wanglab/gogpt-training-data huggingface dataset:
Protein: Four domain-type voltage-gated ion channel alpha-1 subunit (Q6Q762)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLARKNSSSRGAPGSAAGFGARESIAAISDMLSSQHKKPVRSSYVESDRVEWALKIACTISMITVCIHTPRTIELFQPLNYIILAADFISVSIFMLDSVLRIHYEGIFRCDSSYLSNRWSQFSVFISIIHLLSFLLHCYQLIDNFFPFLHLNYRAWYGAIRSIRPFIIIRLIPLVVKFKLPKNRIEQLLKRSSQQVKNVTLFFVFFMTLYAIFGIQLFGRMDYHCVQPKTDPNNVTIMDLAIPDTMCAPEGIGGYECPAPMVCMQLNLNAKGEGFYGMFNDFGASVFTVYLAASEEGWVYVLYDCMDSLPSYLAFLYFCTLIFFLAWLVKNVFIAVITETFAEIRVQFSEMWQKKEVTLDEGFRKKLEKTDDGWRLIRLDGEVEPEGPKQKLQWMLRSMYFQCFVIIFVVINAIGNAMFVYRHDETDKPRKYNFYLFEVGFTILFNVECIIKILCYGFRNFIRRGIFKFELILCLGSSLNCVKFFYERNYFTYFQTFRLLRLIKASPILEDFVWKIFSPGKKLGGLVIFTIAFICCYSAISLQLFYSVPNLHHFRTFPQAFMSMFQIITQEGWTDFVVEVLRATDDNLVPLVALYFVAYHLFVTLIVLSLFVAVILDNLEMDEELKKVKQLRAREATTSMRSTLPWRLRVFEKFPTRPQMAAMRKADSDFPMPKVRGSFTHQFAVDHSLETTDVIESDFEFPKRIMKSAGKRKISKSGLTFRQIGSTSLRCSLNNLLEMSDRTRQSLSNSLSFLPHFTRSSGSLYPRKDALPKSRSMTGKFLQTAVRNKQFNMYSENGDLSRPSDSAPKKNAKQGEIDIRALQQKRQLAEITRNRIEEDMRENHPFFDRPLFLVGRASQLREFCKKMVHSKYDSQDDGTNGGAKTKKRFKEIRALIGIMPYIDWAMATVTIVSCISMLFESPWPTTGENLVMNNGYLQISDYFFVLSMTFELCVKIIANGLFFTPKAVVRDVGGVMNLFIYFTSVIFLAWMPKHVEINSLAQFLMICRAMRPLRIYTLVPHIRRVVLEFFRGFKEILLVTILMIVVMFIFASFGVQIVGGKLAACNDPTVSSRENCTGVFWQKLFVTRLEVYGKDTEAMHPKIMVPRVWTNPRNFNFDHVGNAMLALFETLSFKGWNVIRDILWSRHGPWAVVFIHIYVFIGCMIGLTLFVGVVIANYTQNRGTALLTVDQRRWHDLKARLKMAQPLHVPPKPSESARLRTKLYDLTMSRWFNQAFALLVVLNSFTLVIPWNVEEEEQRATYVFTVTALAAFMNMLFVIEIILKVIAYTFSGFWQSRRNRVDLLITVFGVIWIFLHFFVALPSSKIDVDVQVELKKFTYTFGYLVVILRFFTIASRNSTLKMLMLTVIMSMFRSFFIITALFLLVLFYAYTGVILFPMVKYGMAVSKHVNFRTASEALVVLFRCLTGEDWNDIMHDCMRSAPFCYWNEGMNYWETDCGNFYGAIIYFCSFYLIITYIVRNLLVAVIMENFSLFYSSEEDALLSYADIRNFQYVWNMVDQEQKRTIPVERVKFLLRLLKGRLEVDPEKDRILFKHMCYEMERLHNGEEVSFHDVLYMLSYRSVDIRKSLQLEELLQREELEFIIEEEVAKQTIRTWLEGCLRKMRNPSQKDAEGVLPFGGGHPVIHSSGHSSISHEETVAQRLRFENIRGDSVDTEETESSEEETPPPIRKKAAVKNRRGSIPDVLSRTGLFQEAARKFMVGSSSEKKQVKSRSPETVQLLPKRANSEIRKGSGQPKNFHLQLNVYDLPDVEERGEDSPFSPKNLSDDFNGEHSPLVITPSLPVPPTHGSPRPLMPCETTKDIEKWWNSLVD
Protein: RNA helicase (EC 3.6.4.13) (Q20935)
Organism: Caenorhabditis elegans
Interaction partners:
- Prion-like-
- MIF4G domain-containing protein
- Probable elongation factor 1-gamma
- Eukaryotic initiation factor 4A
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit I
- Small ribosomal subunit protein RACK1
- Ubiquitin-like domain-containing protein
- Elongation factor 2
- Large ribosomal subunit protein uL30
Sequence:
MTDTKVTISVVDSSSSSKEGNYDEVVESFDDMELKEELLRGIYGFGFEKPSAIQKSAVAPCTTGKDVTIQSQAGSGKTVISLIDILQGIDCEDAHLQVILLAPQRGMAQRAHEQLKSLGRNLNVNATCLGFDTTAENDKISHVLMGTPKDFLSNIPSDTSRIKMFVLDEADEMLSKGFKDQIYEVFRSMPQDVQVVLLSATMPSEVLDVTNRFMRDPIRILVKKDELTLEGIRQFYINVQKDEWKFNCLCDLLKTSRETQALIFCNTRRRVTQLTEQLMSIPIKVSCFHGNMEHNEREDMVKDFNSRNTRVLVTTDLMARGMNIRKSLIINYDVSGNMENYMLRNGRQGNFGSKGLPISFFTENDISDLKKIENHYSTRIEEMPESFLEYLDEN
Protein: receptor protein-tyrosine kinase (EC 2.7.10.1) (Q9UK79)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MELAALCRWGLLLALLPPGAASTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPTNASLSFLQDIQEVQGYVLIAHNQVRQVPLQRLRIVRGTQLFEDNYALAVLDNGDPLNNTTPVTGASPGGLRELQLRSLTEILKGGVLIQRNPQLCYQDTILWKDIFHKNNQLALTLIDTNRSRACHPCSPMCKGSRCWGESSEDCQSLTRTVCAGGCARCKGPLPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTACPYNYLSTDVGSCTLVCPLHNQEVTAEDGTQRCEKCSKPCARGTHSLPPRPAAVPVPLRMQPGPAHPVLSFLRPSWDLVSAFYSLPLAPLSPTSVPISPVSVGRGPDPDAHVAVDLSRYEG
Protein: Clavesin-1 (Retinaldehyde-binding protein 1-like 1) (A6JFQ6)
Organism: Rattus norvegicus (Rat)
Function: Required for normal morphology of late endosomes and/or lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:19651769}; Peripheral membrane protein {ECO:0000269|PubMed:19651769}. Early endosome membrane {ECO:0000250|UniProtKB:Q8IUQ0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8IUQ0}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:19651769}.
Interaction partners:
Sequence:
MGPVSVLPKPQSISTWEGDLAKMTHLQAGLSPDTIEKARLELNENPDVLHQDIQQVRDMIITRPDIGFLRTDDAFILRFLRARKFHQADAFRLLAQYFQYRQLNLDMFKNFKADDPGIKRALIDGFPGVLENRDHYGRKILLLFAANWDQSRNSFTDILRAILLSLEVLIEDPELQINGFILIIDWSNFSFKQASKLTPSILKLAIEGLQDSFPARFGGVHFVNQPWYIHALYTLIKPFLKDKTRKRIFLHGNNLNSLHQLIHPEFLPSEFGGTLPPYDMGTWARTLLGPDYSDENDYTHTSYNAMYVKHTCSNLERECSPKPMKRSQSVVEAGTLKHEEKGENENTQPLLALD
Protein: Spore cortex-lytic enzyme pre-pro-form (Q188Z5)
Organism: Clostridioides difficile (strain 630) (Peptoclostridium difficile)
Interaction partners:
- Subtilisin-like serine germination related protease
- Subtilisin-like serine germination related protease
- Spore coat protein
- Cold shock protein CspB
- Stage III sporulation protein D
- Stage IV sporulation protein A
- RNA polymerase sigma factor
Sequence:
MQDGFLTVSIIDATNNRPIQNAVVNIYSMSNGSQSSSTLYQNLRSNESGQVTGLVLPAPDVDYSLQPSDVRPYSQYIVEAIADGYETVVIEGTQLLATIEARQGVPMSPRTRSKRSFSRQSELIFDIGEHTLYGTYPPKIPESNLKPLPPPTGFVVLDNPVVPEFIVVHDGLPEDSSAPNYWIPFKEYIKNIASSEIYSTWPEQTIYANVIAIISFTLNRVFTEWYRNKGYNFTITSTTAYDHKFINNRNLFEPINVVVDAIFNTFIKRPPTSRQPLLAQYCDGQKSQCPDQMTQWGSKDLGDQGYDYESILRYFYGDEIVFERAPIVSGVPVSFPGTTLQVGSSGQYVRTIQNQLNAISNSYPAVPKVIEDGIYGTDTENAVKIFQGIFGLPQSGVVDFKTWYEISRVYVATTRIASLNPLI
Protein: 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59) (3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA) (Beta-hydroxydecanoyl thioester dehydrase) (Trans-2-decenoyl-[acyl-carrier-protein] isomerase) (EC 5.3.3.14) (P0A6Q3)
Organism: Escherichia coli (strain K12)
Function: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. Is inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP.
Subcellular location: Cytoplasm.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG
- Enoyl-[acyl-carrier-protein] reductase FabI
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Acyl carrier protein
- Fatty acid metabolism regulator protein
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
Sequence:
MVDKRESYTKEDLLASGRGELFGAKGPQLPAPNMLMMDRVVKMTETGGNFDKGYVEAELDINPDLWFFGCHFIGDPVMPGCLGLDAMWQLVGFYLGWLGGEGKGRALGVGEVKFTGQVLPTAKKVTYRIHFKRIVNRRLIMGLADGEVLVDGRLIYTASDLKVGLFQDTSAF
Protein: Rho GDP-dissociation inhibitor 1 (Rho-GDI alpha) (Q802W6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAEQEPTPEQLAAIAAENEQGESVNYKAPAQKSLQEIQELDQDDESLRKYKEALLGSCAVAADPNAPNVQVTRLTLMCETAPAPLVLDLQGDLESFKKQSFILKEGVEYRIKISFKVNKEIVSGLKYVQQTFRKGVRIDKSDYMVGSYGPRPDEYEFLTPLEEAPKGMLARGTYNLKSKFTDDDKHDHLSWEWNLNIKKDWKD
Protein: Beta-2-microglobulin [Cleaved into: Beta-2-microglobulin form pI 5.3] (P61769)
Organism: Homo sapiens (Human)
Function: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. Exogenously applied M.tuberculosis EsxA or EsxA-EsxB (or EsxA expressed in host) binds B2M and decreases its export to the cell surface (total protein levels do not change), probably leading to defects in class I antigen presentation.
Subcellular location: Secreted {ECO:0000269|PubMed:1336137, ECO:0000269|PubMed:7554280}. Cell surface {ECO:0000269|PubMed:25356553}. Note=Detected in serum and urine (PubMed:1336137, PubMed:7554280). {ECO:0000269|PubMed:7554280, ECO:0000269|Ref.6}.; SUBCELLULAR LOCATION: Note=(Microbial infection) In the presence of M.tuberculosis EsxA-EsxB complex decreased amounts of B2M are found on the cell surface (PubMed:25356553). {ECO:0000269|PubMed:25356553}.
Interaction partners:
- T-cell surface glycoprotein CD1c
- HLA class I histocompatibility antigen, alpha chain E
- T-cell surface glycoprotein CD1a
- IgG receptor FcRn large subunit p51
- HLA class I histocompatibility antigen, C alpha chain
- HLA class I histocompatibility antigen, B alpha chain
- Antigen-presenting glycoprotein CD1d
- Protein disulfide-isomerase A3
- HLA class I histocompatibility antigen, A alpha chain
- Hereditary hemochromatosis protein
Sequence:
MSRSVALAVLALLSLSGLEAIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Protein: Tetraspanin 86D, isoform C (A0A0B4KFQ5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- IP12456p
Sequence:
MSNHRYHQGGNYMHPRISTYPHHFSYVSSCVKYMIFLLNFLFWLFGGLLLAIGVYAFMDKLMDGNGWLRLDTIYDVIFNISLVMIIAGVIVFTVSFAGCLGALRENTWLLKLYSMCLLLFFILEMSLAIICFVFPQYMNSFLEYQFTDKIIHSYRDDSDLQNFIDFAQQEFNCCGLSNAGYQDWSKNEYFNCSSPSVERCGVPYSCCINATDISSGLVNIMCGYGVQVRSVAAASKRIWTSGCIEIVRVWVERNLYVIAGVALGIALLQLFVIYLAKTLEGQIDLQKSRWSXVQCHHPYLYGYPPCEDDPYYNSRM
Protein: Putative pre-16S rRNA nuclease (EC 3.1.-.-) (P9WGV7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00651}.
Interaction partners:
- Alanine--tRNA ligase
- Probable shikimate 5-dehydrogenase AroE
- Endolytic murein transglycosylase
- Prepilin type IV endopeptidase peptidase domain-containing protein
- UPF0047 protein Rv2556c
- UPF0301 protein Rv0038
- Tyrosine recombinase XerC
Sequence:
MVPAQHRPPDRPGDPAHDPGRGRRLGIDVGAARIGVACSDPDAILATPVETVRRDRSGKHLRRLAALAAELEAVEVIVGLPRTLADRIGRSAQDAIELAEALARRVSPTPVRLADERLTTVSAQRSLRQAGVRASEQRAVIDQAAAVAILQSWLDERLAAMAGTQEGSDA
Protein: Flocculation protein FLO11 (Flo11p) (Flocculin-11) (Mucin-like protein 1) (P08640)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Homophilic binding protein that enables kin discrimination in heterogeneous yeast populations by mediating homotypic cell-cell interactions during flocculation, a reversible and asexual process in which cells adhere to form aggregates (flocs). Plays a role in cell-substrate adhesion, haploid invasive growth, diploid pseudohyphae formation and biofilm (flor) development. Adhesive activity is inhibited by mannose, but not by glucose, maltose, sucrose or galactose.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:10383953, ECO:0000269|PubMed:11027318, ECO:0000269|PubMed:20619652}. Membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:20619652}. Note=The protein is attached to the cell wall via a GPI-anchor and is also shed liberally into extracellular fluid; increased shedding is associated with biofilm mat expansion but decreased invasive growth. {ECO:0000269|PubMed:20619652}.
Interaction partners:
- Flocculation protein FLO1
- Flocculation protein FLO10
- Flocculation protein FLO5
- Flocculation suppression protein
- Flocculation protein FLO9
- Transcription activator MSS11
- Ty transcription activator TEC1
- Protein STE12
- Putative transcription factor PHD1
- Transcriptional regulator NRG1
Sequence:
MQRPFLLAYLVLSLLFNSALGFPTALVPRGSSEGTSCNSIVNGCPNLDFNWHMDQQNIMQYTLDVTSVSWVQDNTYQITIHVKGKENIDLKYLWSLKIIGVTGPKGTVQLYGYNENTYLIDNPTDFTATFEVYATQDVNSCQVWMPNFQIQFEYLQGSAAQYASSWQWGTTSFDLSTGCNNYDNQGHSQTDFPGFYWNIDCDNNCGGTKSSTTTSSTSESSTTTSSTSESSTTTSSTSESSTTTSSTSESSTSSSTTAPATPTTTSCTKEKPTPPTTTSCTKEKPTPPHHDTTPCTKKKTTTSKTCTKKTTTPVPTPSSSTTESSSAPVPTPSSSTTESSSAPVTSSTTESSSAPVPTPSSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPVPTPSSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPVPTPSSSTTESSSAPVTSSTTESSSAPVPTPSSSTTESSSAPVTSSTTESSSAPVPTPSSSTTESSSAPAPTPSSSTTESSSAPVTSSTTESSSAPVPTPSSSTTESSSTPVTSSTTESSSAPVPTPSSSTTESSSAPVPTPSSSTTESSSAPAPTPSSSTTESSSAPVTSSTTESSSAPVPTPSSSTTESSSAPVPTPSSSTTESSSAPVPTPSSSTTESSSAPVTSSTTESSSAPVTSSTTESSSAPVPTPSSSTTESSSAPVPTPSSSTTESSSAPVPTPSSSTTESSSAPVTSSTTESSSAPVPTPSSSTTESSSAPVPTPSSSTTESSSAPVPTPSSSTTESSVAPVPTPSSSSNITSSAPSSTPFSSSTESSSVPVPTPSSSTTESSSAPVSSSTTESSVAPVPTPSSSSNITSSAPSSIPFSSTTESFSTGTTVTPSSSKYPGSQTETSVSSTTETTIVPTKTTTSVTTPSTTTITTTVCSTGTNSAGETTSGCSPKTVTTTVPTTTTTSVTTSSTTTITTTVCSTGTNSAGETTSGCSPKTITTTVPCSTSPSETASESTTTSPTTPVTTVVSTTVVTTEYSTSTKPGGEITTTFVTKNIPTTYLTTIAPTPSVTTVTNFTPTTITTTVCSTGTNSAGETTSGCSPKTVTTTVPCSTGTGEYTTEATTLVTTAVTTTVVTTESSTGTNSAGKTTTGYTTKSVPTTYVTTLAPSAPVTPATNAVPTTITTTECSAATNAAGETTSVCSAKTIVSSASAGENTAPSATTPVTTAIPTTVITTESSVGTNSAGETTTGYTTKSIPTTYITTLIPGSNGAKNYETVATATNPISIKTTSQLATTASASSVAPVVTSPSLTGPLQSASGSAVATYSVPSISSTYQGAANIKVLGNFMWLLLALPVVF
Protein: Homeobox protein Dlx2a (DLX-2) (Distal-less homeobox gene 2a) (P50574)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in the development of the inner ear.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Crestin
- Transcription factor SOX-10
- Transcription factor sox9a
- Homeobox protein Dlx1a
- Heart- and neural crest derivatives-expressed protein 2
- LIM homeobox 6
- Sonic hedgehog protein
- Glutamate decarboxylase 1b.
- Forkhead box protein D3
- Fibroblast growth factor 8
Sequence:
MTGVFDSLSTDMHSNQITSSSYHSLHKSQESPTLPVSTATDSSINNNNQQCAGSPYGQSSSYQYQNNSMNSVQYNTKSYELGFGNAFGPYGTYGSCSSPTPADAEKEEREPEIRMVNGKPKKVRKPRTIYSTFQLAALQRRFQKTQYLALPERAELAASLGLTQTQVKIWFQNRRSKFKKLWKSGEIPPEQHVASGESPPHPSPPLAAAWDFAHSQRMNTVNSGLSQSSPPNSTTPSFLTNYPWYSSTNSAAHLQPPLHHNTTVSAGTIF
Protein: Peptidase S9 prolyl oligopeptidase catalytic domain-containing protein (Q389H4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDEFVYNRCSLNPIHWVLMLKGCLVDLFFSVRPINFSYSRVGMTNLAGERDQAACLREIRRAVRIIEGRKRTVATGTNKDSFQDMDSRCHTPERPLRLHLVLFGFSRGATTTFYTAMKLPPELATYVSLVVVEAAFDTLHNVIESSCWFPSFVLWFFRTFCDYSGEDAYKYDRNQIHLRCPIAFVMSVKDTRVPNELTQRLIDNVKADCPQIPAVEVLQLKHSRHPLMAVGNREDQDAYVAFMEGLYDRYCN
Protein: DNA replication licensing factor Mcm6 (DmMCM6) (EC 3.6.4.12) (Q9V461)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as component of the Mcm2-7 complex (Mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the Mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity Required for DNA replication and cell proliferation. Required for mitotic cycles, endocycles, and the special S phase associated with the amplification of chorion genes; has a role in origin unwinding or fork elongation at chorion loci.
Subcellular location: Nucleus {ECO:0000269|PubMed:11854416}. Note=Associated with chromatin during cell cycles.
Interaction partners:
- Double parked, isoform A
- CDC45L
- Probable DNA replication complex GINS protein PSF2
- DNA replication complex GINS protein PSF3
- DNA replication licensing factor Mcm3
- DNA replication licensing factor Mcm5
- DNA replication licensing factor MCM4
- DNA replication licensing factor Mcm2
- Cell division control protein
- DNA replication licensing factor Mcm7
Sequence:
MDVADAQVGQLRVKDEVGIRAQKLFQDFLEEFKEDGEIKYTRPAASLESPDRCTLEVSFEDVEKYDQNLATAIIEEYYHIYPFLCQSVSNYVKDRIGLKTQKDCYVAFTEVPTRHKVRDLTTSKIGTLIRISGQVVRTHPVHPELVSGVFMCLDCQTEIRNVEQQFKFTNPTICRNPVCSNRKRFMLDVEKSLFLDFQKIRIQETQAELPRGCIPRAVEIILRSELVETVQAGDRYDFTGTLIVVPDVSVLAGVGTRAENSSRHKPGEGMDGVTGLKALGMRELNYRMAFLACSVQATTARFGGTDLPMSEVTAEDMKKQMTDAEWHKIYEMSKDRNLYQNLISSLFPSIYGNDEVKRGILLQQFGGVAKTTTEKTSLRGDINVCIVGDPSTAKSQFLKQVSDFSPRAIYTSGKASSAAGLTAAVVRDEESFDFVIEAGALMLADNGICCIDEFDKMDQRDQVAIHEAMEQQTISIARAGVRATLNARTSILAAANPINGRYDRSKSLQQNIQLSAPIMSRFDLFFILVDECNEVVDYAIARKIVDLHSNIEESVERAYTREEVLRYVTFARQFKPVISQEAGHMLVENYGHLRQRDTGTSGRSTWRITVRQLESMIRLSEAMAKLECSNRVLERHVKEAFRLLNKSIIRVEQPDIHLDDDEGLDMDDGIQHDIDMENNGAAANVDENNGMDTSASGAVQKKKFTLSFEDYKNLSTMLVLHMRAEEARCEVEGNDTGIKRSNVVTWYLEQVADQIESEDELISRKNLIEKLIDRLIYHDQVIIPLKTSTLKPRIQVQKDFVEEDDPLLVVHPNYVVE
Protein: Malonate--CoA ligase ACSF3, mitochondrial (EC 6.2.1.76) (Acyl-CoA synthetase family member 3) (Q4G176)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial reaction in intramitochondrial fatty acid synthesis, by activating malonate and methylmalonate, but not acetate, into their respective CoA thioester. May have some preference toward very-long-chain substrates.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21841779, ECO:0000269|PubMed:21846720}.
Interaction partners:
- Fatty acid synthase
- Malonyl-CoA decarboxylase, mitochondrial
- Methylmalonyl-CoA epimerase, mitochondrial
- Malonyl-CoA-acyl carrier protein transacylase, mitochondrial
- 4-trimethylaminobutyraldehyde dehydrogenase
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase X, mitochondrial
- Acetyl-CoA carboxylase 1
- Aldehyde dehydrogenase family 3 member A2
- Alpha-aminoadipic semialdehyde dehydrogenase
Sequence:
MLPHVVLTFRRLGCALASCRLAPARHRGSGLLHTAPVARSDRSAPVFTRALAFGDRIALVDQHGRHTYRELYSRSLRLSQEICRLCGCVGGDLREERVSFLCANDASYVVAQWASWMSGGVAVPLYRKHPAAQLEYVICDSQSSVVLASQEYLELLSPVVRKLGVPLLPLTPAIYTGAVEEPAEVPVPEQGWRNKGAMIIYTSGTTGRPKGVLSTHQNIRAVVTGLVHKWAWTKDDVILHVLPLHHVHGVVNALLCPLWVGATCVMMPEFSPQQVWEKFLSSETPRINVFMAVPTIYTKLMEYYDRHFTQPHAQDFLRAVCEEKIRLMVSGSAALPLPVLEKWKNITGHTLLERYGMTEIGMALSGPLTTAVRLPGSVGTPLPGVQVRIVSENPQREACSYTIHAEGDERGTKVTPGFEEKEGELLVRGPSVFREYWNKPEETKSAFTLDGWFKTGDTVVFKDGQYWIRGRTSVDIIKTGGYKVSALEVEWHLLAHPSITDVAVIGVPDMTWGQRVTAVVTLREGHSLSHRELKEWARNVLAPYAVPSELVLVEEIPRNQMGKIDKKALIRHFHPS
Protein: Enkurin (Q6SP97)
Organism: Mus musculus (Mouse)
Function: Adapter that functions to localize a calcium-sensitive signal transduction machinery in sperm to a calcium-permeable ion channel. Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:E1B836}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:37295417, ECO:0000269|PubMed:37865089, ECO:0000269|PubMed:37989994, ECO:0000305|PubMed:15385169}. Note=Sperm acrosomal crescent and flagellar principal piece. {ECO:0000269|PubMed:15385169}.
Interaction partners:
- WD repeat-containing protein 90
- EF-hand domain-containing family member B
- Parkin coregulated gene protein homolog
- Cilia- and flagella-associated protein 45
- PACRG-like protein
- EF-hand domain-containing protein 1
- EF-hand domain-containing family member C2
- Cilia- and flagella-associated protein 52
Sequence:
MDSPCTSESIYNLIPSDLKEPPQHPRYTSLFRATIKNDMKKFKTAMKTMGPAKVEIPSPKDFLKKHSKEKTLPPKKKFNRCSPKKPAVPLRTDHPVMGIQSGKNFINTNAADVIMGVAKKPKPIYVDKRTGDKHDLETSGLFPKYINKKDYGITPEYICKRNEDVKKAQEEYDNYIQENLKKAAMKRLSDEEREAVLQGLKKNWEEVHKEFQSLSVFIDSVPKKIRKQKLEKEMKQLEHDISVIEKHKIIYIANK
Protein: Integrin alpha-2 (CD49 antigen-like family member B) (Collagen receptor) (Platelet membrane glycoprotein Ia) (GPIa) (VLA-2 subunit alpha) (CD antigen CD49b) (Q62469)
Organism: Mus musculus (Mouse)
Function: Integrin alpha-2/beta-1 is a collagen receptor, being responsible for adhesion of platelets and other cells to collagens, modulation of collagen and collagenase gene expression, force generation and organization of newly synthesized extracellular matrix. It is also a receptor for laminins, collagen C-propeptides and E-cadherin. Mice homozygous for a null mutation in the alpha-2 die very early in embryogenesis.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Integrin beta-1
- Fibronectin
- Collagen alpha-1
- Collagen alpha-2
- Collagen alpha-1
- Integrin beta-3
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Focal adhesion kinase 1
- Integrin beta-5
- Integrin beta-2
Sequence:
MGPGQAGGALLLRLLMLVQGILNCLAYNVGLPGAKIFSGPSSEQFGYSVQQLTNPQGNWLLVGSPWSGFPENRMGDVYKCPVDLPTATCEKLNLQNSASISNVTEIKTNMSLGLTLTRNPGTGGFLTCGPLWAHQCGNQYYATGICSDVSPDFQFLTSFSPAVQACPSLVDVVVVCDESNSIYPWEAVKNFLVKFVTGLDIGPKKTQVALIQYANEPRIIFNLNDFETKEDMVQATSETRQHGGDLTNTFRAIEFARDYAYSQTSGGRPGATKVMVVVTDGESHDGSKLKTVIQQCNDDEILRFGIAVLGYLNRNALDTKNLIKEIKAIASTPTERYFFNVADEAALLEKAGTLGEQIFSIEGTVQGGDNFQMEMAQVGFSADYAPQNDILMLGAVGAFDWSGTLVQETSHKPVIFPKQAFDQVLQDRNHSSFLGYSVAAISTEDGVHFVAGAPRANYTGQIVLYSVNKQGNVTVIQSHRGDQIGSYFGSVLCSVDVDKDTITDVLLVGAPTYMNDLKKEEGKVYLFTITKGILNQHQFLEGPEGTGNARFGSAIAALSDINMDGFNDVIVGSPVENENSGAVYIYNGHQGTIRTKYSQKILGSNGAFRRHLQFFGRSLDGYGDLNGDSITDVSIGALGQVIQLWSQSIADVAIEALFTPDKITLLNKDAKITLKLCFRAEFRPAGQNNQVAILFNMTLDADGHSSRVTSRGVFRENSERFLQKNMVVNEVQKCSEHHISIQKPSDVVNPLDLRVDISLENPGTSPALEAYSETVKVFSIPFYKECGSDGICISDLILDVQQLPAIQTQSFIVSNQNKRLTFSVILKNRGESAYNTVVLAEFSENLFFASFSMPVDGTEVTCEVGSSQKSVTCDVGYPALKSEQQVTFTINFDFNLQNLQNQAAINFQAFSESQETNKADNSVSLTIPLLYDAELHLTRSTNINFYEISSDENAPSVIKSVEDIGPKFIFSLKVTAGSAPVSMALVTIHIPQYTKEKNPLLYLTGIQTDQAGDISCTAEINPLKLPHTAPSVSFKNENFRHTKELDCRTTSCSNITCWLKDLHMKAEYFINVTTRVWNRTFAASTFQTVQLTAAAEIDTHNPQLFVIEENAVTIPLMIMKPTEKAEVPTGVIIGSIIAGILLLLAMTAGLWKLGFFKRQYKKMGQNPDEMDETTELNS
Protein: Nuclear receptor (Q21803)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
- Glycosyltransferase family 92 protein R07B7.12
- Alpha-galactosidase
- Ground-like domain-containing protein
Sequence:
MSEESNSFLPDIKVDERYCESTSNSQQSEITNETSRNVLPEKCEVCGNPAVGYHYDVATCNGCKAFFRRTVITGRRVICRRRKNCLVEMEPKNRRICPGCRFSKCEEVGMNPRAIRAEISSGGKILKDELIAKREPRSKIMLSPKSKENEVSRLISDLNLIENQIDELFNSSLPINYGDWRTLSEIIQMKPYLKVSKIPNLKLIRNQMNAELAGYAHNGSLAMVEYAKMLDFFPKISKETAIKLVKHGLFMCGSLSFSRRSIQKYNSDILRFTDGSVAGKPKTNWNGVMLDHRRIAQKTLHSILRVKLDYVEYLFLKAITMCNPAVSDFPAEDQKIIDKHRFNYAQSLLNYCLKQHGQIHGADRFASILSIMSIMEVQQKEEKSCFFVFRSIYSEFDVFVSPLFDEISNY
Protein: RE41430p (Q8MS22)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSLQTKRQHCYLCDLPRMPWAMINDFSEAVCRGCVNYEGADRIEAVLDAARQMKRLHPASKQQRSHENGEVSAAAAAAVVLQQQQQLQVGPVPGQGPGSHRGGGGGGPPGAPPGSGGPGPSGAGSLSSLGNAVAAAAAAAAVHHHHQMPYQMPVPRIGPPLDYPVKLEDAPGGGVRPVRISHMTPHHLPPNATSGGGGAPGGGVPTAGSGGGSLPPALSVNLKRPPSEDVDVDVSQQQQQSGHGLAPDGSAGNSLSAGGGVSGGCPPGIKRSAMDDPSGVGGRPPLTRGESLPAAVSYVPERQLSGLRDKQQPVRAPSFDASTFKAEHMSPASRRNGSSPPSGPLPPRSVHSPNSSGSSSGRRSSGSRHVSSTTVTSSEVGGSNPGQAVVAGGLGGGGGGGPGSNAASGQLGGPSGGSGQLSCTSGGPGGSASSGSGGNGAIGPASMAPNSVAGDGSPAGGNGPSGSNGSGGSVNPGPGSSGSQGGGGGGTPLASGGGSAGSGGLGGAPGSSAASNSAAAAAAAAAQNATLKCTLCQERLEDTHFVQCPSVNHHKFCFPCSRESIKRQNGLGNEVYCPSGDRCPLANSVIPWAFMQGEITTILGEEVKVKKERES
Protein: Isopentenyl-diphosphate delta-isomerase (IPP isomerase) (EC 5.3.3.2) (Isopentenyl diphosphate:dimethylallyl diphosphate isomerase) (Isopentenyl pyrophosphate isomerase) (Type 2 isopentenyl diphosphate isomerase) (IDI-2) (P61615)
Organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12) (Sulfolobus shibatae)
Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00354}.
Interaction partners:
Sequence:
MPDIVNRKVEHVEIAAFENVDGLSSSTFLNDVILVHQGFPGISFSEINTKTKFFRKEISVPVMVTGMTGGRNELGRINKIIAEVAEKFGIPMGVGSQRVAIEKAEARESFAIVRKVAPTIPIIANLGMPQLVKGYGLKEFQDAIQMIEADAIAVHLNPAQEVFQPEGEPEYQIYALEKLRDISKELSVPIIVKESGNGISMETAKLLYSYGIKNFDTSGQGGTNWIAIEMIRDIRRGNWKAESAKNFLDWGVPTAASIMEVRYSVPDSFLVGSGGIRSGLDAAKAIALGADIAGMALPVLKSAIEGKESLEQFFRKIIFELKAAMMLTGSKDVDALKKTSIVILGKLKEWAEYRGINLSIYEKVRKRE