wanglab/gogpt-training-data huggingface dataset:
Protein: Receptor-like serine/threonine-protein kinase SD1-6 (EC 2.7.11.1) (Arabidopsis thaliana receptor kinase 2) (S-domain-1 (SD1) receptor kinase 6) (SD1-6) (Q9S972)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of cellular expansion and differentiation.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Cell wall integrity/stress response component
- Rop guanine nucleotide exchange factor 12
Sequence:
MRNVPNYHHSYFILFIIILFLAFSVYASNFSATESLTISSNKTIISPSQIFELGFFNPDSSSRWYLGIWYKIIPIRTYVWVANRDNPLSSSNGTLKISDNNLVIFDQSDRPVWSTNITGGDVRSPVAAELLDYGNFVLRDSKNNKPSGFLWQSFDFPTDTLLSDMKMGWDNKSGGFNRILRSWKTTDDPSSGDFSTKLRTSGFPEFYIYNKESITYRSGPWLGNRFSSVPGMKPVDYIDNSFTENNQQVVYSYRVNKTNIYSILSLSSTGLLQRLTWMEAAQSWKQLWYSPKDLCDNYKECGNYGYCDANTSPICNCIKGFEPMNEQAALRDDSVGCVRKTKLSCDGRDGFVRLKKMRLPDTTETSVDKGIGLKECEERCLKGCNCTAFANTDIRNGGSGCVIWSGGLFDIRNYAKGGQDLYVRVAAGDLEDKRIKSKKIIGSSIGVSILLLLSFIIFHFWKRKQKRSITIQTPIVDLVRSQDSLMNELVKASRSYTSKENKTDYLELPLMEWKALAMATNNFSTDNKLGQGGFGIVYKGMLLDGKEIAVKRLSKMSSQGTDEFMNEVRLIAKLQHINLVRLLGCCVDKGEKMLIYEYLENLSLDSHLFDQTRSSNLNWQKRFDIINGIARGLLYLHQDSRCRIIHRDLKASNVLLDKNMTPKISDFGMARIFGREETEANTRRVVGTYGYMSPEYAMDGIFSMKSDVFSFGVLLLEIISGKRNKGFYNSNRDLNLLGFVWRHWKEGKELEIVDPINIDALSSEFPTHEILRCIQIGLLCVQERAEDRPVMSSVMVMLGSETTAIPQPKRPGFCVGRSSLEVDSSSSTQRDDECTVNQVTLSVIDAR
Protein: Serine/threonine-protein kinase SIK2 (EC 2.7.11.1) (Salt-inducible kinase 2) (SIK-2) (Serine/threonine-protein kinase SNF1-like kinase 2) (Q8CFH6)
Organism: Mus musculus (Mouse)
Function: Serine/threonine-protein kinase that plays a role in many biological processes such as fatty acid oxidation, autophagy, immune response or glucose metabolism. Phosphorylates 'Ser-794' of IRS1 in insulin-stimulated adipocytes, potentially modulating the efficiency of insulin signal transduction. Inhibits CREB activity by phosphorylating and repressing TORCs, the CREB-specific coactivators. Phosphorylates EP300 and thus inhibits its histone acetyltransferase activity. In turn, regulates the DNA-binding ability of several transcription factors such as PPARA or MLXIPL (By similarity). Also plays a role in thymic T-cell development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12624099}.
Interaction partners:
- CREB-regulated transcription coactivator 2
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- CREB-regulated transcription coactivator 3
Sequence:
MVMADGPRHLQRGPVRVGFYDIEGTLGKGNFAVVKLGRHRTTKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKVVHRDLKAENLLLDNNMNIKIADFGFGNFFKTGELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLSIAQIKEHKWMLIEVPVQRPILYPQEQENEPSIGEFNEQVLRLMHSLGIDQQKTVESLQNKSYNHFAAIYFLLVERLKSHRSSFPVEQRLDGRQRRPSTIAEQTVAKAQTVGLPVTLHPPNVRLMRSTLLPQASNVEAFSFPTSSCQAEAAFMEEECVDTPKVNGCLLDPVPPVLVRKGCQSLPSSMMETSIDEGLETEGEAEEDPSQAFEAFQATRSGQRRHTLSEVTNQLVVMPGAGKMFSMSDNPSLESVDSEYDMGSAQRDLNFLEDSPSLKDIMLANQPSPRMTSPFISLRPANPAMQALSSQKREAHNRSPVSFREGRRASDTSLTQGIVAFRQHLQNLARTKGILELNKVQLLYEQMGSNADPTLTSTAPQLQDLSSSCPQEEISQQQESVSSLSASMHPQLSPQQSLETQYLQHRLQKPNLLPKAQSPCPVYCKEPPRSLEQQLQEHRLQQKRLFLQKQSQLQAYFNQMQIAESSYPGPSQQLALPHQETPLTSQQPPSFSLTQALSPVLEPSSEQMQFSSFLSQYPEMQLQPLPSTPGPRAPPPLPSQLQQHQQPPPPPPPPPPQQPGAAPTSLQFSYQTCELPSTTSSVPNYPASCHYPVDGAQQSNLTGADCPRSSGLQDTASSYDPLALSELPGLFDCEMVEAVDPQHNGVVSCLARET
Protein: FAD synthase (EC 2.7.7.2) (FAD pyrophosphorylase) (FMN adenylyltransferase) (Q6FNA9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Riboflavin kinase
- Candida glabrata strain CBS138 chromosome D complete sequence
- Adenylyl-sulfate kinase
- Candida glabrata strain CBS138 chromosome D complete sequence
- Sulfite reductase subunit beta
- Sulfate adenylyltransferase
- Amino-acid acetyltransferase, mitochondrial
Sequence:
MRLGDAAELCYNLTSSYLQIAAESDSIIAQTQRAINTTKSILINETFPKWSPLNGEISFSYNGGKDCQVLLLLYLSCLWEYYIVKLSQSQFDGKFHRFPLTKLPTVFIDHDDTFKTLENFIEETSLRYSLSLYESDRDKCETMAEAFETFLQVFPETKAIVIGIRHTDPFGEHLKPIQKTDANWPDFYRLQPLLHWNLANIWSFLLYSNEPICELYRYGFTSLGNVEETLPNPHLRKDKNSTPLKLNFEWEIENRYKHNEVTKAEPIPIADEDLVKIENLHEDYYPGWYLVDDKLERAGRIKKK
Protein: Serine incorporator 1 (Axotomy-induced glyco/Golgi protein 2) (Membrane protein TMS-2) (Tumor differentially expressed protein 1-like) (Tumor differentially expressed protein 2) (Q9QZI8)
Organism: Mus musculus (Mouse)
Function: Enhances the incorporation of serine into phosphatidylserine and sphingolipids.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q7TNK0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q7TNK0}.
Interaction partners:
Sequence:
MGSVLGLCSVASWIPCLCGSAPCLLCRCCPSGNNSTVTRLIYALFLLVGVCVACVMLIPGMEEQLNKIPGFCENEKGVVPCNILVGYKAVYRLCFGLAMFYLLLSLLMIKVKSSSDPRAAVHNGFWFFKFATAVAIIIGAFFIPEGTFTTVWFYVGMAGAFCFILIQLVLLIDFAHSWNESWVEKMEEGNSRCWYAALLSATALNYLLSLVAVVLFFVYYTHPASCAENKAFISVNMLLCIGASVMSILPKIQESQPRSGLLQSSVITVYTMYLTWSAMTNEPETNCNPSLLSIIGFNTTRPIPKDGQSVQWWHPQGIIGLVLFLLCVFYSSIRTSNNSQVNKLTLTSDESTLIEDGNGRSDGSLDDGDGIHRAVDNERDGVTYSYSFFHFMLFLASLYIMMTLTNWYRYEPSREMKSQWTAVWVKISSSWIGLVLYVWTLVAPLVLTNRDFD
Protein: Protein BCAP (Basal body centriole-associated protein) (Outer dense fiber protein 2-like) (Q9D478)
Organism: Mus musculus (Mouse)
Function: Acts as a suppressor of ciliogenesis, specifically, the initiation of ciliogenesis.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9ULJ1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q9ULJ1}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250|UniProtKB:Q9ULJ1}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9ULJ1}. Note=Localizes to centrioles in proliferative cells and basal bodies in ciliated cells. Disappears during ciliogenesis but reappears, albeit at a lower levels once ciliogenesis has completed. {ECO:0000250|UniProtKB:Q9ULJ1}.
Interaction partners:
Sequence:
MEMPTSDGSLSEGLISYLIRERGSAPQCAPEKHLSRLKQDVANTKMELKATLKEAQLASCSVELLLPLFKNTVEGISLENANLSASSLKKIFEQNDILSKELDTFNRVKLALEHLIKQTDYEQIGDSLLCLLKDLSDNESENRNLEEKVLEKETYIRELSCLFQNEKESALKANRLSQSVKVVHDRLQRQIQKREAENEKLKEHVQSLETQIAKWNLQVKMNKQEAVAIKEASRQKAVALKKASKVYRQRLRHFTGDIERLASQVRDQEAKLSETVSASSDWKSQFEKIAIEKTELEVQIETMKKQIANLLEDLRKMETHGKNSCEEILRKLHSLEDENEALNIENVKLKGTLDALKDEVASVENELVELQEVEKRQKTLVEGYRTQVQKLQEAAEMVKSRCKNLLHENNLIITNKNKKLEKMRGQVESNLKQVEQARSSFTSAEQRLQECQEKLQRCKEKCAEQALTIRELQGQVDGNQSLLTKLSLEEENHLIQLKCENLKEKLEQMDAENKELEKKLADQEECLKHSDLELKEKAAEYTALSRQLEAALEEGRQKVSEEVEKMSSRERALQIKILDLEAELRKKNEEQNQLVDKMNTKTQHQAICLKEIQHSLEKSETRNESIKNYLQFLQISYVTMFR
Protein: Semaphorin-4G (Q9NTN9)
Organism: Homo sapiens (Human)
Function: Cell surface receptor for PLXNB2. May play a role in axon guidance (By similarity).
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Plexin-B2
- Plexin-B1
- Plexin-B3
Sequence:
MWGRLWPLLLSILTATAVPGPSLRRPSRELDATPRMTIPYEELSGTRHFKGQAQNYSTLLLEEASARLLVGARGALFSLSANDIGDGAHKEIHWEASPEMQSKCHQKGKNNQTECFNHVRFLQRLNSTHLYACGTHAFQPLCAAIDAEAFTLPTSFEEGKEKCPYDPARGFTGLIIDGGLYTATRYEFRSIPDIRRSRHPHSLRTEETPMHWLNDAEFVFSVLVRESKASAVGDDDKVYYFFTERATEEGSGSFTQSRSSHRVARVARVCKGDLGGKKILQKKWTSFLKARLICHIPLYETLRGVCSLDAETSSRTHFYAAFTLSTQWKTLEASAICRYDLAEIQAVFAGPYMEYQDGSRRWGRYEGGVPEPRPGSCITDSLRSQGYNSSQDLPSLVLDFVKLHPLMARPVVPTRGRPLLLKRNIRYTHLTGTPVTTPAGPTYDLLFLGTADGWIHKAVVLGSGMHIIEETQVFRESQSVENLVISLLQHSLYVGAPSGVIQLPLSSCSRYRSCYDCILARDPYCGWDPGTHACAAATTIANRTALIQDIERGNRGCESSRDTGPPPPLKTRSVLRGDDVLLPCDQPSNLARALWLLNGSMGLSDGQGGYRVGVDGLLVTDAQPEHSGNYGCYAEENGLRTLLASYSLTVRPATPAPAPKAPATPGAQLAPDVRLLYVLAIAALGGLCLILASSLLYVACLREGRRGRRRKYSLGRASRAGGSAVQLQTVSGQCPGEEDEGDDEGAGGLEGSCLQIIPGEGAPAPPPPPPPPPPAELTNGLVALPSRLRRMNGNSYVLLRQSNNGVPAGPCSFAEELSRILEKRKHTQLVEQLDESSV
Protein: Claret, isoform A (Claret, isoform C) (FI02178p) (Q9VAG5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSGQAELKELGMFELRPLITNISCKLSAVTAGLDEKRQFLCLVSEENEILLRYISAASGQEVVKMISWFRNRVIHDVCFDPAGVWLLVLCFDNTLHIVPALALVDKAHGLSACSLYSTTQVTSYIIPFVGPHECPNSKKCPNHSTGLEESTAEPMDQLAENLEQARLQEGEEEEPLGHDLPEHMLVRNSGTEDAVQPLPQQQQTIDTTGNSQVMAASFMASKTCPYPLSVVWWKTNSGQNRAIIGYSDGSICFVGLSPNCPMIASTAIENGSVMRLVICKDKAYDGVMLLITSSLKQQYKLLLEQKAIKYVYPGDSSPTTREGAWQIVMSVQDKHQSAATGARQSNSSDPASDSSQLEEDVFAPPSSDDVVCSGPGAANSDPSTVSASAEAATADVPPPPAPPSYSEAVARQSGDQGGVRFQQQQLPAGSMDGILPATRARLASLKSLGSKKLQAIKMRLSDQRQKFDEFMPDSTMGSFAIMDSPSVTPEPLGTTSGSFYNIQNLRSTFLLSALHSNSHSLTVHSIDISLKPLFVYKIPKHTQEILISSNILYGIHYVDLHCRSDSDHFTAASLLDDPLVANTEKENRDADIEKVDQSDVSAQKSDSTSATTTATSSLDQSDMPSTAINAVSVISSAMASLHTSDEDRFNNLAQLGLFRFENETVLHLYQMAQYRNPSAEPETLTKEEKAKAFELKDIHTPMDYIQFYETADVSSEFSLRQMEIMQSEFPKINYDPSYVITNKNVYTIQLKKEPFELFLDAALQNEFNQCRDFCNTFDLSFEQCIEFAGDYLLRRKKITQALLTYNKARVKPIRTALKLAMYGHTYALMQLSAMALKSTYLLRSRYLGHPLLKGILGDITYRHSEDVRVILPEKHEEEDVNSGVFCSDYHYGVDESISALQMSPSSQFHLANLLLITLAEKAVNDKNYIPLWNFLVTNSKYHTNMTSIVLCQSGLFSSAIILAKIRGVCLDTFNALISVVAQEFGWYNELNVCLYNLSENIFLETITYLPHVSMDYFAFIQEKLHHIRPCVLQRLSKQLNPFSPALRPIVSHNSDCAMSNDNNPQLFEFCKSLIETYLAVLIHMESQRVKYDSIVNALSNFRINYEDNQFAIESSRFKPISAGCAYCACVVDGTAYFWGSSGIPSYYSAQKSTEPPEPAHAVKSLDLLSQLNLQVHAIKCGRQHTLILTNNGLYSLGNNNLCQLGIGRHMQMALQPMLVTALDGMNITMLEAGQYHNAAVADGKLYMWGWGIYGQLGQGSCENIATPQLVSFFKFKKILQISLGHAHTLVLCGAPNSHMEANHCGNELFVFGSNHFGQLGTGNSDHGDTKTNLPVRLEVGDCSLRLIHTKFFTNLAVDEQDRLFTWGSSPQALRLANQIKRRANAKQKMEENQQRELLSKQLEATLLPAPIPSTSTLVEPTTSYAAVVAGSTPKSSVSDTKDCQDVQNEAAPSDATETIAPASAKAAPPPVPVASPPVLVPEPDPTEHLTPHLVDTSEVAGRILQISSGLFHFCLISSSCTLYTWGKNLEHQLGTEDKDRRAVLKPSPIDSIERPMYVDCGSDFTLVMTTDHVVRAFGGNSNGQCGRDLGPSVERMRQRVVCLPATKRLVRFESQCVEVPVEINLPRPRIRLDQDPVRYLKVMPPYQPHFLQPANISFDQHCSVGTPNYKSSTEHAATGQDSDDMLSSLENLSQNDASFSYNAPVLGDAHSSLDMDYTPEEQSYVPLPEQAVGSGMPANAEQLLGRDDDDGSTYTQSTEGMGESSLQHLRHYIHYCLYAFHGLYNPDKIGECARPHRNEYRIRICMLNFRFVEAFRLCLQSCGSAQRTLKLFEYFSKDTGYVPLRRTDLKHLIYHLCLHFLERKFDMLECERFFMGDLDYYLLELAYVFYFNNNNSTLEQNLNQKFKQLIAAADSNQAATSAGQELEQLQDTDVIFDSFTVKFKTILCQRLLSYSDCDAAN
Protein: Xanthine dehydrogenase/oxidase (EC 1.17.1.4) (EC 1.17.3.2) (M1ZMM0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- Beta-carotene oxygenase 1,-like.
- Sulfite oxidase, mitochondrial
- Aldehyde dehydrogenase 1 family member A3
- Uncharacterized protein LOC393330
- Beta-carotene oxygenase 1.
- Cytochrome P450, family 3, subfamily A, polypeptide 65
- Aldehyde dehydrogenase 1 family, member A2
- Cytochrome P450 26C1
- Cytochrome P450 1A
- Acyl-CoA synthetase family member 3
Sequence:
MSSLSVNSELVFYINGKKIVEKNADPEEMLLAYLRRKVGLTGAKYGCGGGGCGACTVMVSRYDPLQDTVLHWSVNACLQPICSLHGAAVVTVEGIGSTKTKLHPVQERIVKAHGSQCGFCTPGMVMSMYTLLRNNPHPTIEDIRETLGGNLCRCTGYRPIIDGFKTFCETPVCCQNGGGNGKCCMENGNSHNESDISGELFIMDNVLPLDPTQDLIFPPELLIMGKKKAERHCFQGEKVRWISPSDLKDLIKLKAEHSDAPLLVGNTTIGPKMNLNKTVHPLVIYGGSIAELQAIKWRKNCITVGAGCSLSVLKDVLQQRIEDLGPEKSRVYQALVQTLQCLAGKQIRNMATIGGNILSANPKYDLSSILAAAECTLHIASKDGDREICLSEEFFTDFGKTALRPEEILLAIDIPHSKPWEFVSAFRQAQRREFAFSIVNAGMRVAFRHDSNVVEHLDIFYGGVGCTLVKARHTCKELIGRKWDEKLLAEGTQLLEEEISVPATVPGGREEYRKALVLSFFFKFYMQVLLELQQREVGVNDLPLEYLSALKPFKNEVPQGNYSYQLVPETQSSSDPVGRPNVHLAALQQATGEAVYYDDIPSVKGELFVSMVTSTRAHAKIISIDASVALAMPGVVDFISAKDVPGQNRRLWFNNPEELFAEEEVICVGQIIGAIVAETREQAKRAAQQVDITYQDMQPVFFTIEEAIEHESFFDPKRKLERGNVEEGFAKADQILEGEMYMGGQEHFYMETQGVIAIPTGEASEIELYVASQHAAYTQEVVGITLGIDSNKITCHVKRLGGGFGGKVMKIASLSAIAATAAIKTGHAVRCVLERGDDMLITSGRSPFLGRYKIGYMNDGTILAADITYYSNGGCTLDESSFIMEKALLHMDNGYKIPNLRGRGLVCKTFLPSYTAFRGFGGPQGLTIIESVLHEVAVKCGLPAHQVRDINLYKEEKCFTHHKQLFSPHDMVRCWNECLEKSNYTQRCQYIEQFNGHNHWKKRGISIVPIKFGIGFSKGFYNQGAALVNVYKDGSVVISHGGTEMGQGINTKAIQIASRILKVSMSSIHIKETCTGNVPNAAPSAASFGTDAVGMAVKNGCEKLMRRLEPLIKKHPQYTWQQLVVEAYCQKISLSATGFFMGPHTSVDWEKSEGNAYYYFTFGACCSEVEIDCLTGDHKNIRTDIVMDVGRSINPALDVGQVEGGFVQGIGLYTIEELQFSPQGVLLTRGPSQYKIPALCDVPPQINVHLLRNADNPHAIYSSKGIGEPPVFFGCTLFFAIKEAIAAARKERGLSESFSFSSPATAEKIRMACEDCFTRMIPQDKKVKTKPWAINV
Protein: ABC transporter G family member 28 (ABC transporter ABCG.28) (AtABCG28) (Putative white-brown complex homolog protein 29) (AtWBC29) (Q9FF46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- ABC transporter F family member 1
Sequence:
MGRRNSYFPGNFVPLFFVFIVLILQQERVICQEDRSLDNPAANRLYNQFVFDKISNLTEVFEDDIKRELGFCITNVKEDYNEAFNFSTKPDFLNACGKTTKGDMMQRICTAAEVRIYFNGLLGGAKRATNYLKPNKNCNLSSWMSGCEPGWACRTAKDVKVDLKDDKNVPVRTQQCAPCCAGFFCPRGITCMIPCPLGAYCPEANLNRTTGLCDPYHYQLPSGQPNHTCGGADIWADIGSSSEVFCSAGSFCPSTIDKLPCTKGHYCRTGSTAELNCFKLATCNPRSTNQNITAYGIMLFAGLGFLLIILYNCSDQVLATRERRQAKSREKAVQSVRDSQSREKWKSAKDIAKKHATELQQSFSRTFSRRKSMKQPDLMRGLSQAKPGSDAALPPMLGSSSDTKKGKKKEKNKLTEMLHDIEQNPEDPEGFNLEIGDKNIKKHAPKGKALHTQSQMFRYAYGQIEKEKAMQEQNKNLTFSGVISMANDIDIRKRPMIEVAFKDLSITLKGKNKHLMRCVTGKLSPGRVSAVMGPSGAGKTTFLTALTGKAPGCIMTGMILVNGKVESIQSYKKIIGFVPQDDIVHGNLTVEENLWFSARCRLPADLPKPEKVLVVERVIESLGLQHVRDSLVGTVEKRGISGGQRKRVNVGLEMVMEPSLLILDEPTSGLDSSSSQLLLRALRREALEGVNICMVVHQPSYTLFRMFDDLILLAKGGLICYQGPVKKVEEYFSSLGIVVPERVNPPDYYIDILEGILKPSTSSGVTYKQLPVRWMLHNGYPVPMDMLKSIEGMASSASGENSAHGGSAHGSVVGDDGTSFAGEFWQDVKANVEIKKDNLQNNFSSSGDLSEREVPGVYQQYRYFLGRLGKQRLREARTLAVDYLILLLAGICLGTLAKVSDETFGAMGYTYTVIAVSLLCKITALRSFSLDKLHYWRESRAGMSSLAYFLAKDTVDHFNTIVKPLVYLSMFYFFNNPRSTVTDNYVVLICLVYCVTGIAYTLAILFEPGPAQLWSVLLPVVLTLIATSTNDNKIVDSISELCYTRWALEAFVVSNAQRYKGVWLITRCGSLMENGYNIKHFPRCLVFLTLTGILSRCAAFFCMVTFQKK
Protein: CCHC-type domain-containing protein (Q38DE2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ATP-dependent DEAD/H RNA helicase, putative
- Exosome component CSL4
- Ribosomal RNA-processing protein 43
- Ribosomal RNA processing protein 45
- Ribosomal RNA processing protein 4
- RNasePH-like protein exosome-associated protein 1 Rrp42 homologue
- Exosome complex exonuclease RRP40
- U3 small nucleolar RNA-associated protein 14
- Sas10 C-terminal domain-containing protein
- Bms1-type G domain-containing protein
Sequence:
MFRTIGIVRLWRTSRIVRLPASGLGTDAKSCTAPTQPLSTSSATSSSSMILKYPYRVVDTHEKLKEAVTSLQGARSIALDIEAFCTTDQAKQLGRISLVQACSDAKPVVFLFDVLTLTPDVFVKDMQSLLSDREIRKLFFDCRRDVEALSCQLGVKPEGVLDLQVFFTAIQWKLRSVNRRSGMGYVLKSVAGLTRQEGDSAVQTAMTLGNRPVWDIRPLPDHFLEYAAGDVRHILLLSNYLVGNKDVPVDVVAVERLTAQYVEHYAVGKPVITEADATPAEVNRAWLERYIGPGGGCHFCGAKGHTEAECFKKQNGKAKCSFCGEVGHTARNCFKKHPQLLTCEKCGQLGHTGTSCFRTNPCKHCGGPHSSANCHKVIWQQKRLGENSLH
Protein: Glutamate carboxypeptidase 2 (EC 3.4.17.21) (Cell growth-inhibiting gene 27 protein) (Folate hydrolase 1) (Folylpoly-gamma-glutamate carboxypeptidase) (FGCP) (Glutamate carboxypeptidase II) (GCPII) (Membrane glutamate carboxypeptidase) (mGCP) (N-acetylated-alpha-linked acidic dipeptidase I) (NAALADase I) (Prostate-specific membrane antigen) (PSM) (PSMA) (Pteroylpoly-gamma-glutamate carboxypeptidase) (Q04609)
Organism: Homo sapiens (Human)
Function: Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Involved in prostate tumor progression.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9809977}; Single-pass type II membrane protein {ECO:0000269|PubMed:9809977}.; SUBCELLULAR LOCATION: [Isoform PSMA']: Cytoplasm {ECO:0000269|PubMed:9809977}.
Interaction partners:
- Prostate-specific antigen
- Aspartoacylase
- Beta-citrylglutamate synthase B
- N-acetylaspartylglutamate synthase A
- N-acetylaspartate synthetase
- Prostate stem cell antigen
- N-acetylated-alpha-linked acidic dipeptidase 2
- Receptor tyrosine-protein kinase erbB-2
- Gastrin-releasing peptide receptor
- Folate receptor alpha
Sequence:
MWNLLHETDSAVATARRPRWLCAGALVLAGGFFLLGFLFGWFIKSSNEATNITPKHNMKAFLDELKAENIKKFLYNFTQIPHLAGTEQNFQLAKQIQSQWKEFGLDSVELAHYDVLLSYPNKTHPNYISIINEDGNEIFNTSLFEPPPPGYENVSDIVPPFSAFSPQGMPEGDLVYVNYARTEDFFKLERDMKINCSGKIVIARYGKVFRGNKVKNAQLAGAKGVILYSDPADYFAPGVKSYPDGWNLPGGGVQRGNILNLNGAGDPLTPGYPANEYAYRRGIAEAVGLPSIPVHPIGYYDAQKLLEKMGGSAPPDSSWRGSLKVPYNVGPGFTGNFSTQKVKMHIHSTNEVTRIYNVIGTLRGAVEPDRYVILGGHRDSWVFGGIDPQSGAAVVHEIVRSFGTLKKEGWRPRRTILFASWDAEEFGLLGSTEWAEENSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVHNLTKELKSPDEGFEGKSLYESWTKKSPSPEFSGMPRISKLGSGNDFEVFFQRLGIASGRARYTKNWETNKFSGYPLYHSVYETYELVEKFYDPMFKYHLTVAQVRGGMVFELANSIVLPFDCRDYAVVLRKYADKIYSISMKHPQEMKTYSVSFDSLFSAVKNFTEIASKFSERLQDFDKSNPIVLRMMNDQLMFLERAFIDPLGLPDRPFYRHVIYAPSSHNKYAGESFPGIYDALFDIESKVDPSKAWGEVKRQIYVAAFTVQAAAETLSEVA
Protein: Purine nucleoside phosphorylase Rv2149c (EC 2.4.2.1) (Adenosine deaminase Rv2149c) (EC 3.5.4.4) (S-methyl-5'-thioadenosine phosphorylase Rv2149c) (EC 2.4.2.28) (P9WKD5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity.
Interaction partners:
- Pyridoxal phosphate homeostasis protein
- Cell division protein SepF
- Probable peptidoglycan glycosyltransferase FtsW
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Cell division protein FtsZ
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- UDP-N-acetylmuramate--L-alanine ligase
- Penicillin-binding protein PbpB
- Cell division protein FtsQ
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
Sequence:
MLASTRHIARGDTGNVSVRIRRVTTTRAGGVSAPPFDTFNLGDHVGDDPAAVAANRARLAAAIGLPGNRVVWMNQVHGDRVELVDQPRNTALDDTDGLVTATPRLALAVVTADCVPVLMADARAGIAAAVHAGRAGAQRGVVVRALEVMLSLGAQVRDISALLGPAVSGRNYEVPAAMADEVEAALPGSRTTTAAGTPGVDLRAGIACQLRDLGVESIDVDPRCTVADPTLFSHRRDAPTGRFASLVWME
Protein: FMRFamide receptor (DFR) (DrmFMRFa-R) (Q9VZW5)
Organism: Drosophila melanogaster (Fruit fly)
Function: A receptor for the FMRFamide peptides. Reacts with high affinity to FMRFamide and intrinsic FMRFamide-related peptides. By stimulating intracellular calcium signaling through the inositol 1,4,5-trisphosphate receptor, Itpr, in dopaminergic neurons, may be involved in the maintenance of neuronal excitability and in the regulation of flight bout duration.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- POU domain protein CF1A
Sequence:
MSGTAVARLLLRLELPSPGVMPPPPTDYDYGGPISDDEFLASAMATEGPTVRYDLFPQNNSQPTLQIVLNHTEVQTDLQYPHYEDLGLDPDPNWTRICEDVYNPLLENNRIEFWVCGVLINIVGVLGILGNIISMIILSRPQMRSSINYLLTGLARCDTVLIITSILLFGIPSIYPYTGHFFGYYNYVYPFISPAVFPIGMIAQTASIYMTFTVTLERYVAVCHPLKARALCTYGRAKIYFIVCVCFSLAYNMPRFWEVLTVTYPEPGKDVILHCVRPSRLRRSETYINIYIHWCYLIVNYIIPFLTLAILNCLIYRQVKRANRERQRLSRSEKREIGLATMLLCVVIVFFMLNFLPLVLNISEAFYSTIDHKITKISNLLITINSSVNFLIYIIFGEKFKRIFLLIFFKRRLSRDQPDLIHYESSISNNGDGTLNHRSSGRFSRHGTQRSTTTTYLVATGGPGGGGCGGGGGNNSLNNVRLTQVSGSPGLVKIKRNRAPSPGPVVYFPAREMQRSASTTNSTTNNNTSIGYDWTLPDSKKLGHVSSGF
Protein: Probable biotin sulfoxide reductase BisC (BDS reductase) (BSO reductase) (O06817)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Biotin--[acetyl-CoA-carboxylase] ligase
- Biotin synthase
- Cytochrome bc1 complex cytochrome c subunit
- Elongation factor Tu
- Glutamate synthase large chain
- R2-like ligand binding oxidase
Sequence:
MQVYTSATHWGVFTARVHGGDIAAVAALASDTNPAPQLQNLPGAVRHRSRIANPAVRRGWLQHGPGPSSARGAEEFVEVSWDELIELLASELRRTVDRYGNEAIYGSSYGWASAGRFHHAQSQVHRFLNMLGGYTASRHSYSAGASEVIFPHIVGAALFEALAETTTWDVIVDHTALLVAFGGLPVKNTAVMPGGTTAHPDRDYVGRYRARGGRLVSVSPLRDDIAAIAGPLDDRCRWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCTGYERFERYLLGLDDGIPKTPEWAAALSGLAAGDLRDLARRMAEHRTLITTSLSLQRIEHGEQTVWMAATLAAMLGQIGLPGGGFGHGYSSNGVGNPPLACGLPALPQGNNPVSTFIPVAAISELLQRPGQRLAYNGRLLELPDIKCVYWAGGNPFHHHQNLPRLRRALSRVDTIVVHEQYWTAMAKHADIVVPTTTSFERDDFAASKTNPTLIAMPAMVPPYANARDDYHTFSALAHRLGFGKQFTEGRSAREWLEHMYDKWSAELDFPVPSFAEFWRTGRLELPTRTGLTWLADFRADPAAHPLGTPSGRIEIFSDTVDAFALPDCAGHPTWYEPSEWLGGPRAARYPLHLIANQPRTRLHSQLDHGGASMASKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQLSTGAWFDPADPRDPDSMCVHGNPNALSNDSGTSSLAHGSTGQHVLVQIERFTGELPPVRAHEPPRLA
Protein: Calreticulin (Q23858)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Subcellular location: Endoplasmic reticulum lumen.
Interaction partners:
- Endoplasmin homolog
- Luminal-binding protein 1
- Luminal-binding protein 2
- Calnexin
- Protein disulfide-isomerase 2
- J domain-containing protein
- 116 kDa U5 small nuclear ribonucleoprotein component
- Probable UDP-glucose:glycoprotein glucosyltransferase A
- J domain-containing protein
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
Sequence:
MRLLLCLIFLVFVFNFALSTVHFKDTFDNDWESRWVVSDWHKEDGKSGKLVHTAGKWFGDENQKGIQTSEDARFYAVSAKFPSFSNKGKDLVLQYTVKNEQKVDCGGSYIKLLPSKLDQSAFDGESEYSIMFGPDVCGASKRVHVILNYKGKNHLIKKEINKVETDQLTHQYTLVISPDNTYKVLVDNKEIQAGNLADDWELLPSKQIKDPKQSKPVDWVDVKEIDDPEDVKPAGHDDIPASIVDPEAVKPEDWNEEDDGEWEAPTIANPEYKGEWKAKKIPNPEYKGEWVHPLIDNPEYAEDNELYLFNDLGAIGFELWQVKSGSIFNNMIVTDSVEEAKDFSEKTFVANQEAEKKMFDDLEAAKAEERKKADEKLAAEKAAEKEAEEADEEEEEVAEEDLVKTDDKKEEVKKSTKKVDHDEL
Protein: Ion transport domain-containing protein (Q8MXH5)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLSSQHKKPVRSSYVESDRVEWALKIACTISMITVCIHTPRTIELFQPLNYIILAADFISVSIFMLDSVLRIHYEGIFRCDSSYLSNRWSQFSVFISIIHLLSFLLHCYQLIDNFFPFLHLNYRAWYGAIRSIRPFIIIRLIPLVVKFKLPKNRIEQLLKRSSQQVKNVTLFFVFFMTLYAIFGIQLFGRMDYHCVQPKTDPNNVTIMDLAIPDTMCAPEGIGGYECPAPMVCMQLNLNAKGEGFYGMFNDFGASVFTVYLAASEEGWVYVLYDCMDSLPSYLAFLYFCTLIFFLAWLVKNVFIAVITETFAEIRVQFSEMWQKKEVTLDEGFRKKLEKTDDGWRLIRLDGEVEPEGPKQKLQWMLRSMYFQCFVIIFVVINAIGNAMFVYRHDETDKPRKYNFYLFEVGFTILFNVECIIKILCYGFRNFIRRGIFKFELILCLGSSLNCVKFFYERNYFTYFQTFRLLRLIKASPILEDFVWKIFSPGKKLGGLVIFTIAFICCYSAISLQLFYSVPNLHHFRTFPQAFMSMFQIITQEGWTDFVVEVLRATDDNLVPLVALYFVAYHLFVTLIVLSLFVAVILDNLEMDEELKKVKQLRAREATTSMRSTLPWRLRVFEKFPTRPQMAAMRKADSDFPMPKVRGSFTHQFAVDHSLETTDVIESDFEFPKRIMKSAGKRKISKSGLTFRQIGSTSLRCSLNNLLEMSDRTRQSLSNSLSFLPHFTRSSGSLYPRKDALPKSRSMTGKFLQTAVRNKQFNMYSENGDLSRPSDSAPKKNAKQGEIDIRALQQKRQLAEITRNRIEEDMRENHPFFDRPLFLVGRASQLREFCKKMVHSKYDSQDDGTNGGAKTKKRFKEIRALIGIMPYIDWAMATVTIVSCISMLFESPWPTTGENLVMNNGYLQISDYFFVLSMTFELCVKIIANGLFFTPKAVVRDVGGVMNLFIYFTSVIFLAWMPKHVEINSLAQFLMICRAMRPLRIYTLVPHIRRVVLEFFRGFKEILLVTILMIVVMFIFASFGVQIVGGKLAACNDPTVSSRENCTGVFWQKLFVTRLEVYGKDTEAMHPKIMVPRVWTNPRNFNFDHVGNAMLALFETLSFKGWNVIRDILWSRHGPWAVVFIHIYVFIGCMIGLTLFVGVVIANYTQNRGTALLTVDQRRWHDLKARLKMAQPLHVPPKPSESARLRTKLYDLTMSRWFNQAFALLVVLNSFTLVIPWNVEEEEQRATYVFTVTALAAFMNMLFVIEIILKVIAYTFSGFWQSRRNRVDLLITVFGVIWIFLHFFVALPSSKIDVDVQVELKKFTYTFGYLVVILRFFTIASRNSTLKMLMLTVIMSMFRSFFIITALFLLVLFYAYTGVILFPMVKYGMAVSKHVNFRTASEALVVLFRCLTGEDWNDIMHDCMRSAPFCYWNEGMNYWETDCGNFYGAIIYFCSFYLIITYIVRNLLVAVIMENFSLFYSSEEDALLSYADIRNFQYVWNMVDQEQKRTIPVERVKFLLRLLKGRLEVDPEKDRILFKHMCYEMERLHNGEEVSFHDVLYMLSYRSVDIRKSLQLEELLQREELEFIIEEEVAKQTIRTWLEGCLRKMRNPSQKDAEGVLPFGGGHPVIHSSGHSSISHEETVAQRLRFENIRGDSVDTEETESSEEETPPPIRKKAAVKNRRGSIPDVLSRTGLFQEAARKFMVGSSSEKKQVKSRSPETVQLLPKRANSEIRKGSGQPKNFHLQLNVYDLPDVEERGEDSPFSPKNLSDDFNGEHSPLVITPSLPVPPTHGSPRPLMPCETTKDIEKWWNSLVD
Protein: F-box protein 2 (A0A8I5ZK45)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
GEGEGERERERRRGRERSVSHPEEASPEEQPEEAGAEASAEEEQPREEEEEETEAVEYLAELPEPLLLRVLAELPATELVQACRLVCLRWKELVDGAPLWLLKCQQEGLVPEGSADDERDHWQQFYFLSKRRRNLLRNPCGEEDLEGWCDVEHGGDGWRVEELPGDSGVEFTHDDSVKKYFASSFEWCRKAQVIDLQAEGYWEELLDTTQPAIVVKDWYSGRTDAGSLYELTVRLLSEHEDVLAEFNTGQVAVPEDGSWMEISHTFTDYGPGVRYVRFEHGGQDSVYWKGWFGARVTNSSVWVEP