wanglab/gogpt-training-data huggingface dataset:
Protein: Methionine aminopeptidase 2 (MAP 2) (MetAP 2) (EC 3.4.11.18) (Initiation factor 2-associated 67 kDa glycoprotein) (p67) (p67eIF2) (Peptidase M) (P50579)
Organism: Homo sapiens (Human)
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03175, ECO:0000269|PubMed:21537465}. Note=About 30% of expressed METAP2 associates with polysomes.
Interaction partners:
- Methionine aminopeptidase 1
- Large ribosomal subunit protein uL18
- Sphingolipid delta
- Sphingolipid delta
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL23
- Ubiquitin carboxyl-terminal hydrolase isozyme L5
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL5
Sequence:
MAGVEEVAASGSHLNGDLDPDDREEGAASTAEEAAKKKRRKKKKSKGPSAAGEQEPDKESGASVDEVARQLERSALEDKERDEDDEDGDGDGDGATGKKKKKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY
Protein: Phytochrome A-2 (GmphyA2) (B4YB07)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenic responses, whereas reconversion of Pfr to Pr cancels the induction of those responses. Pfr controls the expression of a number of nuclear genes including those encoding the small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B binding protein, protochlorophyllide reductase, rRNA, etc. It also controls the expression of its own gene(s) in a negative feedback fashion.
Interaction partners:
- BHLH domain-containing protein
- BHLH domain-containing protein
- BHLH transcription factor
- BHLH domain-containing protein
- BHLH transcription factor
- Protein GIGANTEA
- Protein GIGANTEA
- Phytochrome
- Phytochrome A
- FT-like protein
Sequence:
MSTSRPSQSSSNSGRSRRSARAMALATVDAKLHATFEESGSSFDYSSSVRISGTADGVNQPRHDKVTTAYLHHMQKGKMIQPFGCLLALDEKTCKVIAYSENAPEMLTMVSHAVPSVGDHPALGIGTDIKTLFTAPSASALQKALGFAEVLLLNPVLIHCKTSGKPFYAIIHRVTGSMIIDFEPVKPYEVPMTAAGALQSYKLAAKAITRLQSLPSGSMERLCDTMVQEVFELTGYDRVMAYKFHEDDHGEVIAEITKPGLEPYLGLHYPATDIPQASRFLFMKNKVRMIVDCHAKHVRVLQDEKLPFDLTLCGSTLRAPHSCHAQYMANMDSIASLVMAVVVNDNEEDGDTDAIQPQKRKRLWGLVVCHNTTPRFVPFPLRYACEFLAQVFAIHVNKEIELEYQIIEKNILRTQTLLCDLVMRDAPLGIVSESPNIMDLVKCDGAALIYKNKVWRLGVTPSESQIREIAFWLSEYHMDSTGFSTDSLSDAGFPSALSLGDVVCGMAAVRVTAKDVVFWFRSHTAAEIRWGGAKHEAGEKDDGRRMHPRSSFKVFLDVVKARSLPWKEYEIDAMHSLQLILRNAFKDTESMDLNTKAINTRLSDLKIEGMQELEAVTSEIVRLIETATVPILAVDVDGLVNGWNIKIAELTGLPVGEAMGKHLLTLVEDSSTDRVKKMLNLALLGEEEKNVQFEIKTHGSKMDSGPISLVVNACASRDLRDNVVGVCFVAHDITAQKNVMDKFTRIEGDYKAIVQNRNPLIPPIFGTDEFGWCCEWNPAMTKLTGWKREEVMDKMLLGELFGTHMAACRLKNQEAFVNLGVVLNKAMTGLETEKVPFGFFARNGKYVECLLSVSKKLDVEGLVTGVFCFLQLASPELQQALHIQRLSEQTALKRLNALSYMKRQIRNPLCGIIFSRKMLEGTALGTEQKQLLRTSAQCQQQLSKILDDSDLDSIIDGYLDLEMAEFTLHEVLVTSLSQVMTKSNGKSIRIVNDVAEQIVMETLYGDSLRLQQVLADFLLISINFTPNGGQVVVAGTLTKEQLGKSVHLVKLELSITHGGSGVPEALLNQMFGNNGLESEEGISLLISRKLLKLMNGDVRYLREAGKSAFILSAELAAAHNLKG
Protein: Semaphorin-3A (Semaphorin III) (Sema III) (Q63548)
Organism: Rattus norvegicus (Rat)
Function: May be involved in guiding growing axons towards their targets by forming a molecular boundary that instructs axons to engage in the formation of specific nerve tracts. Binds to neuropilin. Involved in the development of the olfactory system and in neuronal control of puberty (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Plexin-A2
- Plexin-A4
- Neuropilin-1
- Plexin-A1
- Plexin-A3
- Neuropilin-2
- Plexin-D1
- Plexin-B1
- Dihydropyrimidinase-related protein 1
- Dihydropyrimidinase-related protein 2
Sequence:
MGWFTGIACLFWGILLTARANYANGKNNVPRLKLSYKEMLESNNVITFNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLKAYNQTHLYACGTGAFHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYQGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQYDVMFIGTDVGTVLKVVSVPKETWHDLEEVLLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPLHRCDIYGKACAECCLARDPYCAWDGSSCSRYFPTAKRRTRRQDIRNGDPLTHCSDLQHHDNHHGHSLEERIIYGVENSSTFLECSPKSQRALVYWQFQRRNEDRKEEIRVGDHIIRTEQGLLLRSLQKKDSGNYLCHAVEHGFMQTLLKVTLEVIDTEHLEELLHKDDDGDGSKTKEMSSSMTPSQKVWYRDFMQLINHPNLNTMDEFCEQVWKRDRKQRRQRPGHSQGSSNKWKHMQESKKGRNRRTHEFERAPRSV
Protein: Unconventional myosin (Q95VU9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLTTTIWTGLTTSIWRPRDASSSNEAVHLQQRLKSLSTELVTLRNRLHVGHGPGQGQSQGNGAQPVAPAPNAGPKANNFDLNASSPNLNLSSSGAGLSASAVQQHTNGHHTTSKNHSFSHTLPANSGSGGGEGAGGGAVVSARNTSIPHPLPHQLAEKPGLSHQQSGSGHGQSTGTLPHMSGMGSILGQNSHSHAPVNNNSNNSNTLPMRTSNSGHLGINGGGVGHHLSHAHSQQLPFIPQSKHTNPCQSVKTLPFGFGFSESQQKMQQQQQQGNSSPKDMQDLIHLSGPLTEHAVMRTLQARFNERRYFTNVGPILLSINPYLDVGNPLTLTSTRAMPLAPQLQKIVQEAVRQQSETGYPQAIILSGTSGAGKTANAMLMLRQLFAIAGGGPETDAFKHLAAAFTVLRSLGSAKTTTNSESSRIGQFIEVQVTDGALYRTKIHCYFLDQTRVIRPLPKEKNYHIFYQLLAGLSREERQKLHLDGYSPANLRYLRGDIGQNEQEDAARFQAWKTCLGILGIPFLDVVRVLAAVLLLGNVQFIDGGGLEVDVKGETELNSVASLLGVPPAALFRGLTTRTHNVRGQLVKSVCGDGDANMTRDCLAKALYCRTVATIVRRANSLKRLGSTLGTLSSDSNESVHNQADVASQHASTIGGGNAGSKSMAALNNAVRHATSDGFIGILDMFGFEEPSPHAHLEHLCINLCAETMQHFYNTHIFKSSVESCRDEGIVCDTEVDYVDNVPCIDLISSLRTGLLSMLDAECSVRGTAESYVTKLKVQHRSSTRLETKPTAEPHDPRMFLIRHFAGRVEYDTTDFLDTNRDVVPDDLVGVFYKHTCNFGFATHLFGSELKALYAQQQAPRGLSFRISPTSHSDLLNGDEPVSTLTQDFHTRLDNLLRTLVHARPHFVRCIRSNGTEAARSFDRATVVRQIRSLQVLETVNLMASGFPHRMRFKQFNARYRMLAPFRLLRRSEDKALEDCQLILKYAMEQPPVLDGSVTLAWAPGKRHVFLSEGIRQHLEHLRTEIRHKSATLMQATWRGWWWRKKMGNGGAKRSKIPGLQQAPLPNNKTTPNSAAQNKAASSTMAALAAVAAAAPISVPRLSAKTTSLGIGGTVARPRPQPIAGTPPPDPQEKCDQKIIQQTCNLFGLDLERPPPVPPSRSYTITGNSKISYPQNRVMKMNFPEEGQSEAPQLKKGEAVTVVGASTVRGHLMVEHKGQSFHVPFQFMTLSK
Protein: AT3g61870/F21F14_40 (Plant/protein) (Q9M277)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MATTLHCLSTLHLLPRTHHPKTLNSLKPITTKSQPCKTPEIPSTPNALQLLKSSSLPLAVIALPFFLDPQDAAAAGGEFGILEGRSFALIHPIVMGGLFAYTLWTGYLGWQWRRVRTIQSEISDLKKQLKPTPVSPDGSTAVDSSSPPSTTELQIQRLTEERKELVKGSYRDKHFDAGSVLLGFGVLEAVFGGVNTYLRTGKLFPGPHLYAGAGITVLWAAAAALVPAMQKGNDTARSLHIALNAVNVLLFIWQIPTGLDIVLKVFEFTKWP
Protein: G protein subunit alpha transducin 1 (D3ZSS5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Rhodopsin
- Regulator of G-protein signaling 9
- Rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Guanine nucleotide-binding protein G
- Phosphodiesterase
- Phosphodiesterase
- Guanine nucleotide-binding protein subunit gamma
- G protein subunit alpha transducin 2
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNKKDVFSEKIKKAHLSICFPDYDGPNTYDDAGNYIKVQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
Protein: Eukaryotic translation initiation factor 4E-binding protein 3 (4E-BP3) (eIF4E-binding protein 3) (O60516)
Organism: Homo sapiens (Human)
Function: Repressor of translation initiation that regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22684010}. Nucleus {ECO:0000269|PubMed:22684010}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Eukaryotic initiation factor 4A-I
- Eukaryotic translation initiation factor 4 gamma 2
- Eukaryotic translation initiation factor 4E type 3
- Eukaryotic translation initiation factor 4E type 1B
- Eukaryotic translation initiation factor 4E-binding protein 1
- ANKHD1-EIF4EBP3 readthrough
- Eukaryotic translation initiation factor 4 gamma 1
- Eukaryotic translation initiation factor 4E-binding protein 2
- Eukaryotic initiation factor 4A-II
Sequence:
MSTSTSCPIPGGRDQLPDCYSTTPGGTLYATTPGGTRIIYDRKFLLECKNSPIARTPPCCLPQIPGVTTPPTAPLSKLEELKEQETEEEIPDDAQFEMDI
Protein: POU domain protein (O57602)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MENGIHGVQAAQTNGLDSQQKPNGQATSAISNIQAQALLQQLSLSSAQQQQLFLQQAQQILAAAVQQQQQQTANQQSSTTGANISASAATPITQIPLSQPIQIAHQLQPTGLNLQQFVLVQPGQLQPAQFIISPSPQGQTGLLQGLQAQNLLTQLPQSQAHILQPQSSIALTTQAATPTRKIAAMPSAAPTTTKRVDVPLVEEASELEELEQFAKAFKQRRIKLGFTQGDVGLAMGKLYGNDFSQTTISRFEALNLSFKNMCKLKPLLEKWLNDAENMTSESAVSSPSDMSPGICEGLNRRRKKRTSIDTNIRIALEKSFLEQSQKPTSEEITMIADQLNMEKEVVRVWFCNRRQKEKRINPPSSSTSNTPIKTVFTNSSPSVISSSSNTLNASSALSLSTASVPNFTLAGTTLGPVTSNTATVISLAPAVATPAPTMTSPSLTPSATVATLTATKQEVVRTTETGSTIATSAAQGPGQFVMSPAGLGGANLAAMAAAAGLNPGIISPSQLTQGGALLSLAPASLGNALTPTALMNNTTLATIQALASGGALPITSFDGNGNVLFANTSAGGPILFNSPLSLLPTGVLSAGGAGGGALNLQVTGDAHQSAMPVKSITVASKAQ
Protein: NIMA related kinase 3 (EC 2.7.11.1) (Q8I629)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Protein kinase, putative
- Ran-specific GTPase-activating protein 1, putative
Sequence:
MVCIYLFCFLLFHLFVVNTRMRILCNLLIVICEYMFPFYSFILFKFVKMLSLLLPSILSCEKKYQVYKNNGYKFETVLDFMTSDSEIHLIRSIESDEIYISKVYDIYGINEDDLNKYMNELYIMNKLRNCENIVNIIDYIKENDTLSFILEFCNQGDLHSDILRKKLNNEIYTESEIFNILHQILNGLNIIHQNGIIHGDLKSTNIFIKDNKIKIGDFGISSEQSSNNNLGTLNCLSYESIKFKKTNKLSDLFQVGCILYELATLSSPFCATNINDMISLFEDKNYKSYIIKNISSIYSQKLVNVISKLLSLNTLERLEVITNYNLETTQHVHLENANKIISCITVQ
Protein: Glutaredoxin-2, mitochondrial (A0A0R4ILJ8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Thioredoxin
- Thioredoxin
- Ribonucleoside-diphosphate reductase large subunit
- Thioredoxin, mitochondrial
- Glutaredoxin 3
- Glutaredoxin-related protein 5, mitochondrial
- Low molecular weight phosphotyrosine protein phosphatase
- Glutathione reductase
Sequence:
MIDLNCQSNSLVSALTAFAFLVSSTCFFYRPVIITRMGNFSSSAPGLSSSACGQFVQDIVSSNCVVIFSKTTCPYCKMAKGVFNEIGATYKVVELDEHNDGRRLQETLAELTGARTVPRVFINGQCIGGGSDTKQLHQQGKLLPLIEQCRPCCLNMTPEGSGNSQNQPHQ
Protein: Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1 (PAPS synthase 1) (PAPSS 1) (Sulfurylase kinase 1) (SK 1) (SK1) [Includes: Sulfate adenylyltransferase (EC 2.7.7.4) (ATP-sulfurylase) (Sulfate adenylate transferase) (SAT); Adenylyl-sulfate kinase (EC 2.7.1.25) (3'-phosphoadenosine-5'-phosphosulfate synthase) (APS kinase) (Adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenylylsulfate 3'-phosphotransferase)] (O43252)
Organism: Homo sapiens (Human)
Function: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway. Required for normal biosynthesis of sulfated L-selectin ligands in endothelial cells.
Interaction partners:
- FAD synthase
- Sulfite oxidase, mitochondrial
- Golgi-resident adenosine 3',5'-bisphosphate 3'-phosphatase
- 3'
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- Sulfate transporter
- Elongation factor 1-alpha 1
- Elongation factor 1-alpha 2
- HBS1-like protein
- Eukaryotic peptide chain release factor GTP-binding subunit ERF3A
Sequence:
MEIPGSLCKKVKLSNNAQNWGMQRATNVTYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTVSMALEEYLVCHGIPCYTLDGDNIRQGLNKNLGFSPEDREENVRRIAEVAKLFADAGLVCITSFISPYTQDRNNARQIHEGASLPFFEVFVDAPLHVCEQRDVKGLYKKARAGEIKGFTGIDSEYEKPEAPELVLKTDSCDVNDCVQQVVELLQERDIVPVDASYEVKELYVPENKLHLAKTDAETLPALKINKVDMQWVQVLAEGWATPLNGFMREREYLQCLHFDCLLDGGVINLSVPIVLTATHEDKERLDGCTAFALMYEGRRVAILRNPEFFEHRKEERCARQWGTTCKNHPYIKMVMEQGDWLIGGDLQVLDRVYWNDGLDQYRLTPTELKQKFKDMNADAVFAFQLRNPVHNGHALLMQDTHKQLLERGYRRPVLLLHPLGGWTKDDDVPLMWRMKQHAAVLEEGVLNPETTVVAIFPSPMMYAGPTEVQWHCRARMVAGANFYIVGRDPAGMPHPETGKDLYEPSHGAKVLTMAPGLITLEIVPFRVAAYNKKKKRMDYYDSEHHEDFEFISGTRMRKLAREGQKPPEGFMAPKAWTVLTEYYKSLEKA
Protein: mRNA 5'-phosphatase (EC 3.6.1.74) (Q582T2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMEATERRRKRERNERNDERRDDCEVLAKTDEKRTIVEELFQRLQSLDHTHMELEARLCRRAEVSDKSGSTSSEREWKGRRARKTRTEVMPGVAEEDYKRIEEFCLDKGKEGSVTRSTTRDVSFGQWRYTYTSGKPSECIACIRKERLFVLDVPVPSGAYDIRFSACTEITGELPSPNFAPTRGYTRHKDRLSVTDGLFRYDLTRVRDKHTTGYEVEVEFLLKDNDEKKITDSHVEELVGRALSLATLTASEG
Protein: Mannitol-1-phosphate 5-dehydrogenase (M1PDH) (MPD) (MPDH) (EC 1.1.1.17) (Q5B0F5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway.
Interaction partners:
- ATP-dependent 6-phosphofructokinase
- Hexokinase
- Phosphotransferase
- Phosphotransferase
- Mannose-6-phosphate isomerase
- 6-phosphofructo-2-kinase domain-containing protein
- Fructose-1,6-bisphosphatase
- Probable D-xylulose kinase A
Sequence:
MGKAIHFGGGNIGRGFVGEFLHEAGYEVVFVDVVDDLITSIQNTPSYEITEISEDGEKTKKITNYRALNSKSHEADVVQEIATADIVTCAVGPRVLQFIAPVIAKGLESRNVSTPLTVIACENAINATDTLRGHIEKKTKPEIISERAVFANCAIDRIVPNQPPNNGLNVRIEKYWEWVVEQTPFKEKGVAHPNVSAIHWVDKLDPYIERKLFTVNTGHATTAYYGHLAGKKTIADALHDPKIRENVHKVLDETASLIINKHGISEQEQKEYVDKIISRISNPYLEDGVERVGRAPLRKLSRNERFIGPASQLAERGLKFDALLGAIEQALRFQNVEGDEESKELAKILKEKTAEEATSELTELEKDHPLYSHVLERVRTVQQESK
Protein: Protein scarlet (EC 7.6.2.-) (ATP-binding cassette transporter sub-family G member scarlet) (Broad substrate specificity ATP-binding cassette transporter scarlet) (P45843)
Organism: Drosophila melanogaster (Fruit fly)
Function: ATP-dependent transporter of the ATP-binding cassette (ABC) family which transports various molecules including bioamines, neurotransmitters and metabolic intermediates. In the eye and probably in association with w/white, required for the transport of the eye brown pigment precursors, kynurenine and probably tryptophan, into pigment cell granules. In Malpighian tubules and pupal eyes, involved in kynurenine transport. Probably in association with w/white, plays a role in zinc storage granule biogenesis in Malpighian tubule principal epithelial cells.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:11294610}; Multi-pass membrane protein {ECO:0000269|PubMed:11294610}. Note=Co-localizes with w/white to pigment granules within pigment cells and retinula cells of the compound eye. {ECO:0000269|PubMed:11294610}.
Interaction partners:
Sequence:
MSDSDSKRIDVEAPERVEQHELQVMPVGSTIEVPSLDSTPKLSKRNSSERSLPLRSYSKWSPTEQGATLVWRDLCVYTNVGGSGQRMKRIINNSTGAIQPGTLMALMGSSGSGKTTLMSTLAFRQPAGTVVQGDILINGRRIGPFMHRISGYVYQDDLFLGSLTVLEHLNFMAHLRLDRRVSKEERRLIIKELLERTGLLSAAQTRIGSGDDKKVLSGGERKRLAFAVELLNNPVILFCDEPTTGLDSYSAQQLVATLYELAQKGTTILCTIHQPSSQLFDNFNNVMLLADGRVAFTGSPQHALSFFANHGYYCPEAYNPADFLIGVLATDPGYEQASQRSAQHLCDQFAVSSAAKQRDMLVNLEIHMAQSGNFPFDTEVESFRGVAWYKRFHVVWLRASLTLLRDPTIQWLRFIQKIAMAFIIGACFAGTTEPSQLGVQAVQGALFIMISENTYHPMYSVLNLFPQGFPLFMRETRSGLYSTGQYYAANILALLPGMIIEPLIFVIICYWLTGLRSTFYAFGVTAMCVVLVMNVATACGCFFSTAFNSVPLAMAYLVPLDYIFMITSGIFIQVNSLPVAFWWTQFLSWMLYANEAMTAAQWSGVQNITCFQESADLPCFHTGQDVLDKYSFNESNVYRNLLAMVGLYFGFHLLGYYCLWRRARKL
Protein: ATP synthase subunit c (ATP synthase F(0) sector subunit c) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein) (Q8RGD7)
Organism: Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355)
Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01396}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01396}.
Interaction partners:
- ATP synthase subunit a
- ATP synthase subunit delta
- ATP synthase subunit alpha
- ATP synthase gamma chain
- ATP synthase subunit b
- ATP synthase subunit beta
- ATP synthase epsilon chain
- V-type sodium ATP synthase subunit I
- V-type ATP synthase beta chain
- V-type sodium ATP synthase subunit C
Sequence:
MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAVESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLYANPFLSKLG
Protein: Rifin (C6KSK9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYINILLFELPLNILIYNQRNHNSTTPHHPPNTRLLCECELYAPATYDDDPQMKEVMQQFEDRTSQRFHEYDERMKTTRQKCKDKCDKEIQKIILKDKLEKELMDKFATLQTDIQNDAIPTCVCEKSLEDKMEKGCLRCGGVLGGGIAPTFGLIGSVAINMWKTTEIAAATKAAIAAGKAAGKIAGEAAGKKAVIEALKYFGVDDFFPEIFKSILKMSRYTDVTKFGAAIAEKHVLNCAMSARGGSVNDSTCNAFEIKLGLFEAETGKPNGPPAYQAIPQKINELAEEATQAAAEAAKKASESATAAFETAEKEAIEAASMQLYTTIAYSILAILIIVLIMVIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: Mini-chromosome maintenance complex-binding protein (MCM-BP) (MCM-binding protein) (Q7ZYP6)
Organism: Xenopus laevis (African clawed frog)
Function: Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the mcm complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. May also be required for sister chromatid cohesion.
Subcellular location: Nucleus {ECO:0000269|PubMed:21196493}. Note=Imported in the nucleus in late S phase when mcm2-7 dissociates from chromatin.
Interaction partners:
Sequence:
MAGVEDWISAPLAVVQGLFSQRQANGDWEKNVTDYFHDKLQGNRSPASVPCLNDVPLHYLKPNSLVRFRCMVQDMFDPEFYMGVYETVDTNTSARVLHFGKYRDLAESLPQQEVDLDSRRNVTCERQTFYCVPVPGESPWVKDAYTSSSQARACASTSYTPSRQKRSYEEDEDVGPCDTRTSHGLGEPKRLETEAAGLQQNQPSSCSSAPDLNFPLPGEKGPACLIKVYEGWDSFKVNDIIEVYGILSVDPALSAVNEDRDAVSALLDPSDNMETLEEQRAHCPPASLVPRIHSVVTWKLQHNNPLLPGTLQGTEESKLFVSNLLCEVSAVRAELLGFLSHALLGDSLAAEYLIIHLISTVYARRDVLPLGKFTLNLSGCPRNGIFSELLYRILQQIVPAAHYLPMTIENMNKLRFIPHKDYNANRLRSGLLQLSAHTSLLLDETLLEQGQLDTAGVHNVTALGNLITWQKVDYDFSYHRMEFPCNINVLVTSEGRSLLPSDCRVHLQPQMTPPNLEQYMGALLSASLPSLLNKFRSYIGLLRLLDYSISDEITKAVEDDFVEMRKNDPQSISADDLHRLLVVSRLLSLSSGQTTLSREMWLRAKQLEQQRKSRFREQKHVNGNEL
Protein: Ribonucleases P/MRP protein subunit pop3 (RNA-processing protein pop3) (O74450)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for processing of 5.8S rRNA (short form) at site A3 and for 5'- and 3'-processing of pre-tRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribonuclease MRP protein subunit rmp1
- Ribonuclease P/MRP protein subunit POP5
- Probable ribonuclease P protein subunit 1
- Probable ribonuclease P protein subunit 3
- Ribonucleases P/MRP protein subunit pop1
- Uncharacterized protein C6C3.09
- Large ribosomal subunit protein uL30C
- Ribonuclease P protein subunit rpr2
- Uncharacterized protein C16C4.19
- Probable ribonucleases P protein subunit pop8
Sequence:
MKKKQTKVKQTVKLVLRNPLSISWPIVDANTQEKLAQTLVQWLPASHKDILDSKLTVGLNSVNELLERCCQNAKDVTQPAVVFILHDQDSMLVTHMPQLVANANFYGSSKCRLVPLGFSAQALIAKKLGLSRAGAIAVQDDSPLWKYLKDLVMNIEEPQARWLSENPEYEVTKVEKIITSQKENQGTKKEGKNEKGNEFKK
Protein: Proteasome inhibitor PI31 subunit (hPI31) (Q92530)
Organism: Homo sapiens (Human)
Function: Plays an important role in control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Also inhibits the activation of the proteasome by the proteasome regulatory proteins PA700 and PA28.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18495667}. Endoplasmic reticulum {ECO:0000269|PubMed:18495667}.
Interaction partners:
- Proteasome subunit beta type-7
- Proteasome subunit beta type-4
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-1
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-4
- Proteasome subunit alpha type-7
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-2
- Proteasome subunit beta type-3
Sequence:
MAGLEVLFASAAPAITCRQDALVCFLHWEVVTHGYFGLGVGDQPGPNDKKSELLPAGWNNNKDLYVLRYEYKDGSRKLLVKAITVESSMILNVLEYGSQQVADLTLNLDDYIDAEHLGDFHRTYKNSEELRSRIVSGIITPIHEQWEKANVSSPHREFPPATAREVDPLRIPPHHPHTSRQPPWCDPLGPFVVGGEDLDPFGPRRGGMIVDPLRSGFPRALIDPSSGLPNRLPPGAVPPGARFDPFGPIGTSPPGPNPDHLPPPGYDDMYL
Protein: aldehyde dehydrogenase (NAD(+)) (EC 1.2.1.3) (Q4WCK7)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Choline dehydrogenase, putative
- GMC oxidoreductase, putative
- Versicolorin B synthase, putative
- glucose oxidase
- GMC oxidoreductase, putative
- aldehyde dehydrogenase
- Actin-related protein 2/3 complex subunit 5
Sequence:
MADLPFAPRHPYYDGKVQLASSGRTFRTINPADNTPLAEIHVASNSDTDAAIAAADRAFPLWSQTPHIARARILQKAAALLRERNDELARLETLDSGKAYSETSTVDIVTGADVLEYYANLVGGGGLNGETTQLREDAWVFTKKAPLGVCVGIGAWNYPLQIALWKSAPCLAAGNTMVYKPSEYTPLHAQMLAEIYREAGLPPGVFNVVYGAGDVGAYLTAHPLVAKVSFTGQVSTGMKVAGSAAGQMKYVTMELGGKSPLLILPDADLENAVNGAMMANFFSTGQVCTNGTRVFVPRGMKSAFEKALLDKMQYIRPGPLFDNATNFGPLSSALHLEKVTSYIRHGIETDKATLLYGGLGKPSLPKDLENGFWVRPTVFTDCTDSMRIVQEEIFGPVMSILYYDTVEEAVRRANNTELGLAAGVFTRDLNMAHRIIDQLQAGITWINSWGESPAEMAVGGWKKSGVGVENGRRGIEAWVRNKSTLVDMNGRVATVFAKL
Protein: Protein mono-ADP-ribosyltransferase PARP11 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 11) (ARTD11) (Poly [ADP-ribose] polymerase 11) (PARP-11) (Q8CFF0)
Organism: Mus musculus (Mouse)
Function: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins (By similarity). Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9NR21}. Note=Colocalizes with NUP153 at nuclear pores. {ECO:0000250|UniProtKB:Q9NR21}.
Interaction partners:
- Zinc finger CCCH-type antiviral protein 1-like
- Protein mono-ADP-ribosyltransferase PARP16
- Protein mono-ADP-ribosyltransferase PARP4
- Protein mono-ADP-ribosyltransferase PARP8
- Protein mono-ADP-ribosyltransferase PARP6
- Protein mono-ADP-ribosyltransferase PARP3
Sequence:
MFHKTEEFFPKKTDSDVDDMDTSDTQWGWFYLAECGKWHMFQPDTNIQCSVSSEDIEKSFKTNPCGSISFTTSKFSYKIDFAEMKQMNLVTGKQRLIKRAPFSISAFSYICENEAIPMPTHWENVNPDVPYQLVSLQNQTHEYNEVASLFGKTMDRNRIKRIQRIQNLDLWEFFCRKKAQLKKKRGVPQINEQMLFHGTSSEFVEAICIHNFDWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHGNTFQIHGVSLQQRHLFRTYKSMFLARVLIGDYINGDSKYMRPPSKDGSYVNLYDSCVDDTWNPKIFVVFDANQIYPEYLIDFH