wanglab/gogpt-training-data huggingface dataset:
Protein: Oligopeptide transporter 1 (High affinity glutathione transporter 1) (P40897)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: High affinity transporter for glutathione. Also transports tetra- and pentapeptides like the opioids leucine enkephalin (Tyr-Gly-Gly-Phe-Leu) and methionine enkephalin (Tyr-Gly-Gly_Phe-Met) across the cell membrane.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Peptide transporter PTR2
- Glutamate--cysteine ligase
- Homocysteine/cysteine synthase
Sequence:
MSTIYRESDSLESEPSPTPTTIPIQINMEEEKKDAFVKNIDEDVNNLTATTDEEDRDPESQKFDRHSIQEEGLVWKGDPTYLPNSPYPEVRSAVSIEDDPTIRLNHWRTWFLTTVFVVVFAGVNQFFSLRYPSLEINFLVAQVVCYPIGRILALLPDWKCSKVPFFDLNPGPFTKKEHAVVTIAVALTSSTAYAMYILNAQGSFYNMKLNVGYQFLLVWTSQMIGYGAAGLTRRWVVNPASSIWPQTLISVSLFDSLHSRKVEKTVANGWTMPRYRFFLIVLIGSFIWYWVPGFLFTGLSYFNVILWGSKTRHNFIANTIFGTQSGLGALPITFDYTQVSQAMSGSVFATPFYVSANTYASVLIFFVIVLPCLYFTNTWYAKYMPVISGSTYDNTQNKYNVTKILNEDYSINLEKYKEYSPVFVPFSYLLSYALNFAAVIAVFVHCILYHGKDIVAKFKDRKNGGTDIHMRIYSKNYKDCPDWWYLLLQIVMIGLGFVAVCCFDTKFPAWAFVIAILISLVNFIPQGILEAMTNQHVGLNIITELICGYMLPLRPMANLLFKLYGFIVMRQGLNLSRDLKLAMYMKVSPRLIFAVQIYATIISGMVNVGVQEWMMHNIDGLCTTDQPNGFTCANGRTVFNASIIWSLPKYLFSSGRIYNPLMWFFLIGLLFPLAVYAVQWKFPKFKFAKHIHTPVFFTGPGNIPPSTPYNYSLFFAMSFCLNLIRKRWRAWFNKYNFVMGAGVEAGVAISVVIIFLCVQYPGGKLSWWGNNVWKRTYDNDYKKFYTLKKGETFGYDKWW
Protein: E3 ubiquitin-protein ligase RLIM (EC 2.3.2.27) (LIM domain-interacting RING finger protein) (RING finger LIM domain-binding protein) (R-LIM) (RING finger protein 12) (RING-type E3 ubiquitin transferase RLIM) (Renal carcinoma antigen NY-REN-43) (Q9NVW2)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase. Acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex-related dosage differences of X-encoded genes in somatic cells of female placental mammals.
Subcellular location: Nucleus {ECO:0000269|PubMed:19117995, ECO:0000269|PubMed:19164295}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 E2
- Ubiquitin-conjugating enzyme E2 D2
- Polyubiquitin-C
- Axin-2
- Ubiquitin-ribosomal protein eL40 fusion protein
- LIM domain-binding protein 1
- Ubiquitin-conjugating enzyme E2 D1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-B
- UBX domain-containing protein 1
Sequence:
MENSDSNDKGSGDQSAAQRRSQMDRLDREEAFYQFVNNLSEEDYRLMRDNNLLGTPGESTEEELLRRLQQIKEGPPPQNSDENRGGDSSDDVSNGDSIIDWLNSVRQTGNTTRSGQRGNQSWRAVSRTNPNSGDFRFSLEINVNRNNGSQNSENENEPSARRSSGENVENNSQRQVENPRSESTSARPSRSERNSTEALTEVPPTRGQRRARSRSPDHRRTRARAERSRSPLHPMSEIPRRSHHSISSQTFEHPLVNETEGSSRTRHHVTLRQQISGPELLSRGLFAASGTRNASQGAGSSDTAASGESTGSGQRPPTIVLDLQVRRVRPGEYRQRDSIASRTRSRSQTPNNTVTYESERGGFRRTFSRSERAGVRTYVSTIRIPIRRILNTGLSETTSVAIQTMLRQIMTGFGELSYFMYSDSDSEPTGSVSNRNMERAESRSGRGGSGGGSSSGSSSSSSSSSSSSSSSSSSSSPSSSSGGESSETSSDLFEGSNEGSSSSGSSGARREGRHRAPVTFDESGSLPFLSLAQFFLLNEDDDDQPRGLTKEQIDNLAMRSFGENDALKTCSVCITEYTEGNKLRKLPCSHEYHVHCIDRWLSENSTCPICRRAVLASGNRESVV
Protein: RE49895p (TweedleD) (Q9VBD2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Mucin 91C, isoform A
- Cuticular protein 65Ea
- TweedleB
- LD21452p
- GEO07425p1
- DUF4766 domain-containing protein
- Protein obstructor-E
- Pro-resilin
- Cuticular protein 67B
- RE24507p
Sequence:
MRAFIVLCLLAVSCSADKLGYNYQPVAHADEGLSFLPGSGQVIGELPSQVLPVQSGEAVLSQPIEAPVAPQIAPLVEEFQKEFYSYAAPEEQYDEGASNQQIANSLKKNLRVVFIRTPENQGFERAALQLAKQSAQQETAIYVLTKQSDVSNLAKQLNALKTSSTNKPEVHFVKYRTPEDAANAQLAIQNQYNQLPGVSRISNEGRAPVLNFASSPAQAAAIPAVAAAAPSSEYLPANVVAGQDYLPPNLRRFRVK
Protein: Putative endonuclease segB (EC 3.1.-.-) (Endodeoxyribonuclease segB) (P13325)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Probably involved in the movement of the endonuclease-encoding DNA.
Interaction partners:
Sequence:
MFYYTYKITNKINNKIYIGVHSTENLDDGYMGSGKLLKRAQDKYGIENFSKEILEYFDDKESMLEAEKNIVTEEFLNRPDVYNLKLGGEGGWDHVNIPGMLNQKKDASLKGAKSFKSRFENDILLQEKYRKIGSNVFKRLWSTPEYREKFLNNSRFLNKHHTPETINKMKESHAKNNHQKGEKNSQFGMMWIHSLDEKVSKRIKKTDPIPEGWFKGRKMKF
Protein: Adhesion G-protein coupled receptor G1 precursor (EC 2.7.11.25) (Fc49b10 G-protein coupled receptor) (Q59I63)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNQNPAKTARMWIIICLLFVLGQATDNDRDFKMCGKWLHGIAPQNLEYDLKTGCERIEISANESTLSIQGRITAKCTQSSSIQLDSNPHQNQSHFCVFWEPLLDLLIVEVNGKNHTLCKPNGLQGTCCTDLSQGVQDNAHMYGIVNGSVKGDIITGDLKGNYIFDGAHINCKEKFCDEARLKPRGANMIEEVVMRFNAKGRVDLPCAQGTVIEMDEEFTGHNFTVPAPRFVDANTIPSVYIPSSLRSVSRRKSKVVCTYYKNKTLFERGPSKSALLDDIVGLSVENETIRNLIEPVKIRFHHRPFAPDSSGRCVSWDTKQDNEVNWKDDGCDTVKINEEQTECHCNHLTYFAILVQVEQKSTVRHLKALTFITAVGCAVSLVSCLVLFYWLCKRRRGKKNQISLVHRGLVVAIFLLCLFFILTGILANVANETVCQLTGSLLHYGLLSTLCWMAMEVFHTFLLVRKVFNSPLPIWIFYLMGFGFPFLLVSILLSVGDIYGERKIKPSDDVNNPYRMCWMTEGDKSQLAHYIINIGLLAVVVSSGLVMLFLVVREIRNRPDWKKIHVAFLSIWGLTCLYGTTWALGFLDFGPFSEVTLFLFCIINSLQGFFLMLRYYALERMKKKDVSSSDGSSSGSSKQHMLQTNEKS
Protein: Neuropeptide SIFamide (Q6IGX9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Ligand for the neuropeptide SIFamide receptor. Modulates sexual behavior by negatively regulating female receptivity to male courtship and by playing a role in male sex discrimination. Also involved in promoting sleep.
Subcellular location: Secreted {ECO:0000305|PubMed:16378592}.
Interaction partners:
- Neuropeptide SIFamide receptor
- Diuretic hormone 44, isoform A
- Short neuropeptide F
- Eclosion hormone
- FMRFamide-related peptides
Sequence:
MALRFTLTLLLVTILVAAILLGSSEAAYRKPPFNGSIFGKRNSLDYDSAKMSAVCEVAMEACPMWFPQNDSK
Protein: Origin recognition complex subunit 6 (Origin recognition complex, subunit 6) (Q6ZM36)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Origin recognition complex subunit 3
- Origin recognition complex subunit 4
- Origin recognition complex subunit 5
- Cell division control protein
- Origin recognition complex subunit 1
- Origin recognition complex, subunit 2.
- Chromatin licensing and DNA replication factor 1
- DNA replication licensing factor MCM7
- Protein DBF4 homolog A
- DNA replication licensing factor MCM4
Sequence:
MDKELFRKLASKIGITSIKVLSQAEEYMRLSQVKCVGLGSGTATSKAVICLELAATAMKFPLDKEYAIKLSGLNPKVYSSNLKTMECMLGLQSNLGLRDLAVQFGCLEAVKVASQILQRYETSLPAAQQQDLDLTKPLFTTAALYTACKCMKIRTDRKLASSSGAKKSIFDRLCAQFQKFGQEICNEASSLEKPVKGTQKRQKTLTEMLEMEDDDKPLTSPKQERVEKTEEEETHHYEEWKRKILENALKAKAVDS
Protein: F-box/WD repeat-containing protein pof11 (Meiotically up-regulated gene 156 protein) (Q09855)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Suppressor of kinetochore protein 1
- RING-box protein pip1
- Cullin-1
- Cullin-3
- Serine/threonine-protein kinase plo1
- Ubiquitin-like protein 1
- M-phase inducer phosphatase
Sequence:
MNQDDNGKNVVSKVSDLTSCSDFSTSSPVPCLNPLSHENNRIDLIRDLLASLSKEGVVAVYNHVRSLLFTDFTEVFPEEVSLRVFSYLDQLDLCKCKLMSKRWKRLLEDPGIWKALYMQKGWFVNENVLNEFEAWRRTHKFPQPRFENFLKQQNIIGPYGTMFLPQQFIFDSNGRPLLNWSYLYKEHAHLDSNWRHGRFLVSTFNNPSIRFPADQDFRATLDSVYCVQYDDEIMVSGSKDRTVSVWDVNSRFILYKLYGHSGSVLCLDFCRRRNLLVSGSSDSTIIIWDWQNRRPLKVYFGHTDNVLGVVVSENYIISSSRDHTARVWRLDATSPAEACMHVLRGHLASVNSVQYSSKTGLIVTASSDRTLRTWDITTGHCIRIIHAHQRGIACAQYNGKFIVSGSSDLTIRIFEASSGKLLRMLQGHEDLIRTVRFNDEKIVSGGYDGTVRIWNFNTGEQHCVLHNSRNSRVFGLQFDHRRIIACTHSSEILVWNFDDGLDCTFF
Protein: Disintegrin and metalloproteinase domain-containing protein 28 (ADAM 28) (EC 3.4.24.-) (Epididymal metalloproteinase-like, disintegrin-like, and cysteine-rich protein II) (eMDC II) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein L) (MDC-L) (Q9UKQ2)
Organism: Homo sapiens (Human)
Function: May play a role in the adhesive and proteolytic events that occur during lymphocyte emigration or may function in ectodomain shedding of lymphocyte surface target proteins, such as FASL and CD40L. May be involved in sperm maturation.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
Interaction partners:
- Leucine-rich glioma-inactivated protein 1
- Disintegrin and metalloproteinase domain-containing protein 22
Sequence:
MLQGLLPVSLLLSVAVSAIKELPGVKKYEVVYPIRLHPLHKREAKEPEQQEQFETELKYKMTINGKIAVLYLKKNKNLLAPGYTETYYNSTGKEITTSPQIMDDCYYQGHILNEKVSDASISTCRGLRGYFSQGDQRYFIEPLSPIHRDGQEHALFKYNPDEKNYDSTCGMDGVLWAHDLQQNIALPATKLVKLKDRKVQEHEKYIEYYLVLDNGEFKRYNENQDEIRKRVFEMANYVNMLYKKLNTHVALVGMEIWTDKDKIKITPNASFTLENFSKWRGSVLSRRKRHDIAQLITATELAGTTVGLAFMSTMCSPYSVGVVQDHSDNLLRVAGTMAHEMGHNFGMFHDDYSCKCPSTICVMDKALSFYIPTDFSSCSRLSYDKFFEDKLSNCLFNAPLPTDIISTPICGNQLVEMGEDCDCGTSEECTNICCDAKTCKIKATFQCALGECCEKCQFKKAGMVCRPAKDECDLPEMCNGKSGNCPDDRFQVNGFPCHHGKGHCLMGTCPTLQEQCTELWGPGTEVADKSCYNRNEGGSKYGYCRRVDDTLIPCKANDTMCGKLFCQGGSDNLPWKGRIVTFLTCKTFDPEDTSQEIGMVANGTKCGDNKVCINAECVDIEKAYKSTNCSSKCKGHAVCDHELQCQCEEGWIPPDCDDSSVVFHFSIVVGVLFPMAVIFVVVAMVIRHQSSREKQKKDQRPLSTTGTRPHKQKRKPQMVKAVQPQEMSQMKPHVYDLPVEGNEPPASFHKDTNALPPTVFKDNPVSTPKDSNPKA
Protein: Protein MICRORCHIDIA 4 (AtMORC4) (EC 3.6.-.-) (Protein CRT1-homolog 4) (CRT1-h4) (F4KAF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Exhibits ATPase activity. Binds DNA/RNA in a non-specific manner and exhibits endonuclease activity. Probably involved in DNA repair. Involved in RNA-directed DNA methylation (RdDM) as a component of the RdDM machinery and required for gene silencing. May also be involved in the regulation of chromatin architecture to maintain gene silencing. Together with MORC7, acts to suppress a wide set of non-methylated protein-coding genes, especially involved in pathogen response. Positive regulator of defense against the oomycete Hyaloperonospora arabidopsidis (Hpa).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:27171361}. Note=Accumulates in discrete nuclear bodies adjacent to chromocenters. {ECO:0000269|PubMed:27171361}.
Interaction partners:
- Disease resistance protein RRS1
- Protein LURP1
- Putative nuclear RNA export factor SDE5
Sequence:
MEPIVKQENPVTTSTLSTWKPAARNKTIPPPESVIELSSSNEGSELGENLDEIAEIQSVDRTGGDDVSGTKRARSDSIASPAKRLAVMIPDDDEEFLLSTTSGQAILALPATPCNVVAAPSSWGSCKQFWKAGDYEGTSGGDWEVSAGGFDHVRVHPKFLHSNATSHKWSLGAFAELLDNALDEVRSGATFVNVDMIQNRKDGSKMILIEDNGGGMNPEKMRHCMSLGYSAKSKLADTIGQYGNGFKTSTMRLGADVIVFSRCLGKDGKSSTQSIGLLSYTFLKSTGKEDIVVPMLDYERRDSEWCPITRSSVSDWEKNVETVVQWSPYATEEELLCQFNLMKKHGTRIIIYNLWEDDEGMLELDFDTDPHDIQLRGVNRDDKNIVMASQFPNSRHYLTYKHSLRSYASILYLKISHEFRIILRGKDVEHHNIVNDMMQTEKITYRPKEAADVSQLSAVVTIGFVKDAKHHVDVQGFNVYHKNRLIKPFWRIWNAAGSDGRGVIGVLEANFVEPAHDKQGFERTTVLSRLEARLLHMQKDYWRSKCHKIGYAKRQGRKSAKDTEKDTEDRESSPEFDPKGSASSRKRTVPSSFKTPTAAPRFNTPTAASEKFNPRSNVNGGGKGSVKVSKDIGYKSSEKGGKLGNSFSKSNKRAKPQGARAVEVTNSDDDYDCDSSPERNVTELPGKSSELPKPQSGPRTLSQLEQENNELRERLDKKEEVFLLLQKDLRRERELRKTLEAEVETLKNKLKEMDKEQASLIDVFAEDRDRRDKEEENLRIKLEEASNTIQKLIDGKARGR
Protein: Replication-associated protein (EC 2.7.7.-) (EC 3.1.21.-) (EC 3.6.1.-) (ATP-dependent helicase Rep) (RepP) (Q8BB16)
Organism: Porcine circovirus 2 (PCV2)
Function: Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep and/or Rep' binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the conserved sequence 5'-AGTATTAC-3' in the intergenic region of the genome, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, and nucleotidyl transferase.
Subcellular location: Host nucleus {ECO:0000269|PubMed:19150331}.
Interaction partners:
Sequence:
MPSKKNGRSGPQPHKRWVFTLNNPSEDERKKIREPPISLFDYFIVGEEGNEEGRTPHLQGFANFVKKQTFNKVKWYLGARCHIEKAKGTDQQNKEYCSKEGNLLIECGAPRSQGQRSDLSTAVSTLLESGSLVTVAEQHPVTFVRNFRGLAELLKVSGKMQKRDWKTNVHVIVGPPGCGKSKWAANFADPETTYWKPPRNKWWDGYHGEEVVVIDDFYGWLPWDDLLRLCDRYPLTVETKGGTVPFLARSILITSNQTPLEWYSSTAVPAVEALYRRITSLVFWKNATEQSTEEGGQFVTLSPPCPEFPYEINY
Protein: 6-hydroxytryprostatin B O-methyltransferase (EC 2.1.1.293) (Fumitremorgin biosynthesis protein D) (Q4WAW6)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: 6-hydroxytryprostatin B O-methyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Interaction partners:
- Tryprostatin B 6-hydroxylase
- Fumitremorgin C synthase
Sequence:
MTQAVDIGTIQTLIRLEVPDQVPLTGSIPYDALVKKLKTPVDPELLQRLIRFTRLVGFLDEDAEGAVKHSPMSAIFVNDPDTAGQARFMADFGIRPCSFIYESIKLDPSGEAARQGPLALMAREPGAREGPTFFEVLEKDPVNRKRWHDGMAVHNDSMVRHVAGAYDWGTVQSLVDIGGSEGHVAAVIVNAFPHIQITVQDLPEIIEKARQRGDRHPNIIFEEHDFFTPQPRIADAYFLRLILHDWNDADCTRIVRQISSALRPGARLLIMDAVLPEPGEGSLQSERRLRRSDIGMYTLFSAKERSLAQMRRLVEDCDSRLRFEKLYTPPGSHASMLSWICE
Protein: bZIP transcription factor 30 (AtbZIP30) (Protein DRINK ME) (Q9SIG8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that acts as a repressor of reproductive development, meristem size and plant growth. Acts as a transcriptional repressor in inflorescence tissues. Interacts with well known regulators of meristem and gynoecium development such as WUS, HEC1, KNAT1, KNAT2, HAT1, BEL1 and NGA1. Acts as positive regulator of JAG and OFP1 expression in developing gynoecia.
Subcellular location: Nucleus {ECO:0000269|PubMed:27402171}.
Interaction partners:
Sequence:
MGGGGDTTDTNMMQRVNSSSGTSSSSIPKHNLHLNPALIRSHHHFRHPFTGAPPPPIPPISPYSQIPATLQPRHSRSMSQPSSFFSFDSLPPLNPSAPSVSVSVEEKTGAGFSPSLPPSPFTMCHSSSSRNAGDGENLPPRKSHRRSNSDVTFGFSSMMSQNQKSPPLSSLERSISGEDTSDWSNLVKKEPREGFYKGRKPEVEAAMDDVFTAYMNLDNIDVLNSFGGEDGKNGNENVEEMESSRGSGTKKTNGGSSSDSEGDSSASGNVKVALSSSSSGVKRRAGGDIAPTGRHYRSVSMDSCFMGKLNFGDESSLKLPPSSSAKVSPTNSGEGNSSAYSVEFGNSEFTAAEMKKIAADEKLAEIVMADPKRVKRILANRVSAARSKERKTRYMAELEHKVQTLQTEATTLSAQLTHLQRDSMGLTNQNSELKFRLQAMEQQAQLRDALSEKLNEEVQRLKLVIGEPNRRQSGSSSSESKMSLNPEMFQQLSISQLQHQQMQHSNQCSTMKAKHTSND
Protein: Protein FAM133B (Q5BKY9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKRDNRVAYMNPIAMARSRGPIQSSGPTIQDYLNRPRPTWEEVKEQLEKKKKGSKALAEFEEKMNENWKKELEKHREKLLSGSESSSKKRQRKKKEKKKSGRYSSSSSSSSDSSSSSSDSEDEDKKQGKRRKKKKNRSHKSSESSMSETESDSKDSLKKKKKSKDGTEKEKDIKGLSKKRKMYSEDKPLSSESLSESEYIEEVRAKKKKSSEEREKATEKTKKKKKHKKHSKKKKKKAASSSPDSP
Protein: Protocadherin gamma A10 (Protocadherin gamma subfamily A, 10) (Q91XY9)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MAAQRNLSERTKLVLLFLWMPWESAARQIRYSVPEELEKGSFVGNIAKDLGLEPRQLAERGVRIISRGRSQLFSLNPRGGSLVTAGRIDREELCAQSAPCLVSFNILVEDRVKLFGIEIEVTDVNDNAPKFQAETLDVKINENVAPGMRFPLPEATDPDVGVNSLQSYQLSSNKHFSLVVQSGAKGVKYPELVLEQALDREEEAIHHLVLVASDGGNPPRSGTVLITVTVFDANDNAPVFTSTEYRVNIPENLPVGTQLLKVTATDKDEGANGEVTYAFRKSLDTQLSKFQLDKHTGEIKISENLDYEEMSFYEIEIQAEDGGAYLATAKVLITVEDVNDNSPEVTITSLFSPVTEDSPVGTVIALLNVHDLDSGQNGEVACSISGNLPFKLEKSIDNYYRLVTQRALDREQVPAYNITVTATDGGNPPLSTKADFTLQVADINDNPPTFSHPSYFTYIPENNPRGASIFSVTALDPDSKENAQIVYSLAEDTIEGAPLSSYISINSDTGILYALWSFDYEQFRELQVQVTASDSGKPPLHSNVSLTLFVLDQNDNSPEILYPTMPTDGSTGVELAPRSAELGYLVTKVVAVDRDSGQNAWLSYRLLKASEPGLFTVGLHTGEVRTARALMERDALKQSLVVAVQDHGQPPLSATVTLTVAVADSIPDVLADLGNLEPPQDSEASNLTLYLVVAVAAVSCVFLAFVIVLLALKLRRWHKSHVLQSSRDGLAGVPASHYVGVDGVRAFLQTYSHEVSLTADSRKSHLIFPQPNYADTLISQESCEKKDPLSLLDDSKCPVEDAPLVPQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Combgap, isoform M (A0A0B4LFC7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCAAQNPPPFGYTWGFADNGNRAAESVLEISPNINYTVSGESMPYLLSTDGSLAVQKDVKGLTAGGKNNVVRRMFVVNDPSFPPGTQRVITAGGASTVVKKQDNNQQVLSLDKNYLLVDPATAAAAAAAAGGDSGLAHHHTLTNGSIVDAKTGQTVLTAGSAAAKSHFSSIGALHLTQEECNEILIKRAIAAGHHQTHTITAADGSHHHASGGTPSGATTLLGDILPGISVQVQKVIQGLEDNEDSQGEAPNLKLEPGTLELSPKTELQESMHFSETDATIKKERPYSCDECGKSFLLKHHLTTHARVHTGERPHICTHCGKSFAHKHCLNTHLLLHSTERPYQCQECKKSFTLKHHLLTHSRVHSRERPFVCQECGRAFPLKRHLVTHSKFHAGERPYVCEECGESFAQENHLIMHSRFHGSLNPFVCAECGASFPRKFQLVNHGRIHGKIPHSCTVCGKEFLQKRTLVSHMRRVHTGEQAHPCVSCGEGFLTKAELHQHVRTAHNGVNPNTSSATIIANQQQLQQAHHHQAGQQTHPQTITVVSNPGNSTLLTVSTTDANGVARPQFVCRECGSAFNSREALALHLRLHTGDKSLMTDLCALTAALPGHFLSTASLNPGTVVTANPNLVGQSPVPVQIISSTGQVMSQTTLVQAANSTHPQAVVTAVPTMPVHGQQQHLQHVAQQQQQQQQQQQQQQQHVVSVAPANKPKSHFCASCGKGFAAKHGLMQHNRRHPNGGCTVRTHVCECGKAFFQKNHLMLHQRQHLETKPAISQQQVC
Protein: Beclin-1 (A0A024R1X5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367123}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004150, ECO:0000256|RuleBase:RU367123}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004150, ECO:0000256|RuleBase:RU367123}. Endosome membrane {ECO:0000256|ARBA:ARBA00004481, ECO:0000256|RuleBase:RU367123}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481, ECO:0000256|RuleBase:RU367123}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406, ECO:0000256|RuleBase:RU367123}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406, ECO:0000256|RuleBase:RU367123}. Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004318, ECO:0000256|RuleBase:RU367123}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004318, ECO:0000256|RuleBase:RU367123}. Cytoplasmic vesicle, autophagosome {ECO:0000256|RuleBase:RU367123}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEGSKTSNNSTMQVSFVCQRCSQPLKLDTSFKILDRVTIQELTAPLLTTAQAKPGETQEEETNSGEEPFIETPRQDGVSRRFIPPARMMSTESANSFTLIGEASDGGTMENLSRRLKVTGDLFDIMSGQTDVDHPLCEECTDTLLDQLDTQLNVTENECQNYKRCLEILEQMNEDDSEQLQMELKELALEEERLIQELEDVEKNRKIVAENLEKVQAEAERLDQEEAQYQREYSEFKRQQLELDDELKSVENQMRYAQTQLDKLKKTNVFNATFHIWHSGQFGTINNFRLGRLPSVPVEWNEINAAWGQTVLLLHALANKMGLKFQRYRLVPYGNHSYLESLTDKSKELPLYCSGGLRFFWDNKFDHAMVAFLDCVQQFKEEVEKGETRFCLPYRMDVEKGKIEDTGGSGGSYSIKTQFNSEEQWTKALKFMLTNLKWGLAWVSSQFYNK
Protein: Adenylate kinase 8 (AK 8) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 8) (Q32M07)
Organism: Mus musculus (Mouse)
Function: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. Also displays broad nucleoside diphosphate kinase activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96MA6}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q96MA6}. Note=Located in the proximal region of respiratory cilia. {ECO:0000250|UniProtKB:Q96MA6}.
Interaction partners:
- Adenylate kinase 7
- Adenylate kinase 9
- Adenosine kinase
- Cancer-related nucleoside-triphosphatase homolog
- Adenylosuccinate lyase
- Adenine phosphoribosyltransferase
- Adenylate kinase isoenzyme 1
- Adenylate kinase 2, mitochondrial
- Adenylate kinase isoenzyme 5
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Sequence:
MDATTAPHRIPPEMPQYGEDYYIFEMMQNMLEQLLIHQPEDPISFMITHLRRNNDNVPKVVILGPPASGKTTIAMWLCKHLNSNLITKESLLEREFSRLSVEAKSYYQVYKKIPNSILVSLVQERLNEDDCLRKGWILDGIPERREQALMIQTLGLAPKHVIVLNAPDTVLIERNVGKRIDPVTGEIYHTTFDWPPEPEIQNRLRQPEGISEIETAKKLLEYHRHIIRILPSYPKILKTISSDQPCVDVFYQALTYVQSGHRCNAPFTPKVLLCGPLGSGKRLQATLLAQKYGLVNISCGQLLKEAVAAKSSFGELIQPFFEKRMTVPDSIITKVLADRMEQQDCIQKGWVLHGFPRDLDQARMLNSMGYNPNRVFFLSVPLDSILERLTLRRTDPVTGERFHLMYKPPPTIEVQVRLLQNPKDSEEYIKLQTDLFYRNSGDLEQYYDRAIIVNGDQDPYTVFEYIESGIINPLPRKVT
Protein: 17-beta-hydroxysteroid dehydrogenase type 3 (17-beta-HSD 3) (Short chain dehydrogenase/reductase family 12C member 2) (Testicular 17-beta-hydroxysteroid dehydrogenase) (Testosterone 17-beta-dehydrogenase 3) (EC 1.1.1.64) (Q6QA32)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the conversion of 17-oxosteroids to 17beta-hydroxysteroids in the presence of NADPH. Favors the reduction of androstenedione to testosterone. Testosterone is the key androgen driving male development and function (By similarity). Among further tested androgens epiandrosterone and dehydroepiandrosterone are accepted as substrates and reduced at C-17. Can also reduce 11-ketoandrostenedione as well as 11beta-hydroxyandrostenedione at C-17 to the respective testosterone forms. Cannot use androsterone and androstanedione as substrates.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16216911}. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTLTEIIFVLTGTCAILVFGGKIASLIMMLITKLFCPLPEAFFTSLGKWAVITGGSDGIGRAYAEELSKQGMSVIIISRNQEKLDRAAKKIELNTGGKVKVIAADFTKDDIYGHITENIEGLDIGVLVNNVGILPSQIPCKLLETSDLEERIYDIVNCNVKSMVKMCRIVLPGMQQRRRGVILNVSSGIAKIPCPIYTLYAASKVFVERFSQGLQAEYISKGIIIQTVAPFGVSTAMTGHQKPDMVTFTAEEFVRSSLKYLKTGDQTYGSITHTLLGRIVQSIPTWVLQSETFQHHFQEYVKNRDRR
Protein: GH01676p (GH02239p) (Q86P86)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAYPRDYGIEHILTCEADNCQVRLDFTDFQLGLTSTLEIFDSNGQMLDSYTGEHFRPPITVSSGKSLLLQFRGNSATGVGFRAEVSFVSSKQLKDERLVPYTDCGGMVTGPGGAITMMNMIENATDVRLFDCIWIIKPGNNYMMMKTHISLRVDDFYGMAARSELTIRQGTTSDAVEIENVMWPNNGLSKESHVAPILNGYYIRLRGVFGMSSKLAIVYSVFNYLNCYIGSEFLCGNNHCISIRLHCDGFDHCGDGSDEPDSCEEDWAHLHHDRRWYSHKPNYYFPKIDQYPDLKTATGIFIISTLGIFGVLSGWMVILYRMGVRARHQRELQSHLQTISELLDRQDEDRTPDEPPSYEAPPDYEEVIKVGMQQELREPRRQRRARRAPPRDRSCSRAASNCTVQSVLPLHRSCTLERDQEQPSTSAAAMTHAVAATDTTEDAEHVQTMAQRMLLATAICGTAGTSLPAAKESGQRVQSVGISTSPSSLSAGGELPTAGGSATTPGSTADECTQGGDSLSISLTLGLPSTTAESPVTTDQNQLQKQSPEQTISNCTEHTFLKRSWLVVQQVPPGRGYRVRRLRHTFSSPEAFTSDELHLPYPDFLSYGTNLPHERSSSNFGSELSRDPSSYSVGKRARLTPEDTSGSETITQEMEQSNQTLQSHVIVESHPNHSESESEAEQQVSCFGAVAQRPKRRHRGHVRSRSFSNARGGSAGRRRLMQRSSSADLLMNYATMAVSTPQKTSEAMQRLFFI