wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphoenolpyruvate carboxykinase, cytosolic [GTP] (EC 4.1.1.32) (Serine-protein kinase PCK1) (Q7T3G9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPPQLQSQDRSCPRVLQGDLASLSASVREFIDSSVSLCQPDALHICDGSEQENSTILSLLEEQGAIKRLRKYSNCWLARTDPRDVARVESKTVIVTAEQRDTVPTPTGGGVSQLGRWMCPEEWDKAMNLRFPGCMKGRVMYVIPFSMGPVGSPLSKIGVELTDSPYVVASMRIMTRMGKTVLSALGNGEFVRCLHSVGCPLPLKKPLVNNWPCNPELTLVAHIPDQRKIVSFGSGYGGNSLLGKKCFALRIASRIAKEEGWLAEHMLILGITNPAGQKKYFAAAFPSACGKTNLAMLKPSLPGWKVECVGDDIAWMKFDKEGNLRAINPENGFFGVAPGTSSKTNPNAMSTISCNTLFTNVAESSDGGVFWEGMDEDLPEGVTLTSWKNQPWTPEDGEPCAHPNSRFCTPAAQCPIIDPQWESPEGVPIEAIIFGGRRPQGVPLVYEAFDWAHGVFVGASMRSEATAAAEHKGKVIMHDPFAMRPFFGYNFGQYLSHWLSMEQRPGAKLPKIFHVNWFGRSSSGRFLWPGFGENIRVLEWMFGRLSGGAEARTTAVGLVPADGALNLHGLPDVEPLELFRVSQEFWMQELQEIREYFSRELNRDLPQEMQRQLELLEHRLTHTHVSSKHG
Protein: CD74 molecule, major histocompatibility complex, class II invariant chain b (Iclp2 protein) (Invariant chain-like protein 2) (Q9PVD9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSSEGNETPLISDQSSVNMGPQPRNKNQALKVAGVTLLAGILIAGQAFTAYMAYSHKEQLNTLERRGDRLHEISRKSAMRAPLKMHLPMSSLALKYEDDTKENKDSPPSSPKPEPKVLTQCQKEAAGEVKSLLPSFKPRCNENGDYLSQQCWEQTDFCWCVDKNGVEIPDTLKEGPAQCWALNSADIVNEPLLRKNGE
Protein: T. brucei spp.-specific protein (Q389N8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKERRSVSQSRTSRTGQLRNGGFRESRFRVALMSRCARPSSSGTSHMFAPSSLPSVGQPSYESGVSSMPNISFPTCNDGALSPGDSMYPPSLPQRAKNKRTGQKDKQKRQSTLGSVDSEEEKRSFLASAAAFRRHRRYNNPFTAYCLASDPYDRPREIERQRQFMSCYKRIACRFVAGGKNALDKPTRYMLGDCVARLYKAVAADWPEADPMVVSSAEDLIVVFMNLDAVRNPVTALRYMNALLKRCDVVRAFDLKKVPEGWDVVTEDGHLMYTFRPPWVGERRFLPDQVAVKKSRGR
Protein: Putative ribosome biogenesis protein C306.07c (U3 snoRNP-associated protein C306.07c) (Q9Y7R7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in rRNA-processing and ribosome biosynthesis.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized RNA-binding protein C1827.05c
- Ribosome biogenesis protein erb1
- Ribosome biogenesis protein ytm1
- U3 small nucleolar RNA-associated protein 6
- Ribosome production factor 2 homolog
- ATP-dependent RNA helicase has1
- Pescadillo homolog
- U3 small nucleolar RNA-associated protein 4
- U3 small nucleolar ribonucleoprotein protein imp4
- Periodic tryptophan protein 2 homolog
Sequence:
MAITSEKKKNLKSLDKIDIKLLEKTIRALLQHIRSSDKPIEKEKVYIQVNTFQPVEKESLRRPSKVFLPHRIMHVTDACLIVKDSQQTYQDLVEQQGLDEVITKVLSIPRLKLKYKTIREKCELRDSHNLFLVDDRVLKYIPLLMGKVFEQKKIKPFPISVLQKKETLRNQVARCLHSTYLKLSAGTSHTILCGLATQTNEQLLENITTVLKCLLTNFIPKGWSAIDNVAIKTADSASLPIWTSDTNLAAHKRHIVHIQDARPLKKSELRAQKRGSSGEGKGNK
Protein: Asc-type amino acid transporter 1 (Asc-1) (Solute carrier family 7 member 10) (Q9NS82)
Organism: Homo sapiens (Human)
Function: Associates with SLC3A2/4F2hc to form a functional heterodimeric complex that translocates small neutral L- and D-amino acids across the plasma membrane. Preferentially mediates exchange transport, but can also operate via facilitated diffusion (By similarity). Acts as a major transporter for glycine, L- and D-serine in the central nervous system. At the spinal cord and brainstem regulates glycine metabolism and glycinergic inhibitory neurotransmission by providing for glycine de novo synthesis from L-serine and glycine recycling from astrocytes to glycinergic motor neurons (By similarity). At Schaffer collateral-CA1 synapses mediates D-serine and glycine release that modulates post-synaptic activation of NMDA receptors and excitatory glutamatergic transmission (By similarity). May regulate D-serine release from mesenchymal progenitors located in developing subcutaneous adipose tissue, favoring white adipocyte over thermogenic beige adipocyte lineage commitment (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P63115}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with OLIG2 in astrocytic processes. Localizes to the plasma membrane in mature adipocytes and to intracellular structures in preadipocytes. {ECO:0000250|UniProtKB:P63115}.
Interaction partners:
- Amino acid transporter heavy chain SLC3A2
- Amino acid transporter heavy chain SLC3A1
Sequence:
MAGHTQQPSGRGNPRPAPSPSPVPGTVPGASERVALKKEIGLLSACTIIIGNIIGSGIFISPKGVLEHSGSVGLALFVWVLGGGVTALGSLCYAELGVAIPKSGGDYAYVTEIFGGLAGFLLLWSAVLIMYPTSLAVISMTFSNYVLQPVFPNCIPPTTASRVLSMACLMLLTWVNSSSVRWATRIQDMFTGGKLLALSLIIGVGLLQIFQGHFEELRPSNAFAFWMTPSVGHLALAFLQGSFAFSGWNFLNYVTEEMVDARKNLPRAIFISIPLVTFVYTFTNIAYFTAMSPQELLSSNAVAVTFGEKLLGYFSWVMPVSVALSTFGGINGYLFTYSRLCFSGAREGHLPSLLAMIHVRHCTPIPALLVCCGATAVIMLVGDTYTLINYVSFINYLCYGVTILGLLLLRWRRPALHRPIKVNLLIPVAYLVFWAFLLVFSFISEPMVCGVGVIIILTGVPIFFLGVFWRSKPKCVHRLTESMTHWGQELCFVVYPQDAPEEEENGPCPPSLLPATDKPSKPQ
Protein: NCK adaptor protein 1 (C9J869)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVERKNSARKASIVKNLKDTLGIGKVKRKPSVPDSASPADDSFVDPGERLYDLNMPAYVKFNYMAEREDELSLIKGTKVWNHHLHSVITLGLHSLESLLAILGIMAKS
Protein: Tail assembly protein GT (Gene product 15) (gp15) (Gene product GT) (gpGT) (Minor tail protein GT) (P03735)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Promotes tail assembly by creating a scaffold for the tail tube proteins. Tail assembly proteins G and GT probably wrap the linear tape measure protein to create a tail assembly scaffold. This allows the polymerization of the tail tube protein, during which G and GT are released, therefore they are absent in the mature virion. The tail assembly protein GT is produced by a rare -1 ribosomal frameshift. The ratio of translated G/GT is about 20, and this ratio is important for proper tail assembly.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04134}.
Interaction partners:
Sequence:
MFLKTESFEHNGVTVTLSELSALQRIEHLALMKRQAEQAESDSNRKFTVEDAIRTGAFLVAMSLWHNHPQKTQMPSMNEAVKQIEQEVLTTWPTEAISHAENVVYRLSGMYEFVVNNAPEQTEDAGPAEPVSAGKVFDGELSFALKLAREMGRPDWRAMLAGMSSTEYADWHRFYSTHYFHDVLLDMHFSGLTYTVLSLFFSDPDMHPLDFSLLNRREADEEPEDDVLMQKAAGLAGGVRFGPDGNEVIPASPDVADMTEDDVMLMTVSEGIAGGVRYG
Protein: Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1 (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase 1) (HACD1) (Cementum-attachment protein) (CAP) (Protein-tyrosine phosphatase-like member A) (B0YJ81)
Organism: Homo sapiens (Human)
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular location: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18554506}; Multi-pass membrane protein {ECO:0000269|PubMed:18554506}.
Interaction partners:
- Very-long-chain enoyl-CoA reductase
- Very-long-chain 3-oxoacyl-CoA reductase
- Very long chain fatty acid elongase 6
- Very long chain fatty acid elongase 4
- Very long chain fatty acid elongase 2
- Very-long-chain
- Acyl-CoA
- Very-long-chain
- Stearoyl-CoA desaturase
- Stearoyl-CoA desaturase 5
Sequence:
MGRLTEAAAAGSGSRAAGWAGSPPTLLPLSPTSPRCAATMASSDEDGTNGGASEAGEDREAPGERRRLGVLATAWLTFYDIAMTAGWLVLAIAMVRFYMEKGTHRGLYKSIQKTLKFFQTFALLEIVHCLIGIVPTSVIVTGVQVSSRIFMVWLITHSIKPIQNEESVVLFLVAWTVTEITRYSFYTFSLLDHLPYFIKWARYNFFIILYPVGVAGELLTIYAALPHVKKTGMFSIRLPNKYNVSFDYYYFLLITMASYIPLFPQLYFHMLRQRRKVLHGEVIVEKDD
Protein: Possible sensor-transducer protein BlaR (P95164)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Transcriptional regulator BlaI
- 6-phosphogluconate dehydrogenase, decarboxylating
- GMP reductase
- UPF0053 protein Rv1842c
- Uncharacterized protein Rv1841c
Sequence:
MSALAFTILAVLLAGPTPALLARATWPLRAPRAAMVLWQAIALAAVLSSFSAGIAIASRLLMPGPDGRPTTSFVGAAGRLGWPLWAAYITVFALTVLVGARLAVAVVRVATATRRRRAHHRMVVDLVGVGHNGALAQPCARARDLRVLDVAQPLAYCLPGVRSRVVVSEGTLTALADAEVAAILTHERAHLRARHDLVLEAFTAVHAAFPRLVRSANALGAVQLLVELLADDAAVRAAGRTPLARALVACASGRAPSGALAVGGPSTVLRVRRLSGRGNSAVLSAAAYLAAAAVLVVPTVALAVPWLTQLQRLFIA
Protein: NADH-ubiquinone oxidoreductase, mitochondrial, putative (EC 1.6.5.3) (Q582M4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Acyl carrier protein
- Electron transfer protein, putative
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase 20 kDa subunit, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Reiske iron-sulfur protein, mitochondrial
- Uncharacterized protein
- 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein
- Mitochondrial carrier protein, putative
- Mitochondrial processing peptidase alpha subunit, putative
Sequence:
MWRRAGANLPPIIPALTGCVVPFPVCSPRRVIHGEVRHHNTDTNNTRIPWDFTMASYEEINNVILPKFPRSRRRSAIIPLLHLAQRQQGGYIPVTAMYKIARICEVPPMQVFETVTFYSMFNRQPVGKYHIQFCVTTPCMLCGCDELVHRTEAYLNVKMHGTTRDGLITLGEMQCLGACVNAPMLVVSDYSRPPHFSYDFVEDLTWDSVKELIENLREGRPFKVGTCREDRRWSEPAGGRTSIFMKEPPKPYCRDLDAKPVQPGASTGGAAKK
Protein: Signal peptide peptidase-like 2B (SPP-like 2B) (SPPL2b) (EC 3.4.23.-) (Intramembrane protease 4) (IMP-4) (Presenilin homologous protein 4) (PSH4) (Presenilin-like protein 1) (Q8TCT7)
Organism: Homo sapiens (Human)
Function: Intramembrane-cleaving aspartic protease (I-CLiP) that cleaves type II membrane signal peptides in the hydrophobic plane of the membrane. Functions in ITM2B and TNF processing. Catalyzes the intramembrane cleavage of the anchored fragment of shed TNF-alpha (TNF), which promotes the release of the intracellular domain (ICD) for signaling to the nucleus. May play a role in the regulation of innate and adaptive immunity. Catalyzes the intramembrane cleavage of the simian foamy virus processed leader peptide gp18 of the envelope glycoprotein gp130 dependently of prior ectodomain shedding by furin or furin-like proprotein convertase (PC)-mediated cleavage proteolysis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16829952}; Multi-pass membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:17965014}; Multi-pass membrane protein {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:15998642}; Multi-pass membrane protein {ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:15998642}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000269|PubMed:15385547}; Multi-pass membrane protein {ECO:0000305}; Lumenal side {ECO:0000269|PubMed:15385547}. Note=targeted through the entire secretory pathway to endosomes/lysosomes (PubMed:15998642). {ECO:0000269|PubMed:15998642}.
Interaction partners:
- Tumor necrosis factor
Sequence:
MAAAVAAALARLLAAFLLLAAQVACEYGMVHVVSQAGGPEGKDYCILYNPQWAHLPHDLSKASFLQLRNWTASLLCSAADLPARGFSNQIPLVARGNCTFYEKVRLAQGSGARGLLIVSRERLVPPGGNKTQYDEIGIPVALLSYKDMLDIFTRFGRTVRAALYAPKEPVLDYNMVIIFIMAVGTVAIGGYWAGSRDVKKRYMKHKRDDGPEKQEDEAVDVTPVMTCVFVVMCCSMLVLLYYFYDLLVYVVIGIFCLASATGLYSCLAPCVRRLPFGKCRIPNNSLPYFHKRPQARMLLLALFCVAVSVVWGVFRNEDQWAWVLQDALGIAFCLYMLKTIRLPTFKACTLLLLVLFLYDIFFVFITPFLTKSGSSIMVEVATGPSDSATREKLPMVLKVPRLNSSPLALCDRPFSLLGFGDILVPGLLVAYCHRFDIQVQSSRVYFVACTIAYGVGLLVTFVALALMQRGQPALLYLVPCTLVTSCAVALWRRELGVFWTGSGFAKVLPPSPWAPAPADGPQPPKDSATPLSPQPPSEEPATSPWPAEQSPKSRTSEEMGAGAPMREPGSPAESEGRDQAQPSPVTQPGASA
Protein: DNA repair protein RAD51 homolog (O61127)
Organism: Leishmania major
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU364139}.
Interaction partners:
- BRCA2 OB1 domain-containing protein
- RecA-like N-terminal domain-containing protein
- Crossover junction endonuclease MUS81
- Replication protein A subunit
- Uncharacterized protein
- Uncharacterized protein
- DNA 3'-5' helicase
- DNA 3'-5' helicase
- DNA 3'-5' helicase
- MutS homologue
Sequence:
MQTRSKAKGRRGRPSARPSEEVEVVESQPQEVLQNEEQEPQQQQQQQSTDMAEPNASGFRVIQILENYGVASSDIKKLMECGFYTVESAAYAPKKAILAVKGISENKAEKIMAECAKLVPMGFTSAVAYHEARKEIIMVTTGSREVDKLLGGGIETGSITELFGEFRTGKTQLCHTLCVTCQLPISQGGAEGMALYIDTEGTFRPERLVAVAERYKLDPEDVLANVACARAFNTDHQQQLLLQASAMMAENRFALIIVDSATALYRTDYSGRNELAARQMHLGKFLRSLHNLAEEYGVAVVVTNQVVANVDGSAQMFQADSKKPIGGHIMAHASTTRLSLRKGRGEQRIIKVYDSPCLAEAEAIFGIYDDGVGDARD
Protein: Toxin ParE (Gyrase inhibitor ParE) (Q79EC5)
Organism: Escherichia coli
Function: Toxin component of a type II toxin-antitoxin (TA) system involved in plasmid partition. Acts by inhibiting DNA gyrase, converting supercoiled plasmid DNA into a singly cleaved linear form in an ATP-dependent fashion. To do so it probably interacts with one of the gyrase subunits. Gyrase inhibition is prevented by antitoxin ParD, and is reversed in vitro by incubation with ParD. In cells that have lost the plasmid filamentation and growth inhibition occur; this is suppressed when ParD is supplied in trans. The parDE operon alone is capable of stabilizing an RK2-derived minireplicon under defined growth conditions in several different Gram-negative bacteria. It does so by the post-segregational killing (PSK) of plasmid-free cells, also referred to as a plasmid addiction system.
Interaction partners:
Sequence:
MTAYILTAEAEADLRGIIRYTRREWGAAQVRRYIAKLEQGIARLAAGEGPFKDMSELFPALRMARCEHHYVFCLPRAGEPALVVAILHERMDLMTRLADRLKG
Protein: Rho GTPase-activating protein REN1 (Protein ROP1 ENHANCER 1) (Rho-type GTPase-activating protein REN1) (F4JQZ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state. Maintains the global inactivation of ARAC11/ROP1 at the apex in pollen tubes in order to regulate the polar cell growth.
Subcellular location: Cell membrane {ECO:0000305|PubMed:19108776}; Peripheral membrane protein {ECO:0000305|PubMed:19108776}. Note=Localizes to the apical plasma membrane and accumulates in the clear zone of growing pollen tubes.
Interaction partners:
- Rho GTPase-activating protein 1
- Protein JINGUBANG
- Rac-like GTP-binding protein ARAC11
- Ras-related protein RABA4d
- CRIB domain-containing protein RIC3
- CRIB domain-containing protein RIC4
- Ras-related protein RABA1b
- Tlg2p-like protein a
Sequence:
MANKNAESSSQPPPHVQPNQQQQQQPPIANEQEQEPHGDTCSIPPAQSGNTDSRSRGGNTVFKSGPLSISSKGIGWTSWKKRWFILTRTSLVFFRSDPSAVQQKGSEVNLTLGGIDLNNSGSVVVKADKKLLTVLFPDGRDGRAFTLKADTMEDLHEWKAALENALTQAPSASHVMGQNGIFRNDHADPAVGVDEKKDETPTKSTVLGRPVLLALEDVDGAPSFLEKALRFVENHGVRIEGILRQAADVDDVEHRIREYEKGKNEFSPEEDAHIIADCLKYFLRELPSSPVPASCCNALLEACRTDRGNRVNAMRAAICESFPEPNRRLLQRILMMMQTVASNKTVNRMNTNAVAACMAPLLLRPLLAGDCEIENDFDVGGDGSMQLLQAAAAANHAQAIVITLLEEYESIFGEGSLSPGLYSDSEESGSGTEEGSDDEEYDDDDDGSQGSEDYTDEEEDLENESNGSYSESAASEDKYADSIDPDDHKINDNLSTESKSPKRSKEPKKLLSGSRRSSLPRHDDGKKDEDIVVKGVNNTEVKAVVEVSTSEDKNSSTSDVASDTQKPSKLSDAPGGSKRHWGRTPGKKNLSMESIDFSVEVDEDNADIERLESTKLELQSRITEEVKSNAVLQASLERRKKALYGRRQALEQDVGRLQEQLQQERDRKLALETGLNMSKGNQPIPETIDENLKKDLQEVAQAEADIAKLEHKVDDLENRLGHHDGKASGSTHSASKESRKLPEHNAKMKEKQKDTEAASTHISERSTSKDGQGAARENETEKQQDSRSKSSQQETSRGSSKLVGLSKRSGTKGEGSTTTTSALSKLTMRLNFLKERRSQIANELQNMDKGKTLGQPSPTSGQNRVSEETEKGSGSNQDPDSSKLQSPHILDRGRSENGGDRGRGSSGGNHPNTTPRTFSR
Protein: Claudin-14 (O95500)
Organism: Homo sapiens (Human)
Function: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity.
Subcellular location: Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Tight junction protein 1
- Occludin
- Claudin-6
- Claudin-9
- Claudin-1
- Claudin-16
- Claudin-3
- Tight junction protein ZO-3
- Claudin-12
- Tight junction protein 2
Sequence:
MASTAVQLLGFLLSFLGMVGTLITTILPHWRRTAHVGTNILTAVSYLKGLWMECVWHSTGIYQCQIYRSLLALPQDLQAARALMVISCLLSGIACACAVIGMKCTRCAKGTPAKTTFAILGGTLFILAGLLCMVAVSWTTNDVVQNFYNPLLPSGMKFEIGQALYLGFISSSLSLIGGTLLCLSCQDEAPYRPYQAPPRATTTTANTAPAYQPPAAYKDNRAPSVTSATHSGYRLNDYV
Protein: ADP-ribosylation factor-like protein 6 (A0A0J9YXT0)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, cilium membrane {ECO:0000256|ARBA:ARBA00004522}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004522}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004522}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
ILPTIGFSIEKFKSSSLSFTVFDMSGQGRYRNLWEHYYKEGQAIIFVIDSSDRLRMVVAKEELDTLLNHPDIKHRRIPILFFANKMDLRDAVTSVKVSQLLCLENIKDKPWHICASDAIKGEGLQEGVDWLQEKTIQSDPDCEDMKR
Protein: PH domain-containing protein (Q23419)
Organism: Caenorhabditis elegans
Interaction partners:
- Ras-related protein Rab-7a
- small monomeric GTPase
- Vacuolar fusion protein MON1 homolog
- Ras-related protein Rab-10
- Vacuolar fusion protein CCZ1 homolog
- Rab5 GDP/GTP exchange factor
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Receptor-mediated endocytosis protein 6
- Ras-related protein Rab-14
- Ras-related protein ced-10
Sequence:
MSAAPGTISPPARELKTSAICGYLHRIEVRSIGLITRRRYWFALCDSTPYLYWYKDSDDIKCIGRVSLSGAAFTYDPREKGRFEIHSNNEVIALECSSDKQRNEWMKALQSTRKRSWKATKSKSDSSLDISSLTGRNSSSVLEECSSPSPVPPPRSPKPKKRTQFLTEEETDAETSSDVPHSSEETAEVVEDTDNTKIPAEGSATEWYLNPNGQLNERSLQMPKTIESPETVLKRLADQSIEAPFRAIRRNLSTWSRSRQNTSDEPVVGSRKGTVSSVDLTPEEKVIELSDKVSSLEEVVDSLRAALLLAQRNNEALQKIEDMGDNKEEMREYILEKERQVTELHISNSMNARRVRDLEDQNVRLEDTINDLQQSVEAFRESLRTKEELILRMCEEENREDLLGSISERSSNIPADANGLVSDVEVPEGILVDVSSVDCEEATRKVLDEENVRDIGELQDLVEGYRTQNQFLNAEIVQLHAITQSLEDREKKLIRQNFDLEACYYQLKSRYLMVLNHFKSPTKPGKIMEPGVLKELLEESARTPRESQQNLTDQLGFYKKDDFSESDDLLDTATFYMKKAGDVVEATKLEQSEEYMKWLQSWDAFLVNNTVSRQTAIMSSPDLKTLIRTGVPPAYRGRVWKIIVTHWVKDKQAELGNGYYQSMLRKAGTKKQDGSYDAAIKQIDLDLARTLPTNKLFDEPDSANIEKLRNVLYAFRYHNSHVGYCQGLNRLAAIALLNLDEQDSFWFLVACVEHLQPEGYYTSSLIGAVADQKVLRDLVAEKLPKLAAHLRALEVDLSLFALSWFLTCFVDVLPHSIYLTIFDAFLYEGNKVLFRFALALFKICEPHVLQCKTIGTVHQCLSKAQEHIIDFKSLAQVAFNELNPFPQKTIETKRQLYLTQLKDTGHCM
Protein: UPF0098 protein Rv1910c (P9WFN5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- Possible oxidoreductase FadB5
- DUF4262 domain-containing protein
- Probable conserved membrane protein
- Large ribosomal subunit protein uL16
- D-amino-acid oxidase
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL36
Sequence:
MESTVAHAFHRFALAILGLALPVALVAYGGNGDSRKAAPLAPKAAALGRSMPETPTGDVLTISSPAFADGAPIPEQYTCKGANIAPPLTWSAPFGGALVVDDPDAPREPYVHWIVIGIAPGAGSTADGETPGGGISLPNSSGQPAYTGPCPPAGTGTHHYRFTLYHLPAVPPLAGLAGTQAARVIAQAATMQARLIGTYEG
Protein: Rab8, isoform B (M9NEE8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGSDQTGIDFKIRTIELDNKKIKLQIWDTAGQERFRTITTAYYRGAMGIMLVYDITQEKSFENIKNWIRNIEENASADVEKMLLGNKCELTDKRQVSKERGEQLAIEYGIKFMETSAKASINVEEAFLTLASDIKAKTEKRMEANNPPKGGHQLKPMDSRTKDSWLSRCSLL
Protein: GON-4-like protein (GON-4 homolog) (Q9DB00)
Organism: Mus musculus (Mouse)
Function: Has transcriptional repressor activity, probably as part of a complex with YY1, SIN3A and HDAC1. Required for B cell lymphopoiesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00810, ECO:0000269|PubMed:21454521}.
Interaction partners:
- Transcriptional repressor protein YY1
- Chromatin-remodeling ATPase INO80
- E1A-binding protein p400
- Actin-related protein 8
- Transformation/transcription domain-associated protein
- RuvB-like 1
- Actin-related protein 5
- RuvB-like 2
- Nuclear factor related to kappa-B-binding protein
- Histone acetyltransferase KAT5
Sequence:
MLPCKKRRLSVTESSQQQDDQEGDDLDLEAAVKPDTDQLPDSASESLSWGQSQDSAVCPEGLSMQDGDDQLRAEGLSLNSKMLAQHVNLAVLEAVDVAVSQEIPLPSLESSHSLPVHVDKGRLQVSASKKGKRVVFTPGQVTREDRGDHPVPEEPPSGEPAEEAKTEGGELELRSDGEVPLLSSSSQSAKPGAQPRKSVQPDGSAFPQDKPLGPLVRQAEEEMEDGGLFIPTEEQDSEESDKKKKTKKGTKRKRDGKGPEQGTMVYDPKLDDMLDRTLEDGAKQHNLTAVNVRNILHEVITNEHVVAMMKAAISETEDMPLFEPKMTRSKLKEVVEKGVVIPTWNISPIKKASEIKQPPQFVDIHLEEDDSSDEEYSPDEEEEDETAEESLLESDVESTASSPRGVKRSRLRLSSEVAETDEESGMLSEVEKAATPALRHISAEVVPMGPPPPPKPKQSRDSVFMEKLDAVDEELASSPVCMDSFQPMEDSLIAFRTRSKMPLKDVPLGQLEAELQAPDITPDMYDPNTADDEDWKQWLGGLINDDVENEDEADDDDDPEYNFLEDLDEPDTEDFRTDRAVRITKKEVNGLMEELFETVQSVVPSKFQDEMGFSNMEDDGPEEEERATESRPSFNTPQALRFEEPLANLLNERHRTVKELLEQLKMKKPSVRQQPEVEKLKPQEEAAHQTLVLDPAQRSRLQQQMQQHVQLLTQIYLLTTSNPNLSSEASTTRIFLKELGTFAENSIALHQQFNPRFQTLFQPCNWMGAMRLIEDFTQVSIDCSPHKTAKKTASEFPCLPKQVAWILATNKVFMYPELLPICSLKANNPRDKTIFTKAEDNLLALGLKHFEGTEFPKPLISKYLVTCKTAHQLTVRIKNLNLNRAPNNVIKFYKKTKQLPVLVRCCEEIQPHQWKPPFEKEEHRLPFWLKASLQSIQDELRNISEGATEGGSVTTATESSTDQHLQKASPALGDEPQYPLLLPKGVVLKLKPGSKRFSRKAWRQKRPLVQKPLLIQPSPSVQPVFNPGKMATWPTQSEVPPSNTVVQIPHLIQPAAVLQTLPGFPSVGVRGEDGFESPTALPAMPCGSEARTTFPLSETQSAPPSCSAPKLMLPSLAPSKFRKPYVRRKPTRRKGAKVSPCVKPAPIIHPTPVIFTVPATTVKVVSIGGGCNMIQPVSAAVAPSPQTIPITTLLVNPTTFPCSLNQPLVASSISPLIVSSNPLTLPVTSIPEDKAQVKLDVAEGKNAPQNPESKLKPQELTPLCTTVFSKEEPKSWHSSADTGSQEAFSESSACSWAVVKTESQEGSSEKSACGWTVVKTEDGGHAVEPLPQNLQDSLSSSSKDLLNMVKMEAQDCMVEISSNFPKQDIGEEVKEECSMELDSESPQEKPSSASEMSKQTVLQREDMQAAKSPSVPQDAAAEGRTSSHASRGLPKSTLSSMGQGGGLSGPPGKLEDSANADGQSVGTPAGPDTGGEKDGPEEEEEEDFDDLTQDEEDELSSASEESVLSVPELQETMEKLTWLASERRMSQEGESEEENSQEENSEPEEEEEEEAEGMETLQKEDEVNDEAVGDAAKKPPSTLASPQTAPEIETSIAPAGESIKAAGKGRSSHRARNKRGSRARASKDTSKLLLLYDEDILDRDPLREQKDLAFAQAYLTRVREALQHTPGKYEDFLQIIYEFESSTQMHSAVDLFKSLQTLLQDWPQLLKDFAAFLLPEQALSCGLFEEQQAFEKSRKFLRQLEICFAENPSHHQKIIKVLQGCADCLPQDIAELKTQMWQLLRGHDHLQDEFSIFFDHLRPAASRMGDFEEINWTEEKEYEFDGFEEVILPDVEEDEEPAKVSTASKSKRRKEIGVQHQDKDTEWPEAAKDCSCSCHEGGPESKLKKSKRRNCHCSSKVCDSKPYKSKEPPELVGSGPLHEASTVPGSKEAGQGKDMLEEEILEEQENMEVTQSKTARTTRKGEAPAPGSTIGSTLLCPAEVTPMELLLEGPALCSAETPRLPPQTGAVVCSVRRNQAGPEVVSCLSTSSLPPEEGEDQRAAANSETIAPHREASETERLPETVEHSAPLPSPVSTRTRDTGRRHICGKAGSQSWLIESRAEAEAAHVAAPICEKSSGARASEAAPKTAREVLAEDSGTQGMGPEGALPKASEATVCANNSKVSSTGEKVVLWTREADRVILTMCQEQGAQPHTFSVISQQLGNKTPVEVSHRFRELMQLFHTACEASSEDEDDATSTSNADQLSDHGDLLSEEELDE
Protein: Phospholipase A1 member A (EC 3.1.1.111) (Phosphatidylserine-specific phospholipase A1) (PS-PLA1) (Q8VI78)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes the ester bond of the acyl group attached at the sn-1 position of phosphatidylserines (phospholipase A1 activity) and 1-acyl-2-lysophosphatidylserines (lysophospholipase activity) in the pathway of phosphatidylserines acyl chain remodeling (By similarity). Cleaves phosphatidylserines exposed on the outer leaflet of the plasma membrane of apoptotic cells producing 2-acyl-1-lysophosphatidylserines, which in turn enhance mast cell activation and histamine production. Has no activity toward other glycerophospholipids including phosphatidylcholines, phosphatidylethanolamines, phosphatidic acids or phosphatidylinositols, or glycerolipids such as triolein (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P97535}.
Interaction partners:
- Phosphatidylserine synthase 2
- Membrane-bound glycerophospholipid O-acyltransferase 1
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Phosphatidylserine synthase 1
- Lysophospholipid acyltransferase 5
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Lysophospholipid acyltransferase LPCAT4
Sequence:
MRPGLWETCFWLWGPLLWLSIGSSGNVPPTTQPKCTDFQSANLLRGTNLKVQFLLFTPSDPSCGQLVEEGSDIRSSEFNASLGTKVIIHGFRALGTKPSWIDKFISAVLRAADANVIAVDWVYGSTGVYYSAVENVVKLSLEISRFLSKLLELGVSESSIHIIGVSLGAHVGGMVGHFYKGQLGQITGLDPAGPEYTRASLEERLDAGDALFVEAIHTDTDNLGIRIPVGHVDYFVNGGQDQPGCPAFFHAGYNYLICDHMRAVHLYISALENTCPLMAFPCASYKAFLAGDCLDCFNPFLLSCPRIGLVERGGVMIEPLPKEVKVYLLTTSSAPYCVHHSLVEFYLKEKRKKDTSIEVTFLSNNVTSSVKITIPKQQLEGRGVMAHPNPQCQINQVKLKFQVSSRVWRKDRTPVVGTFCTAPLPVNDSKKTVCIPEPVRLQAGVPAFQDLKIACV