wanglab/gogpt-training-data huggingface dataset:
Protein: T-complex protein 1 subunit theta (TCP-1-theta) (CCT-theta) (Chaperonin containing T-complex polypeptide 1 subunit 8) (Renal carcinoma antigen NY-REN-15) (P50990)
Organism: Homo sapiens (Human)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20080638}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:20080638}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P42932}.
Interaction partners:
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit zeta-2
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Cell division cycle protein 20 homolog
Sequence:
MALHVPKAPGFAQMLKEGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMNKMVINHLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQEQEVGDGTNFVLVFAGALLELAEELLRIGLSVSEVIEGYEIACRKAHEILPNLVCCSAKNLRDIDEVSSLLRTSIMSKQYGNEVFLAKLIAQACVSIFPDSGHFNVDNIRVCKILGSGISSSSVLHGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITETKGTVLIKTAEELMNFSKGEENLMDAQVKAIADTGANVVVTGGKVADMALHYANKYNIMLVRLNSKWDLRRLCKTVGATALPRLTPPVLEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAISTIVLRGSTDNLMDDIERAVDDGVNTFKVLTRDKRLVPGGGATEIELAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALAENSGVKANEVISKLYAVHQEGNKNVGLDIEAEVPAVKDMLEAGILDTYLGKYWAIKLATNAAVTVLRVDQIIMAKPAGGPKPPSGKKDWDDDQND
Protein: Dynein assembly factor with WDR repeat domains 1 (WD repeat domain 69) (A6H6T7)
Organism: Mus musculus (Mouse)
Interaction partners:
- Pre-mRNA-processing factor 6
- U4/U6 small nuclear ribonucleoprotein Prp3
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-processing-splicing factor 8
- U4/U6 small nuclear ribonucleoprotein Prp31
- 116 kDa U5 small nuclear ribonucleoprotein component
- U6 snRNA-associated Sm-like protein LSm8
- U4/U6.U5 tri-snRNP-associated protein 1
- U6 snRNA-associated Sm-like protein LSm7
- Small nuclear ribonucleoprotein Sm D2
Sequence:
MKLKSLLLRYYPPGIMLEYEKGGELKTKSIDLLELSPSTDVNTLVGEIQQAEPLITASRTKQVRLLVQRLQEKLRQHSDHNFYLFKVLRAHILPLTNVALNKAGSCFITGSYDRTCKVWDTASGEELHTLEGHKNVVYAIAFNNPYGKVHTLIGHCAEISSALFNWDCSLILTGSMDKTCMLWDATSGKYVATLTGHDDEILDSCFDYTGKLIATASADGTARVYNATTRKCVTKLEGHEGEISKISFNPQGNRLLTGSSDKTARIWDVQTGQCLQVLEGHTDEIFSCAFNYKGNIVITGSKDNSCRIWR
Protein: 5-hydroxytryptamine receptor 2B (Serotonin receptor 2B) (Q50DZ8)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
Sequence:
MAISYRISEQSTIPEHILQSSFHHLIFANWSGLQTESIPEEMKQTGEQQGKKPQWAALLILTVIIPTIGGNILVILAISLEKKLQYATNYFLMSLAVADLLVGLFVMPIALLTIMFETIWPLPLVLCPAWLFLDVLFSTASIMHLCAISVDRYIAIKKPIQANQSNSRATAFIKITVVWLISIGIAIPVPIRGIETDRSNPSNITCVLTKDRFGNFMLYGSLAAFFTPLAIMIVTYFLTIRALQKKASLVKNKPPPCLTWLTVSTAFRRNETPCSSPEKVAMLDGSHKDRTLPSSSDDLLMRRMSTAGKKSMQTISNEQRASKVLGIVFFLFLLMWCPFFITNVTLVLCDSCNQTTLNMLLEVFVWIGYVSSGVNPLVYTLFNKTFRNAFGRYITCNYQAMKSVKTVRKCSSNNYFRNGRELKVFHETWNVKWY
Protein: H(+)/Cl(-) exchange transporter 6 (Chloride channel protein 6) (ClC-6) (Chloride transport protein 6) (P51797)
Organism: Homo sapiens (Human)
Function: Voltage-gated channel mediating the exchange of chloride ions against protons. Functions as antiporter and contributes to the acidification of the late endosome lumen. The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:17534424, ECO:0000269|PubMed:33217309}; Multi-pass membrane protein {ECO:0000269|PubMed:17534424}.
Interaction partners:
- Protein FAM131B
- Methylenetetrahydrofolate reductase
- Osteopetrosis-associated transmembrane protein 1
- Type-1 angiotensin II receptor-associated protein
- UPF0606 protein KIAA1549
- Palmitoyl-protein thioesterase 1
- Serine/threonine-protein kinase B-raf
- Trafficking kinesin-binding protein 1
Sequence:
MAGCRGSLCCCCRWCCCCGERETRTPEELTILGETQEEEDEILPRKDYESLDYDRCINDPYLEVLETMDNKKGRRYEAVKWMVVFAIGVCTGLVGLFVDFFVRLFTQLKFGVVQTSVEECSQKGCLALSLLELLGFNLTFVFLASLLVLIEPVAAGSGIPEVKCYLNGVKVPGIVRLRTLLCKVLGVLFSVAGGLFVEKEGPMIHSGSVVGAGLPQFQSISLRKIQFNFPYFRSDRDKRDFVSAGAAAGVAAAFGAPIGGTLFSLEEGSSFWNQGLTWKVLFCSMSATFTLNFFRSGIQFGSWGSFQLPGLLNFGEFKCSDSDKKCHLWTAMDLGFFVVMGVIGGLLGATFNCLNKRLAKYRMRNVHPKPKLVRVLESLLVSLVTTVVVFVASMVLGECRQMSSSSQIGNDSFQLQVTEDVNSSIKTFFCPNDTYNDMATLFFNPQESAILQLFHQDGTFSPVTLALFFVLYFLLACWTYGISVPSGLFVPSLLCGAAFGRLVANVLKSYIGLGHIYSGTFALIGAAAFLGGVVRMTISLTVILIESTNEITYGLPIMVTLMVAKWTGDFFNKGIYDIHVGLRGVPLLEWETEVEMDKLRASDIMEPNLTYVYPHTRIQSLVSILRTTVHHAFPVVTENRGNEKEFMKGNQLISNNIKFKKSSILTRAGEQRKRSQSMKSYPSSELRNMCDEHIASEEPAEKEDLLQQMLERRYTPYPNLYPDQSPSEDWTMEERFRPLTFHGLILRSQLVTLLVRGVCYSESQSSASQPRLSYAEMAEDYPRYPDIHDLDLTLLNPRMIVDVTPYMNPSPFTVSPNTHVSQVFNLFRTMGLRHLPVVNAVGEIVGIITRHNLTYEFLQARLRQHYQTI
Protein: Probable phosphoglycerate mutase 4 (EC 5.4.2.11) (EC 5.4.2.4) (Q8N0Y7)
Organism: Homo sapiens (Human)
Interaction partners:
- Phosphoglycerate kinase 1
- Alpha-enolase
- Beta-enolase
- Phosphoglycerate mutase 2
- Gamma-enolase
- Phosphoglycerate kinase 2
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase A
- Enolase 4
- Glucose-6-phosphate isomerase
Sequence:
MAAYKLVLIRHGESTWNLENRFSCWYDADLSPAGHEEAKRGGQALRDAGYEFDICLTSVQKRVIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSYESPKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLQGIAKHVEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVCKAIEAVAAQGKAKK
Protein: LIM interaction domain-containing protein (Q9U3E2)
Organism: Caenorhabditis elegans
Interaction partners:
- Single-stranded DNA-binding protein homolog sam-10
- LIM/homeobox protein ttx-3
- LIM/homeobox protein lim-7
- LIM/homeobox protein ceh-14
- DUF281 domain-containing protein
- Uncharacterized protein D2007.2
- PSI domain-containing protein
- DDHD domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- GTP-binding protein drn-1
Sequence:
MCVVIFLKFLFSDNGNNQHGTEAAFGRLAQSYRIQDLLFIIVIFFRAIHIMMFHRPPSARPPLNHVDQLKSLQATALGKPGMRSQATEPQPIGNTVSPLEFRIHDMNRRLYIFSSTGVSENDQQQWWDAFSHEFFDDDCKLWFVIGSEPVAFASRERYIINRQFIPKFFRSIFDSGMRELQYVLRGPSRECTLANGSQAYENENVLQITRYDQSSQFEVNTEGKLYVEFAPFDEVMNYRIKAWTLELKRSNEFVYNQNTADYRVEAQNPEQENKPRMGFFKSTFNLMTMLKILDPMQSIMSSAKSAPAITPREVMKRTLFQHHQVRQQNMRQQQLNQQMMIPAPEPEKPKPARKRQRKPAANPRGSKKATAAAAAAAAAATNGVPPTVPTASPANNQQFPPNPMTSQFQQMSYPDVMVVGEPSMMGSEFGENDERTISRVENSQYDPNAMQMQSLGQGPNSSMNINGRNMMNQHHPGMQPPPGQQHMPPHSMGSQMPTSMHNPMHMPPGSMQGHGGMPPMPSTMANQMPPPNLPPHTMSNQMPNSRMPPMQGQMPPSGMPGQMSNPNMMGSGMPPMSMSSQMPGSMSNPMPNQMPGGMQMNQMPPPNYSQYTGGPPPQWPPPNSAMITG
Protein: Cytochrome P450, family 2, subfamily r, polypeptide 1 (A0A8I6A0G3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}. Microsome membrane {ECO:0000256|ARBA:ARBA00004524}.
Interaction partners:
Sequence:
MFQLPGVQTCAGALAGAFLLLLLVLVVRQLLRQRRPAGFPPGPPRLPFIGNICSLALSADLPHVYMRKQSRVFGEIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWIDHRRLAVNSFHYFGSGQKSFESKILEETWSLIDAIETYKGRPFDLKQLITNAVSNITNLILFGERFTYEDTDFQHMIELFSENVELAASAPVFLYNAFPWIGILPFGKHQRLFRNADVVYDFLSKLIEKAAVNRKPHLPQNFVDAYLDEMDKGQNDPLSTFSKENLIFSVGELIIAGTETTTNVLRWAVLFMALYPNIQGQVHKEIDLIMGHDRRPSWEDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWKDPDMFYPERFLDSSGYFTKKEALIPFSLGRRHCLGEQLARMEMFLFFTSLLQQFHLHFPHELVPNLKPRLGMTLQPQAYLICAERR
Protein: 2-heptyl-3-hydroxy-4(1H)-quinolone synthase (EC 1.14.13.182) (2-heptyl-3,4-dihydroxyquinoline synthase) (Q9I0Q0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the terminal step of the biosynthesis of quinolone which in addition to serve as a potent signal for quorum sensing, chelates iron and promotes the formation of membrane vesicles (MVs). Catalyzes the hydroxylation of 2-heptyl-4-quinolone (C7-HHQ) to yield 2-heptyl-3-hydroxy-4-quinolone (PQS).
Interaction partners:
- 2-heptyl-4
- 2-heptyl-4
- Probable FAD-dependent monooxygenase
- Acyl-homoserine-lactone synthase
- Anthranilate--CoA ligase
- HTH-type quorum-sensing regulator RhlR
- Multiple virulence factor regulator MvfR
- Anthraniloyl-CoA anthraniloyltransferase
- Acyl-homoserine-lactone synthase
- 2-aminobenzoylacetyl-CoA thioesterase
Sequence:
MTVLIQGAGIAGLALAREFTKAGIDWLLVERASEIRPIGTGITLASNALTALSSTLDLDRLFRRGMPLAGINVYAHDGSMLMSMPSSLGGNSRGGLALQRHELHAALLEGLDESRIRVGVSIVQILDGLDHERVTLSDGTVHDCSLVVGADGIRSSVRRYVWPEATLRHSGETCWRLVVPHRLEDAELAGEVWGHGKRLGFIQISPREMYVYATLKVRREEPEDEEGFVTPQRLAAHYADFDGIGASIARLIPSATTLVHNDLEELAGASWCRGRVVLIGDAAHAMTPNLGQGAAMALEDAFLLARLWCLAPRAETLILFQQQREARIEFIRKQSWIVGRLGQWESPWSVWLRNTLVRLVPNASRRRLHQRLFTGVGEMAAQ
Protein: Prolactin (Q6LDQ9)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
VTEVRGMKGAPDAILSRAIEIEEENKRLLEGMEMIFGQVIPGAKETEPYPVWSGLPSLQTKDEDARYSAFYNLLHCLRRDSSKIDTYLKLLNCRIIYNNNC
Protein: Peroxisomal membrane protein PEX13 (Peroxin-13) (Q7JRD4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome membrane {ECO:0000256|ARBA:ARBA00046271}.
Interaction partners:
- Peroxin-19
- Peroxisomal membrane protein PEX14
- Peroxisomal targeting signal 1 receptor
- Peroxisome assembly protein 12
- RING-type E3 ubiquitin transferase
- Peroxin-7
- Peroxin 11
- Peroxisomal biogenesis factor 3
- Peroxisomal membrane protein PEX16
- Peroxisome biogenesis factor 2
Sequence:
MVDNNNLRSAVISDAPLLPPSSSIGVGVSSGGGYPPEAVLRTPYGNVRALPGPAQPPPLPQSPFQQTQQYGGFGSGYGGNNYGLGGYGGFNSGAFGYGGLGGFGSGLGSGFGSGYGYGGGYGGGYGGGFGGGYNRFGAMGENDAEQRFIYMAESSSRPAFQSIESLVSAIGNIASMLDSTFFALTSSFRAILGVATNFVRLRSVFAQFWTTFAIFRGLNWMYRKILYWLRLSNLDPSSAAFKKAFAEALNENNGQARGAPNVPRKGNSPWPVLAFISFIFTAPYLIMKLLGTVTNTAQEEARNPAKWTAPIQTQAVYEFVARSPSELSLRAGQMLHVAPRDIQQTLNLLNTGWALATTNGQTSGIIPISYVKSPQQMRQEMQDQTKPAQPQPELMNLSAGAFASPPLEQQMNYDFNLAAQQQAPLGPPSTTSAVLGEGFA
Protein: Zw10 protein (Q8UUR2)
Organism: Gallus gallus (Chicken)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSVSVTVISPQGEVCTMITKKYSEFLPGMQSAEELVARVDGLSRSVDLLRAGVENEVQRDLTVAVAEFTELKQQLEQDTLVLSILKKLQEFDTALKEYNTALLEKRYIEAAQQLEKARSSLKTLESRKGFELKILKALRTELTVQTQNMLYHLGEEWQKLAVWKLPPSKETIGPESVMHSELHLCTLPSKEEEIAGPPVASVLQAFAVLGELHTKLKTFGKLLLKYILKPLISYPFLQPFVEEQSDVVILKFKSEKPDLDHSSPVEVFDKIKFILEVLHKYLLNVPVEQCVEDKKECRVTLAELLGDMMWEELSDCLIQNCLVNSIPTNSSKLEQYIEVIKSTEEFEKALKKMQFLKGDTTDLLKYARNVNSHFANKKCQDVIVAARNLMTSEIHNTVKITPDSSVALPKLPDPGSGDHVKMQKTSKLPNEMVNLENDSKLSQYTFSLPTCRISASVEKLMELAYQTLLETTASTDQCCIQLFYSVRNIFQLFYDVVPTYHKENLQKLPQLAAIHHNNCMYIAHHLLTMGHQFRYRLTNILCDGACYLVDLEPGYRRLGMECFLAQMRVQKGEILERLSSARNFSNMDDEENYSAANKAIRQVLHQLKRLGKVWQDVLPVNVYCKAMGTLLNTALSEIVTRIAALEDISAEDADRLYSLCRIMVEEGPQVFTPLPEEDKNKKYQEEVPVYVQKWTTFKELMIILQANLQEIVDQWADGKGPLAAEFSPAEVKSLIRALFQNTERRAAALAKIK
Protein: Siderophore iron transporter 1 (Ferrioxamine B permease) (Siderophore iron transporter ARN3) (P39980)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the transport of siderophore ferrioxamine B and so has a role in iron homeostasis.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:10744769, ECO:0000269|PubMed:10748025}; Multi-pass membrane protein {ECO:0000269|PubMed:10744769, ECO:0000269|PubMed:10748025}.
Interaction partners:
- Plasma membrane iron permease
- Iron transport multicopper oxidase FET3
- Facilitator of iron transport 2
- Iron-regulated transcriptional activator AFT1
- mRNA decay factor CTH2
- Facilitator of iron transport 3
- Probable electron transfer flavoprotein subunit beta
- Ferric/cupric reductase transmembrane component 1
- Copper-transporting ATPase
- Iron transporter FTH1
Sequence:
MDPGIANHTLPEEFEEVVVPEMLEKEVGAKVDVKPTLTTSSPAPSYIELIDPGVHNIEIYAEMYNRPIYRVALFFSLFLIAYAYGLDGNIRYTFQAYATSSYSQHSLLSTVNCIKTVIAAVGQIFFARLSDIFGRFSIMIVSIIFYSMGTIIESQAVNITRFAVGGCFYQLGLTGIILILEVIASDFSNLNWRLLALFIPALPFIINTWISGNVTSAIDANWKWGIGMWAFILPLACIPLGICMLHMRYLARKHAKDRLKPEFEALNKLKWKSFCIDIAFWKLDIIGMLLITVFFGCVLVPFTLAGGLKEEWKTAHIIVPEVIGWVVVLPLYMLWEIKYSRHPLTPWDLIQDRGIFFALLIAFFINFNWYMQGDYMYTVLVVAVHESIKSATRITSLYSFVSVIVGTILGFILIKVRRTKPFIIFGISCWIVSFGLLVHYRGDSGAHSGIIGSLCLLGFGAGSFTYVTQASIQASAKTHARMAVVTSLYLATYNIGSAFGSSVSGAVWTNILPKEISKRISDPTLAAQAYGSPFTFITTYTWGTPERIALVMSYRYVQKILCIIGLVFCFPLLGCAFMLRNHKLTDSIALEGNDHLESKNTFEIEEKEESFLKNKFFTHFTSSKDRKD
Protein: 26S proteasome non-ATPase regulatory subunit 9 (26S proteasome regulatory subunit p27) (dp27) (Q9VFS8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC).
Interaction partners:
- 26S proteasome regulatory complex subunit p50
- Regulatory particle triple-A ATPase 4
- 26S proteasome non-ATPase regulatory subunit 1
- AT06668p
- 26S proteasome regulatory subunit 8
- 26S proteasome non-ATPase regulatory subunit 6
- GH11341p
- 26S proteasome regulatory subunit 6B
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 2
Sequence:
MAAGTTTKERLERLINAKKQLEAQINRNGQILAANDNVGMSGPLVDAEGFPRNDIDVYQVRLARQTIICLQNDHKELMNQIQTLLNQYHSEIATTDPELVNRASALDLDSDRSPGGANITDLAPARAIVVVNLVSPDSPAERAGLCAGDAILRFGSINSGNFKGDLAQIGELVRNMQSQNVQLKVKRGEQQLDLILVPKTWSGRGLLGCNIVLPPEAMDH
Protein: Monoglyceride lipase (MGL) (EC 3.1.1.23) (Monoacylglycerol lipase) (MAGL) (O35678)
Organism: Mus musculus (Mouse)
Function: Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol, and thereby contributes to the regulation of endocannabinoid signaling, nociperception and perception of pain. Regulates the levels of fatty acids that serve as signaling molecules and promote cancer cell migration, invasion and tumor growth (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18096503}. Membrane; Peripheral membrane protein {ECO:0000269|PubMed:18096503}.
Interaction partners:
- Patatin-like phospholipase domain-containing protein 2
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- Lipoprotein lipase
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- Fatty-acid amide hydrolase 1
- Glycerol kinase
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
Sequence:
MPEASSPRRTPQNVPYQDLPHLVNADGQYLFCRYWKPSGTPKALIFVSHGAGEHCGRYDELAHMLKGLDMLVFAHDHVGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFLLGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTLKVLAAKLLNFVLPNMTLGRIDSSVLSRNKSEVDLYNSDPLVCRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRLCDSKGAYLLMESSRSQDKTLKMYEGAYHVLHRELPEVTNSVLHEVNSWVSHRIAAAGAGCPP
Protein: RecQ-like DNA helicase blm-1 (EC 5.6.2.4) (Bloom syndrome protein homolog) (DNA 3'-5' helicase BLM) (High incidence of males protein 6) (RecQ helicase homolog) (O18017)
Organism: Caenorhabditis elegans
Function: Component of the BTR double Holliday Junction dissolution complex, which is involved in homologous recombination during meiotic double strand break in the germline (Probable). Stabilizes and positively regulates the localization of the BTR double Holliday Junction dissolution complex component rmh-1 at nuclear foci during meiotic recombination. Participates in DNA replication and repair (By similarity). Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction (By similarity). Negatively regulates sister chromatid exchange (SCE).
Subcellular location: Nucleus {ECO:0000269|PubMed:27011106, ECO:0000269|PubMed:34252074}. Chromosome {ECO:0000269|PubMed:27011106}. Note=Localizes on chromosomes during pachytene in meiotic prophase I in oocytes. Co-localizes with rmh-1 at mid-pachytene and late-pachytene in meiotic prophase I (PubMed:27011106). Localization at nuclear foci is dependent on rmh-1 during meiotic recombination (PubMed:27011106). {ECO:0000269|PubMed:27011106, ECO:0000269|PubMed:34252074}.
Interaction partners:
- DNA topoisomerase 3
- RecQ-mediated genome instability protein 1
- Exonuclease 1
- Crossover junction endonuclease MUS81
- DNA repair protein RAD51 homolog
- DNA repair endonuclease XPF
- DNA mismatch repair protein S5 domain-containing protein
- Probable replication factor A 73 kDa subunit
- Structure-specific endonuclease subunit SLX1 homolog
- Replication protein A C-terminal domain-containing protein
Sequence:
MIKNREIEVAPPRRTIQFGGYTFVEPDLNFKAPIFSCCGSIRDPSCEEREEEYIDNGHDEEPPVEVNRIQESTSFDEPVSSPPRYRPSENPGPSSSSYEPGHYSFNEYQQFPSRPQKRLVDPPIVDLDEEPPIVDLDDSFDNFHVGSTSEEVVSGDIAPEEEEEEGHDSFDDFESVPAQPPSKNTLASLQKSDSEIALNQQRHDMHGRFRGFLQDDSEEFSDEVGLLGADMNKELYDTLKSKFGFNQFRHRQKQCILSTLMGHDTFVLMPTGAGKSLCYQLPAVILPGVTVVVSPLRSLIEDQKMKMKELGIGCEALTADLGAPAQEKIYAELGSGNPSIKLLYVTPEKISASGRLNSVFFDLHRRGLLARFVIDEAHCVSQWGHDFRPDYTKLSSLREKYANPPVPIIALTATATPKIVTDARDHLKMQNSKLFISSFVRDNLKYDLIPKAARSLINVVEKMKQLYPGKSGIVYCLSRKECETVQMMLTKAGLSAEVYHAGLNDNLRVSVQRSWIANKFDVICATIAFGMGIDKPDVRFVIHYSLPKSIEGYYQETGRAGRDGMPSYCLMLYSYHDSIRLRRMIEEGNTTTGVRSMHLNNVLQVVAYCENVSVCRRKMLVEHFGEVYDEQSCRNSKTPCDICERQRKNAEAIRLFDVSTDALSILKCLPRMQKATLKYISELYRGALIKKSQEQAMRLGHTKLPFYSKGQGMSEQDALRFVRKLVIEGYIHERLYSVPNQAAAVFAYAELTEAGRDLANGKKTAKVYLHIVTCERKRKNAGLIELSNMNIVSEAQALKERHMVKHGDVFTRCLQDLTHLITAVAESSGLSGPYSIVSREGIEQIAALLPRTNSDLLRIDSMTQIKVTKYGRLIMELLATYWKQVDEREEEEMRNQLDKLKSGEIVMGGFATLQSDPGFPSVPYMKPLGGGGGCRGRGKKRAFSGFSSGRATKKPRATAPSARGKTSGRGGAKPATSLKRNMYPATSM
Protein: Putative eukaryotic translation initiation factor eIF-4E (E9ADE1)
Organism: Leishmania major
Interaction partners:
- Probable eukaryotic initiation factor 4A
- 4E-interacting protein
- Putative eukaryotic translation initiation factor 4 gamma
- Eukaryotic translation initiation factor-like
- Polyadenylate-binding protein
- Putative eukaryotic translation initation factor 4 gamma
- Putative eukaryotic initiation factor 4a
- Putative eukaryotic initiation factor 4a
- Putative eukaryotic initiation factor 4a
- Probable eukaryotic initiation factor 4A
Sequence:
MSAPSSVPPHKMANLHKLQRAWTLWYDSPSTYNTENWEMSLVPIMTVHSVEEFFVMLRYMKPLHALRTSSQYHFFQEGVKPMWEDPANKKGGKLWVNLDITSANGRSSNNNTSGTSAADGSAAEAKTDLDKAWENVLMATVGEYLDCVDKKDTPTEPFVTGIVMSKRKYHNRLAVWVSDASATDKIEALKKALTKEASLAPIASMVFTKHGEAS
Protein: Lysine-rich membrane-associated PHISTb protein (Q8I3F0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MRFTNSLYSIKNNSIFDMNYLKIDNSGNYNFGEEKNKNKNAKSCFKSLLSKPIVMIIAGILYIVILNVCMRERNFNYEVQFSNRYSRKLCERFIYYNPNVQGVYPDMFIASSSQTYSDGSEYDVMKYANKVIKDLKEHDLWNDHNKVPYTSVYMGVSVQDIDYILDKKIDNLDLYDENIIDSMKYIWNEVMDKEKKRFLGLKNVLRKYQEEFPINNTVINNYNKKKFDKCYERIDLGADIIENGLNKMLSKCIKKNVLDKNQYKVLVTANRFLWRKSLLDVQEECNVILQLPTEVSKLPKKKKLRNRRKSNPNNEISLRTYGQSTNPQVYRRPNYYPSNSAPHVIDYIYKVGYGDNADEDVDKHIEYLVERMAEEEAERIAELSVEPYIEALEASYDAIAYRNAQNRIQKIPKKNPEMLTENQINEEENENTKVGGANTKVRGENKKVRGANKKVRGANKKVGSKNTKVGGENKKAGSSNKKAGNEKEKAGTENKKAGTENKKAGTENKKAGTENTKDKSGKENKKKN
Protein: Stretchin-MLCK (Q9NBA9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
LPLGNQTVCNGGTVAISAEFMETSTPIEVKWLRDRRVVDGPNVKALADRGVYTLTIMNAGPEVEGTYTCRASNAFGRIESNVNVDVAVGAEKDERPPLFLSRPDTEMKIAVGDPFSLSFRIAGDPKPKLTFMKGTKDITQSDRVSKEVSDDYTRFSVQQAQISDSGTYFVVARNNFGTDRIFVTVTIKXPKKKKKKKKKLG
Protein: D-phenylhydantoinase (EC 3.5.2.-) (Hydantoin-utilizing enzyme HyuA) (Q46806)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives with an aromatic side chains at the 5'-position. Has no activity on dihydropyrimidines. The physiological function is unknown.
Interaction partners:
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreA
- Aspartate carbamoyltransferase catalytic subunit
- Uncharacterized protein YgeY
- NAD-dependent dihydropyrimidine dehydrogenase subunit PreT
- Putative carbamoyltransferase YgeW
- Diaminopropionate ammonia-lyase
- Putative oxidoreductase YgfK
- Carbamoyl phosphate synthase large chain
- Carbamoyl phosphate synthase small chain
- Putative aminohydrolase SsnA
Sequence:
MRVLIKNGTVVNADGQAKQDLLIESGIVRQLGNNISPQLPYEEIDATGCYVFPGGVDVHTHFNIDVGIARSCDDFFTGTRAAACGGTTTIIDHMGFGPNGCRLRHQLEVYRGYAAHKAVIDYSFHGVIQHINHAILDEIPMIVEEGLSSFKLYLTYQYKLNDDEVLQALRRLHESGALTTVHPENDAAIASKRAEFIAAGLTAPRYHALSRPLECEAEAIARMINLAQIAGNAPLYIVHLSNGLGLDYLRLARANHQPVWVETCPQYLLLDERSYDTEDGMKFILSPPLRNVREQDKLWCGISDGAIDVVATDHCTFSMAQRLQISKGDFSRCPNGLPGVENRMQLLFSSGVMTGRITPERFVELTSAMPARLFGLWPQKGLLAPGSDGDVVIIDPRQSQQIQHRHLHDNADYSPWEGFTCQGAIVRTLSRGETIFCDGTFTGKAGRGRFLRRKPFVPPVL
Protein: Complement C3 [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc) (Neutrophil chemotactic factor-2) (ENCF-2); Complement C3 alpha chain; C3a anaphylatoxin (Neutrophil chemotactic factor-1) (ENCF-1); Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2] (P01026)
Organism: Rattus norvegicus (Rat)
Function: C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates.
Subcellular location: Secreted.
Interaction partners:
- Complement factor B
- Complement factor H
- Complement C2
- C3a anaphylatoxin chemotactic receptor
- Complement factor D
- Complement factor I
- Plasminogen
- Properdin factor, complement
- Complement C3d receptor 2.
- Integrin beta
Sequence:
MGPTSGSQLLVLLLLLASSLLALGSPMYSIITPNVLRLESEETFILEAHDAQGDVPVTVTVQDFLKKQVLTSEKTVLTGATGHLNRVFIKIPASKEFNADKGHKYVTVVANFGATVVEKAVLVSFQSGYLFIQTDKTIYTPGSTVFYRIFTVDNNLLPVGKTVVIVIETPDGVPIKRDILSSHNQYGILPLSWNIPELVNMGQWKIRAFYEHAPKQTFSAEFEVKEYVLPSFEVLVEPTEKFYYIHGPKGLEVSITARFLYGKNVDGTAFVIFGVQDEDKKISLALSLTRVLIEDGSGEAVLSRKVLMDGVRPSSPEALVGKSLYVSVTVILHSGSDMVEAERSGIPIVTSPYQIHFTKTPKFFKPAMPFDLMVFVTNPDGSPARRVPVVTQGSDAQALTQDDGVAKLSVNTPNNRQPLTITVSTKKEGIPDARQATRTMQAQPYSTMHNSNNYLHLSVSRVELKPGDNLNVNFHLRTDAGQEAKIRYYTYLVMNKGKLLKAGRQVREPGQDLVVLSLPITPEFIPSFRLVAYYTLIGANGQREVVADSVWVDVKDSCVGTLVVKGDPRDNRQPAPGHQTTLRIEGNQGARVGLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKNYAGVFMDAGLTFKTNQGLQTDQREDPECAKPAARRRRSVQLMERRMDKAGQYTDKGLRKCCEDGMRDIPMPYSCQRRARLITQGESCLKAFMDCCNYITKLREQHRRDHVLGLARSDVDEDIIPEEDIISRSHFPESWLWTIEELKEPEKNGISTKVMNIFLKDSITTWEILAVSLSDKKGICVADPYEITVMQDFFIDLRLPYSVVRNEQVEIRAVLFNYREQEKLKVRVELLHNPAFCSMATAKKRYYQTIEIPPKSSVAVPYVIVPLKIGLQEVEVKAAVFNHFISDGVKKILKVVPEGMRVNKTVAVRTLDPEHLNQGGVQREDVNAADLSDQVPDTDSETRILLQGTPVAQMAEDAVDGERLKHLIVTPSGCGEQNMIGMTPTVIAVHYLDQTEQWEKFGLEKRQEALELIKKGYTQQLAFKQPISAYAAFNNRPPSTWLTAMWSRSFSLAANLIAIDSQVLCGAVKWLILEKQKPDGVFQEDGPVIHQEMIGGFRNTKEADVSLTAFVLIALQEARDICEGQVNSLPGSINKAGEYLEASYLNLQRPYTVAIAGYALALMNKLEEPYLTKFLNTAKDRNRWEEPGQQLYNVEATSYALLALLLLKDFDSVPPVVRWLNDERYYGGGYGSTQATFMVFQALAQYRADVPDHKDLNMDVSLHLPSRSSPTVFRLLWESGSLLRSEETKQNEGFSLTAKGKGQGTLSVVTVYHAKVKGKTTCKKFDLRVTIKPAPETAKKPQDAKSSMILDICTRYLGDVDATMSILDISMMTGFIPDTNDLELLSSGVDRYISKYEMDKAFSNKNTLIIYLEKISHSEEDCLSFKVHQFFNVGLIQPGSVKVYSYYNLEESCTRFYHPEKDDGMLSKLCHNEMCRCAEENCFMHQSQDQVSLNERLDKACEPGVDYVYKTKLTTIELSDDFDEYIMTIEQVIKSGSDEVQAGQERRFISHVKCRNALKLQKGKQYLMWGLSSDLWGEKPNTSYIIGKDTWVEHWPEAEERQDQKNQKQCEDLGAFTETMVVFGCPN
Protein: SP9 (Q64HY4)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
RRYSGRATCDCPNCQEAERLGPAGASLRRKGLHSCHIPGCGKVYGKTSHLKAHLRWHTGERPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFACPVCNKRFMRSDHLSKHIKTHNGGGGGKKGSDSDTDASNLETPRSESPDLLLHDGAAAARGPGKEPPGGPGDS