAGHLPCPPPPPMLPLSLEPSKSWN
Protein: GH21273p (Q9VNA3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- DnaJ homolog shv
- T-complex protein 1 subunit gamma
- Heat shock protein 83
- Calreticulin
- Uncharacterized protein, isoform C
- Glucosidase II subunit alpha
- Cyclophilin 40, isoform A
- FI23714p1
- Heat shock protein 83
- Sorting nexin 6, isoform B
Sequence:
MQHILLLTGLALVGSISRGAATESNVVTCGSILKLLNSDYAFRLHSHDVKYGSGSGQQSVTGVEQKEDVNSHWVIKAQTGELCERGEPIACGSTVRLEHLSTKKNLHSHHFSSPLSGEQEVSAYGTDGLGDTGDHWEVVCSNENWMRSAHVRLRHIDTGMYLGMSGRSYGRPISGQMEIVGVHKPQHGTRWTTAEGLFIVPKEKSSTHDEYAHSEL
Protein: Volume-regulated anion channel subunit LRRC8D (Leucine-rich repeat-containing protein 5) (Leucine-rich repeat-containing protein 8D) (Q8BGR2)
Organism: Mus musculus (Mouse)
Function: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine (By similarity). Plays a redundant role in the efflux of amino acids, such as aspartate, in response to osmotic stress family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition (By similarity). Also acts as a regulator of glucose-sensing in pancreatic beta cells: VRAC currents, generated in response to hypotonicity- or glucose-induced beta cell swelling, depolarize cells, thereby causing electrical excitation, leading to increase glucose sensitivity and insulin secretion. VRAC channels containing LRRC8D inhibit transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:29773801}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7L1W4}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q7L1W4}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7L1W4}. Note=In the absence of LRRC8A, resides primarily in a cytoplasmic compartment, probably the endoplasmic reticulum (PubMed:29773801). Requires LRRC8A for expression at the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q7L1W4, ECO:0000269|PubMed:29773801}.
Interaction partners:
- Volume-regulated anion channel subunit LRRC8A
Sequence:
MFTLAEVASLNDIQPTYRILKPWWDVFMDYLAVVMLMVAIFAGTMQLTKDQVVCLPVLPSPANSKAHTPPGNADITTEVPRMETATHQDQNGQTTTNDVAFGTSAVTPDIPLQATHPHAESTLPNQEAKKEKRDPTGRKTNLDFQQYVFINQMCYHLALPWYSKYFPYLALIHTIILMVSSNFWFKYPKTCSKVEHFVSILGKCFESPWTTKALSETACEDSEENKQRITGAQTLPKHVSTSSDEGSPSASTPMINKTGFKFSAEKPVIEVPSMTILDKKDGEQAKALFEKVRKFRAHVEDSDLIYKLYVVQTLIKTAKFIFILCYTANFVNAISFEHVCKPKVEHLTGYEVFECTHNMAYMLKKLLISYISIICVYGFICLYTLFWLFRIPLKEYSFEKVREESSFSDIPDVKNDFAFLLHMVDQYDQLYSKRFGVFLSEVSENKLREISLNHEWTFEKLRQHVSRNAQDKQELHLFMLSGVPDAVFDLTDLDVLKLELIPEAKIPAKISQMTNLQELHLCHCPAKVEQTAFSFLRDHLRCLHVKFTDVAEIPAWVYLLKNLRELYLIGNLNSENNKMIGLESLRELRHLKILHVKSNLTKVPSNITDVAPHLTKLVIHNDGTKLLVLNSLKKMMNVAELELQNCELERIPHAIFSLSNLQELDLKSNNIRTIEEIISFQHLKRLTCLKLWHNKIVAIPPSITHVKNLESLYFSNNKLESLPTAVFSLQKLRCLDVSYNNISTIPIEIGLLQNLQHLHITGNKVDILPKQLFKCVKLRTLNLGQNCIASLPEKISQLTQLTQLELKGNCLDRLPAQLGQCRMLKKSGLVVEDQLFDTLPLEVKEALNQDVNVPFANGI
Protein: ATP synthase F(0) complex subunit 8 (A6L) (F-ATPase subunit 8) (P03930)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Subcellular location: Mitochondrion membrane; Single-pass membrane protein.
Interaction partners:
- ATP synthase F
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MPQLDTSTWFITIISSMITLFILFQLKVSSQTFPLAPSPKSLTTMKVKTPWELKWTKIYLPHSLPQQ