wanglab/gogpt-training-data huggingface dataset:
Protein: Insulin-like peptide 4 (dILP4) (Insulin-related peptide 4) [Cleaved into: Insulin-like peptide 4 A chain; Insulin-like peptide 4 B chain] (Q9VT53)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- GEO04221p1
- Insulin-like peptide 7
- Insulin-like peptide 3
- Insulin-like peptide 6
- Insulin-like peptide 5
- Insulin-like peptide 2
- Protein spalt-accessory
- Insulin-like receptor
- Insulin receptor substrate 1
- Insulin-like peptide 1
Sequence:
MSLIRLGLALLLLLATVSQLLQPVQGRRKMCGEALIQALDVICVNGFTRRVRRSSASKDARVRDLIRKLQQPDEDIEQETETGRLKQKHTDADTEKGVPPAVGSGRKLRRHRRRIAHECCKEGCTYDDILDYCA
Protein: tRNA N6-adenosine threonylcarbamoyltransferase (EC 2.3.1.234) (N6-L-threonylcarbamoyladenine synthase) (t(6)A synthase) (t(6)A37 threonylcarbamoyladenosine biosynthesis protein TsaD) (tRNA threonylcarbamoyladenosine biosynthesis protein TsaD) (P05852)
Organism: Escherichia coli (strain K12)
Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB. TsaD likely plays a direct catalytic role in this reaction. May also be involved in the metabolism of glycated proteins, but does not show sialoglycoprotease activity against glycophorin A.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01445, ECO:0000269|PubMed:19376873}.
Interaction partners:
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaB
- tRNA threonylcarbamoyladenosine biosynthesis protein TsaE
- Threonylcarbamoyl-AMP synthase
- Uncharacterized protein YdiE
- Methionine aminopeptidase
Sequence:
MRVLGIETSCDETGIAIYDDEKGLLANQLYSQVKLHADYGGVVPELASRDHVRKTVPLIQAALKESGLTAKDIDAVAYTAGPGLVGALLVGATVGRSLAFAWDVPAIPVHHMEGHLLAPMLEDNPPEFPFVALLVSGGHTQLISVTGIGQYELLGESIDDAAGEAFDKTAKLLGLDYPGGPLLSKMAAQGTAGRFVFPRPMTDRPGLDFSFSGLKTFAANTIRDNGTDDQTRADIARAFEDAVVDTLMIKCKRALDQTGFKRLVMAGGVSANRTLRAKLAEMMKKRRGEVFYARPEFCTDNGAMIAYAGMVRFKAGATADLGVSVRPRWPLAELPAA
Protein: NAD reductase coq12 (EC 1.5.1.36) (Q9UTQ4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:37156397}.
Interaction partners:
- Heat shock protein sti1 homolog
- Transcription factor prr1
- Uncharacterized protein C1711.08
- Protein wos2
- 40 kDa peptidyl-prolyl cis-trans isomerase
- Serine/threonine-protein phosphatase T
- Hsp90 co-chaperone Cdc37
- Glucose-insensitive transcription protein 7
- Heat shock protein homolog pss1
- F-box/TPR repeat protein pof3
Sequence:
MSIRFTHCFTSSSSLPCYILRHLPFSNFNRYSTASHDNVNAFRLLMRRFAQPVVIITSGFADGHRAGMTASSFTPVSLTPNPVISFNIKIPSRTANAIQQSNRVIVHLLSSSIKKHSEWASLLAKQKHQINPLMNSEKNSTSVEDLPGSNRTQQTSSHSLLHPLHPIDVSLSKEGLPCLVDSLGLLHCSIIHSYQVQDHILFVANVERVEHGSSPLESSSGLVYYNRNYCSTSPLSPIIDSFES
Protein: Circadian clock oscillator protein KaiC (EC 2.7.11.1) (EC 3.6.4.-) (Q79V60)
Organism: Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1)
Function: Central component of the KaiABC oscillator complex, which constitutes the main circadian regulator in cyanobacteria. Complex composition changes during the circadian cycle to control KaiC phosphorylation. KaiA stimulates KaiC autophosphorylation, while KaiB sequesters KaiA, leading to KaiC autodephosphorylation. Clock output pathways impact the RpaA transcriptional regulator. KaiC enhances the autophosphorylation activity of SasA, which then transfers its phosphate group to RpaA to activate it. KaiB and KaiC together enhance the phospho-RpaA dephosphatase activity of CikA.
Interaction partners:
- Circadian clock oscillator protein KaiA
- Circadian clock oscillator protein KaiB
- Adaptive-response sensory kinase SasA
- Protein RecA
- Replicative DNA helicase
- CpmA protein
- Circadian oscillation regulator
- Cell division protein FtsZ
- Amidophosphoribosyltransferase
- Thiamine-phosphate synthase
Sequence:
MTNLPEHQSSPTEQSSAEVKKIPTMIEGFDDISHGGLPQGRTTLVSGTSGTGKTLFAVQFLYNGITIFNEPGIFVTFEESPQDIIKNALSFGWNLQSLIDQGKLFILDASPDPDGQEVAGDFDLSALIERIQYAIRKYKATRVSIDSVTAVFQQYDAASVVRREIFRLAFRLKQLGVTTIMTTERVDEYGPVARFGVEEFVSDNVVILRNVLEGERRRRTVEILKLRGTTHMKGEYPFTINNGINIFPLGAMRLTQRSSNVRVSSGVKTLDEMCGGGFFKDSIILATGATGTGKTLLVSKFLETGCQQGERALLFAYEESRAQLSRNASSWGIDFEELERRGLLRIICAYPESAGLEDHLQIIKSEIADFKPSRVAIDSLSALARGVSNNAFRQFVIGVTGFAKQEEITGFFTNTTDQFMGSNSITESHISTITDTILLLQYVEIRGEMSRAINVFKMRGSWHDKGIREYVITEKGAEIRDSFRNFEGIISGTPTRISVDEKTELARIAKGMQDLESE
Protein: Tyrosine-protein kinase receptor (EC 2.7.10.1) (F1QKJ0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MDLFSIPPRVCLWRILFLLSIFQDYMSSMLDCPPTCTCSTTDIFCNKSYQGNFFPLLALQDTVSDGNTTNSLPDLFENISTIHIENWSLQTLKDLDMELYTGLQRLNIVNCNLRTIQSRAFAKNPHLRYINLSRNPLTTLSWQLFQNLQLLELKLEGVVFNCSCNIRWIQLWQQRGEAGLHNQQLFCFNGYSKIPLQLMNISQCDFPEISVSHSNLTVTEGDRVMITCNGSGIPVPEVDWTVGGLHSINTHQANQYPPNVHSINLTLVNVSRDDNGFMLTCIAENIVGMTNASIQLSVQFPPAIINFEEPQKRHDTCMMFTVRANPLPTLHWSFKGEEIKATEYVHPEMEVYQDNLEGCLLFKNPTQHNNGNYTLEARNYLGVAVKTVYAHFLHPPFEDYPDYVSPTPTAIPTMTHRPEEDTFGVSIAVGLAGFACVLLVVMFVLINKYGRRSKFGMKGPVAVISGEEDSASPLHHVNHGIITPCTLDAGPDAVVIGMTRIPVIENPQYFRHGHNCNKPATYVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKTLKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCVDGDPLIMVFEYMKHGDLNKFLRAHGPDAMILVDGQPLQTNGELGLSQMLHIASQIASGMVYLGSQHFVHRDLATRNCLVGNGLLVKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLANNEVIECITQGRVLERPRLCPKEVYDIMLGCWQREPQQRLNIKDIQKILFALGKATPVYLDILG
Protein: Polyamine oxidase FMS1 (EC 1.5.3.17) (Fenpropimorph resistance multicopy suppressor 1) (P50264)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.
Interaction partners:
- Ornithine decarboxylase
- Aldehyde dehydrogenase [NAD
- Fatty aldehyde dehydrogenase HFD1
- Aldehyde dehydrogenase 5, mitochondrial
- Aldehyde dehydrogenase [NAD
- Spermidine synthase SPE3
- Magnesium-activated aldehyde dehydrogenase, cytosolic
- Potassium-activated aldehyde dehydrogenase, mitochondrial
- Spermine synthase SPE4
- CTD kinase subunit gamma
Sequence:
MNTVSPAKKKVIIIGAGIAGLKAASTLHQNGIQDCLVLEARDRVGGRLQTVTGYQGRKYDIGASWHHDTLTNPLFLEEAQLSLNDGRTRFVFDDDNFIYIDEERGRVDHDKELLLEIVDNEMSKFAELEFHQHLGVSDCSFFQLVMKYLLQRRQFLTNDQIRYLPQLCRYLELWHGLDWKLLSAKDTYFGHQGRNAFALNYDSVVQRIAQSFPQNWLKLSCEVKSITREPSKNVTVNCEDGTVYNADYVIITVPQSVLNLSVQPEKNLRGRIEFQPPLKPVIQDAFDKIHFGALGKVIFEFEECCWSNESSKIVTLANSTNEFVEIVRNAENLDELDSMLEREDSQKHTSVTCWSQPLFFVNLSKSTGVASFMMLMQAPLTNHIESIREDKERLFSFFQPVLNKIMKCLDSEDVIDGMRPIENIANANKPVLRNIIVSNWTRDPYSRGAYSACFPGDDPVDMVVAMSNGQDSRIRFAGEHTIMDGAGCAYGAWESGRREATRISDLLK
Protein: ATP synthase F(1) complex catalytic subunit beta, mitochondrial (EC 7.1.2.2) (ATP synthase F1 subunit beta) (P00829)
Organism: Bos taurus (Bovine)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:95168}; Peripheral membrane protein {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:23407638, ECO:0000269|PubMed:2864455, ECO:0000269|PubMed:8065448, ECO:0000269|PubMed:95168}; Matrix side {ECO:0000269|PubMed:14633978, ECO:0000269|PubMed:95168}.
Interaction partners:
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MLGLVGRVVAASASGALRGLSPSAPLPQAQLLLRAAPAALQPARDYAAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS
Protein: Protein-glutamine gamma-glutamyltransferase 6 (EC 2.3.2.13) (Transglutaminase Y) (TGY) (TGase Y) (Transglutaminase-3-like) (TGase-3-like) (Transglutaminase-6) (TG6) (TGase-6) (O95932)
Organism: Homo sapiens (Human)
Function: Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23206699, ECO:0000269|PubMed:25253745, ECO:0000269|PubMed:29053796}.
Interaction partners:
- Ankyrin repeat and SOCS box protein 17
Sequence:
MAGIRVTKVDWQRSRNGAAHHTQEYPCPELVVRRGQSFSLTLELSRALDCEEILIFTMETGPRASEALHTKAVFQTSELERGEGWTAAREAQMEKTLTVSLASPPSAVIGRYLLSIRLSSHRKHSNRRLGEFVLLFNPWCAEDDVFLASEEERQEYVLSDSGIIFRGVEKHIRAQGWNYGQFEEDILNICLSILDRSPGHQNNPATDVSCRHNPIYVTRVISAMVNSNNDRGVVQGQWQGKYGGGTSPLHWRGSVAILQKWLKGRYKPVKYGQCWVFAGVLCTVLRCLGIATRVVSNFNSAHDTDQNLSVDKYVDSFGRTLEDLTEDSMWNFHVWNESWFARQDLGPSYNGWQVLDATPQEESEGVFRCGPASVTAIREGDVHLAHDGPFVFAEVNADYITWLWHEDESRERVYSNTKKIGRCISTKAVGSDSRVDITDLYKYPEGSRKERQVYSKAVNRLFGVEASGRRIWIRRAGGRCLWRDDLLEPATKPSIAGKFKVLEPPMLGHDLRLALCLANLTSRAQRVRVNLSGATILYTRKPVAEILHESHAVRLGPQEEKRIPITISYSKYKEDLTEDKKILLAAMCLVTKGEKLLVEKDITLEDFITIKVLGPAMVGVAVTVEVTVVNPLIERVKDCALMVEGSGLLQEQLSIDVPTLEPQERASVQFDITPSKSGPRQLQVDLVSPHFPDIKGFVIVHVATAK
Protein: Type 2 DNA topoisomerase 6 subunit B-like (TOP6B like initiator of meiotic double strand breaks) (Type 2 DNA topoisomerase VI subunit B-like) (TOPOVIBL) (J3QMY9)
Organism: Mus musculus (Mouse)
Function: Component of a topoisomerase 6 complex specifically required for meiotic recombination. Together with SPO11, mediates DNA cleavage that forms the double-strand breaks (DSB) that initiate meiotic recombination. The complex promotes relaxation of negative and positive supercoiled DNA and DNA decatenation through cleavage and ligation cycles.
Subcellular location: Chromosome {ECO:0000305}. Note=Localizes to meiotic chromosomes. {ECO:0000305}.
Interaction partners:
- Meiotic recombination protein SPO11
- Interactor of HORMAD1 protein 1
- Meiotic recombination protein REC114
- Meiosis inhibitor protein 1
- Ankyrin repeat domain-containing protein 31
Sequence:
MERTALAVCEILRYLIIHWKCEAGTAKGTLLDGQLVISIEALRSKHLPDSLHCIITIASTRSVYGGLNFKKFLQEIQPALPRLSAKLALASEEGGRSQDASGIAPCQVTFEVDENSQSLMTDCLVIKHFLRKIIIVHHKLKFSFSVAVNGTLSAETFGAENEPTLRLDNGVTLVVGFQRYVSKPKLNWSEAHCSRIHPVLGHPAPLFIPDAKADTGLLGELTLTPAAALCPSPKGFSSQLCRISSVSIFLYGPLGLPLLSSDQDQPSTAVFRDTSYFIDWKKYNLFMVPNLDLNLDTQSVLPDVNYKAESPEGNQSQNMNAQGPALLLFLFVDFQSDVPVQQAKIWGLHTLLTAHLSAILSESRSTVQQSIQSAVDQVWQLYHHDAKTQQRLQASLSVAVNSIMSVLTGSTRSSFRKTCLQALEAADTQEFGVKLHRIFYDITQHQFLKHCSCDTEQHLTPEKNISAQNTKDQHKNIAQEFPEESIGQAENKRPKRGSPNHGREESRVLGSARDRSPPKSATRDRELTEVSLTARGSQTQAAHGRAQAAEAASPAGGLEDLWLQEVSNLSEWLNPGHRS
Protein: Zygote arrest protein 1.S (Q7T3U0)
Organism: Xenopus laevis (African clawed frog)
Function: mRNA-binding protein required for maternal mRNA storage, translation and degradation during oocyte maturation. Probably promotes formation of some phase-separated membraneless compartment that stores maternal mRNAs in oocytes: acts by undergoing liquid-liquid phase separation upon binding to maternal mRNAs (By similarity). Binds to the 3'-UTR of maternal mRNAs in immature oocytes, inhibiting their translation.
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:C3VD30}.
Interaction partners:
Sequence:
MYPAYNPYSYRYLNPRNKGMSWRQKNYLASYGDTGDYCDNYQRAQLKAILSQVNPNLTPRLCRANTRDVGVQVNPRQDASVQCSLGPRTLLRRRPGALRKPPPEQGSPASPTKTVRFPRTIAVYSPVAAGRLAPFQDEGVNLEEKGEAVRSEGSEGGRQEGKQGDGEIKEQMKMDKTDEEEAAPAQTRPKFQFLEQKYGYYHCKDCNIRWESAYVWCVQETNKVYFKQFCRTCQKSYNPYRVEDIMCQSCKQTRCACPVKLRHVDPKRPHRQDLCGRCKGKRLSCDSTFSFKYII
Protein: DGATAe protein (Q9BPQ2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MVCKTISPSVNMQLKMEQQTTQQQQQQQQQQQQQQQLQQQQHQALTKQQLQLLDKIKLESSNGADQLAQQTANNLDEQQEQQQQHQQQAATSVGVVVQTGQAGVSEPEEQYVVVPRNQRRILTTAGTLELNEAREGEPSTNASNASSGSASDSHIEYQRSAHQSPGATHYVQMAPRNAEVTEQVGAAAGAPPGTIFAYPIICNGDDVAAIKIETLEKGEATGESQQQQQQLQQHQHQQQQQCPTPNGASYGETIVISSEAEALQHHHQQQQQHQQQQHQQQHHQHQAAAAASAAAQTVHIATSSHGGTVRFVTEDVRFTTAGPETSASNMYYDVPVVDGSVHANESKTYADLGNAYAPFPPSSSFSSNSYAATLQQGNTIYSVPGTGQFLAKSESGLNQTGLLRQTGPATFQTISFEGGNGIEPLWASPAPPEYQSVQFSNFHPQVIDEYGSGNMSTSHWPPASSIGQYDGSLVTASSTSSPNHELKCENCHGPFLRKGSEYFCPNCPAFMRMAPRITQRQAKPKAAAAPNNRRNGVTCANCQTNSTTLWRRNNEGNPVCNACGLYYKLTT
Protein: Type VI secretion system spike protein VgrG1a (T6SS spike protein VgrG1a) (Q9I741)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Part of the H1 type VI secretion system (H1-T6SS) specialized secretion system, which delivers several virulence factors in both prokaryotic and eukaryotic cells during infection. Forms the spike at the tip of the elongating tube formed by haemolysin co-regulated protein 1/Hcp1. Allows the delivery of the Tse6 toxin to target cells where it exerts its toxicity.
Subcellular location: Secreted {ECO:0000269|PubMed:21325275}.
Interaction partners:
- AAA+ ATPase ClpV1
- Protein hcp1
- Type VI secretion system baseplate subunit TssG
- Type VI secretion system accessory component TagJ
- Type VI secretion system component TssE1
- Type VI secretion system component TssF1
- non-specific serine/threonine protein kinase
- OmpA-like domain-containing protein
- PppA
- Type VI secretion system component TssM1
Sequence:
MQLTRLVQVDCPLGPDVLLLQRMEGREELGRLFAYELHLVSENPNLPLEQLLGKPMSLSLELPGGSRRFFHGIVARCSQVAGHGQFAGYQATLRPWPWLLTRTSDCRIFQNQSVPEIIKQVFRNLGFSDFEDALTRPYREWEYCVQYRETSFDFISRLMEQEGIYYWFRHEQKRHILVLSDAYGAHRSPGGYASVPYYPPTLGHRERDHFFDWQMAREVQPGSLTLNDYDFQRPGARLEVRSNIARPHAAADYPLYDYPGEYVQSQDGEQYARNRIEAIQAQHERVRLRGVVRGIGAGHLFRLSGYPRDDQNREYLVVGAEYRVVQELYETGSGGAGSQFESELDCIDASQSFRLLPQTPVPVVRGPQTAVVVGPKGEEIWTDQYGRVKVHFHWDRHDQSNENSSCWIRVSQAWAGKNWGSMQIPRIGQEVIVSFLEGDPDRPIITGRVYNAEQTVPYELPANATQSGMKSRSSKGGTPANFNEIRMEDKKGAEQLYIHAERNQDNLVENDASLSVGHDRNKSIGHDELARIGNNRTRAVKLNDTLLVGGAKSDSVTGTYLIEAGAQIRLVCGKSVVEFNADGTINISGSAFNLYASGNGNIDTGGRLDLNSGGASEVDAKGKGVQGTIDGQVQAMFPPPAKG
Protein: Respiratory supercomplex factor 1, mitochondrial (Altered inheritance of mitochondria protein 31) (Q03713)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Assembly factor that plays a role in the assembly of the respiratory chain supercomplexes (SCs) composed of ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV). Involved in the recruitment of COX13 and RCF2 into cytochrome c oxidase. May also be required for late-stage assembly of the COX12 and COX13 subunits. Required for the generation and maintenance of a normal proton motive force (PMF) across the inner mitochondrial membrane (IMM) by preventing proton leakage through an inactive population of CIV that accumulates when RCF1 and/or RCF2 proteins are absent.
Subcellular location: Mitochondrion membrane {ECO:0000255|PROSITE-ProRule:PRU00836, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00836, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome b
- Respiratory supercomplex factor 2, mitochondrial
- Uncharacterized protein YBR255C-A
Sequence:
MSRMPSSFDVTERDLDDMTFGERIIYHCKKQPLVPIGCLLTTGAVILAAQNVRLGNKWKAQYYFRWRVGLQAATLVALVAGSFIYGTSGKELKAKEEQLKEKAKMREKLWIQELERREEETEARRKRAELARMKTLENEEEIKNLEKELSDLENKLGKK
Protein: Spermine synthase SPE4 (SPMSY) (EC 2.5.1.22) (Spermidine aminopropyltransferase) (Q12455)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- S-adenosylmethionine decarboxylase proenzyme
- Spermidine synthase SPE3
- Ornithine decarboxylase
- S-methyl-5'-thioadenosine phosphorylase
- Polyamine oxidase FMS1
- Arginase
- Saccharopine dehydrogenase [NADP
Sequence:
MVNNSQHPYIKDGWFREINDKSFPGQAFTMTVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTEFDEFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSNGAFDDERLDLKLCDGFKFLQDIGASDVHKKFDVIITDSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQSSENFWLNLKYLHDLKNTAKKVFPNTEYCYTMVPTYTSGQLGLIVCSNNANIPLNIPQRKISEQEQGKLKYYNPQIHSSAFVLPTWADKVINE
Protein: A disintegrin and metalloproteinase with thrombospondin motifs 18 (ADAM-TS 18) (ADAM-TS18) (ADAMTS-18) (EC 3.4.24.-) (Q4VC17)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
Sequence:
MECALLCLCALRAAGPGPPWGPAGLGRLAKALQLCCFCCASVAVALASDSGSSGGSGLNDDYVFVVPVEVDSGGSYISHDILHHRKRRSAHGASNSLHYRVSAFGQDLHLELKPSAILSSHFRVQVLGKDGASETREPEVPQCLYQGFIRNDSSSSVAVSTCAGLSGLIRTRDNEFLISPLPQLLAQEHNYSSPAGHHPHVLYKRTAEKRVRWYQDYPGSQRTYPGHSPSHTPPASQSQEPEYSHRRWQKRHFCGRRKKYAPKPPAEDAYLRFDEYGGTGRPRRSAGKSQNGLNVETLVVADAKMVEKHGKDDVTTYILTVMNMVSSLFKDGTIGSDINIVVVSLILLEEEPEGLLINHHADQSLNSFCQWQSALVGKNGKRHDHAILLTGFDICSWKNEPCDTLGFAPISGMCSKYRSCTINEDTGLGLAFTIAHESGHNFGMVHDGEGNPCRKAEGNIMSPTLTGNNGVFSWSSCSRQYLKKFLSTPQAGCLVDEPKQTGQYKYPDKLPGQIYDADMQCKWQFGAKAKLCSLGVMKDICKSLWCHRVGHRCETKFMPAAEGTACGLSMWCRQGQCVKLGELGPRPIHGQWSAWSKWSECSRTCGGGVKFQERHCSNPKPQYGGKYCPGSSRIYKLCNINPCPENSLDFRAQQCAEYNNKPFRGWLYRWKPYTKVEEEDRCKLYCKAENFEFFFAMSGKVKDGTPCSPHRNDVCIDGICELVGCDHELGSKAVSDACGVCKGDNSTCKFYKGLYLSQHKANEYYPVVTIPAGARSIEIQELQLSSSYLAVRSLSQKYYLTGGWSIDWPGDFTFAGTTFEYQRSFNRPERLYAPGPTNETLVFEILTQGKNPGIAWKYALPKVMNVTQPATKRYHHTWRTVQSDCSVTCGGGYISIKAICLRDQHTQVNSSFCSVRTKPATEPKICNAFSCPAYWLPGEWSACSKSCAGGQQSRKIRCVQKKPFQKEEAVLHSLCPVSTPTQVQVCNSHACPPEWSPSPWSQCSKTCGRGVRRREVLCKSPAAETLPESLCSSSPRPEAQEGCVLGRCPKNNRLQWIASAWSECSATCGLGVRKRELKCVEKTLQGKLITFPERRCRNIKKPSLELEEACNQRTCPVYSMAVASWYSSPWQQCTVTCGGGVQTRSVHCMQQGRPSSSCLLHQKPPVLRACNTNFCPAPEKKDDPSCVDFFSWCHLVPQHGVCNHKFYGKQCCRSCTRKS
Protein: Coiled-coil domain-containing 57 (Coiled-coil domain-containing protein 57 isoform X1) (E7EY31)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLEAVDLESQLACKEREWKELQGLRIRQLDTALNEATSELYDQRERFLRLRDDFKYNLRVLEERDKELERYDAMAARAQMEESARREEVSELRIEIAKLQNALEEQRRAKEDIEVQFQKRGVEHRVKVEKVQSKMESEIQKLREENESLRRDLQRRIRESDGELALQKQEMMADFDSEMRKREHEFHLKLDEMNNLVLSCQLKEKLLSKELEVHAKAHSQATEALQASEELYQQAQKEIQHRDWDLKNTTAMKDSRIKELEETLKQLENNCKKEQEAYDRKHAELERRTRESKDALDRLREAHARDLQEEREKSSELQAQLDRMILELERREKTRTDDLEHRDQQIQELRAQLETTRSGWDTYIMQVSKEKVARDTELFSAGEREAKVRAELERCKEDIERYKQQVSSGLQREQALEQKRVQLELDWERRCEDVRSEHYLRSEEIIQNLTQARDQVTAELREKERELQETMTVLQSVTVERDQALCGNKPALTGFQTSVIDGSSFPSEEIRRLQQQNNTLKAVVAEMRKEMEILSKQRLAAPRPATNLEPSTAGSTDYTKALEKEILELKAKCRNLEERLEESSKTVNTSINPTPAFPVSPDNAYLQNHIRSLNETIGGLRVEKVANAAALKKQEVRLAHLESTVEQLTQQCHSKHMENESLCLELANHKRAATAEEARLKQRVAAAELELNEVRREAEEHQKGSLLHNLETVALGNQVSALKVDLASRREPIVLNQSEMVKQLQEENLSLRKQLLLLHSSSRGSSIGDVPLLQSKLKQAARMISGLSQDKQQLIEMGNRLRAQLIEAGLDVPRHSKIILQPNTPEPNLAEKDPSQPEHGIQSKSRLSTLEQLQYQLTTQELQYAQRDQNKKTAIIVRPQLSESESSDKHRTTNPWEPSVRVQSVSSKENTPPQQNKPEALVRHHILSSISTDESLQKVWQMLDQGLSSSVFSPSDSEDKGRVSTADRVPDITQPPAPLVSVEGKTASLREKKKQSRTASVPAKKAIPPGKHAKIRNYNIKD
Protein: Homeobox protein engrailed-like (D3Z8B1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Paired box 2
Sequence:
MEEKDSKSSETAAEAQRQPEPSPGGGSGGGSSPSDSDTGRRRALMLPAVLQAPGNHQHPHRITNFFIDNILRPEFGRRKDAGTCCAGAGGARGGEGGAGSTEGGGGADGAEQILGARESRPNPACAPSAGGPLSGASGDPAADGEGGSKTLSLHGGAKKPGDPGGSLDGALKARGLGGGDLSVSSDSDSSQASATLGAQPMLWPAWVYCTRYSDRPSSGPRSRKPKKKNPNKEDKRPRTAFTAEQLQRLKAEFQTNRYLTEQRRQSLAQELSLNESQIKIWFQNKRAKIKKATGNKNTLAVHLMAQGLYNHSTTAKEGKSDSE
Protein: Mitochondrial import inner membrane translocase subunit Tim17-B (Q9Z0V7)
Organism: Mus musculus (Mouse)
Function: Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular location: Mitochondrion inner membrane; Multi-pass membrane protein.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim23
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import inner membrane translocase subunit Tim21
- Mitochondrial import inner membrane translocase subunit TIM16
- Mitochondrial import inner membrane translocase subunit TIM44
- Reactive oxygen species modulator 1
- Mitochondrial import inner membrane translocase subunit TIM14
- Stress-70 protein, mitochondrial
- Mitochondrial import inner membrane translocase subunit Tim17-A
- DnaJ homolog subfamily C member 15
Sequence:
MEEYAREPCPWRIVDDCGGAFTMGVIGGGVFQAIKGFRNAPVGIRHRFRGSVNAVRIRAPQIGGSFAVWGGLFSTIDCGLVRLRGKEDPWNSISSGALTGAVLAARSGPLAMVGSAMMGGILLALIEGVGILLTRYTAQQFRNAPPFLEDPSQLTPKEGSPAPGYPNYQQYH
Protein: Maltoporin (Maltose outer membrane channel) (Maltose-inducible porin) (Phage lambda receptor protein) (P02943)
Organism: Escherichia coli (strain K12)
Function: Involved in the transport of maltose and maltodextrins. Indispensable for translocation of maltodextrins (alpha 1-4 linked polyglucosyls) containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda. Binds maltosaccharides; when LamB binds starch in soft agar, it inhibits motility.
Subcellular location: Cell outer membrane {ECO:0000255|HAMAP-Rule:MF_01301, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:1988451, ECO:0000269|PubMed:4201774, ECO:0000269|Ref.9}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01301, ECO:0000269|PubMed:16079137}.
Interaction partners:
- Maltose/maltodextrin-binding periplasmic protein
- Maltose operon periplasmic protein
- Maltose/maltodextrin import ATP-binding protein MalK
- Maltose/maltodextrin transport system permease protein MalF
- Maltose/maltodextrin transport system permease protein MalG
- Outer membrane porin C
- Outer membrane porin F
- Protein translocase subunit SecA
- Nucleoside-specific channel-forming protein Tsx
- Outer membrane porin PhoE
Sequence:
MMITLRKLPLAVAVAAGVMSAQAMAVDFHGYARSGIGWTGSGGEQQCFQTTGAQSKYRLGNECETYAELKLGQEVWKEGDKSFYFDTNVAYSVAQQNDWEATDPAFREANVQGKNLIEWLPGSTIWAGKRFYQRHDVHMIDFYYWDISGPGAGLENIDVGFGKLSLAATRSSEAGGSSSFASNNIYDYTNETANDVFDVRLAQMEINPGGTLELGVDYGRANLRDNYRLVDGASKDGWLFTAEHTQSVLKGFNKFVVQYATDSMTSQGKGLSQGSGVAFDNEKFAYNINNNGHMLRILDHGAISMGDNWDMMYVGMYQDINWDNDNGTKWWTVGIRPMYKWTPIMSTVMEIGYDNVESQRTGDKNNQYKITLAQQWQAGDSIWSRPAIRVFATYAKWDEKWGYDYTGNADNNANFGKAVPADFNGGSFGRGDSDEWTFGAQMEIWW