wanglab/gogpt-training-data huggingface dataset:
Protein: CTD nuclear envelope phosphatase 1 homolog (CTDNEP1) (EC 3.1.3.16) (Serine/threonine-protein phosphatase dullard homolog) (Small C-terminal domain phosphatase-like phosphatase 21) (Q20432)
Organism: Caenorhabditis elegans
Function: Serine/threonine protein phosphatase that may dephosphorylate and activate lipin-like phosphatases. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. Contributes to closure of nuclear envelope (NE) holes and prevents excess nuclear membranes after meiosis and mitosis, possibly through spatial regulation of lipin. May limit the production of endoplasmic reticulum (ER) sheets proximal to the NE to prevent the ER membranes that feed into NE openings from invading the nuclear interior and thereby restrict nuclear transport to nuclear pore complexes (NPCs). May also indirectly regulate the production of lipid droplets and triacylglycerol.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:32271860}.
Interaction partners:
- Nuclear envelope phosphatase-regulatory subunit 1 homolog
- LNS2/PITP domain-containing protein
- Phosphatidate cytidylyltransferase
- Charged multivesicular body protein 7
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phenylalanine-4-hydroxylase
- diacylglycerol cholinephosphotransferase
- EthanolaminePhosphoTransferase 1 homolog
- Transcription initiation factor IIF subunit alpha
- LEM protein 2
Sequence:
MTTIAQSVFCFLAGFFNFFLLYFRKTSRAYCKYQVVKYHSNIPMSPLTTHRLLTVKRKILVLDLDETLIHSHHDGVLRQTVKPGTPSDFTIRVVIDRHPVKFSVHERPHVDYFLSVVSQWYELVVFTASMEVYGTSVADRLDRGRGILKRRYFRQHCTMEVGGYTKDLSAIHPDLSSICILDNSPGAYRKFPHNAIPIPSWFSDPNDTCLLNLLPFLDALRFTSDVRSVLSRNMQALPETQSVQYY
Protein: Abscisic stress-ripening protein 5 (OsASR5) (Q53JF7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May function in gibberellin signaling pathway downstream of GID1 and SLR1. May be involved in the regulation of plant growth in the basal region of leaf sheaths (Probable). Involved in tolerance to aluminum. Regulates the expression of different genes that collectively contribute to the protection of the cell in response to aluminum stress. Binds to the promoter and regulates the expression of target genes involved in aluminum stress response. Binds to the promoter of STAR1 gene, which encodes an ABC transporter required for aluminum tolerance. Involved in drought tolerance. Plays a positive role in response to drought stress response by regulating abscisic acid (ABA) biosynthesis, promoting stomatal closure, and acting as chaperone-like protein that possibly prevents drought stress-related proteins from inactivation.
Subcellular location: Nucleus {ECO:0000269|PubMed:18210155, ECO:0000269|PubMed:22676236}. Cytoplasm {ECO:0000269|PubMed:18210155, ECO:0000269|PubMed:22676236}.
Interaction partners:
Sequence:
MAEEKHHHHLFHHKKDDEPATGVDSYGEGVYTSETVTTEVVAGGQDEYERYKKEEKQHKHKQHLGEAGALAAGAFALYEKHEAKKDPENAHRHKITEEIAATAAVGAGGYAFHEHHEKKKDHKSAEESTGEKKHHLFG
Protein: Calcium-dependent protein kinase 27 (EC 2.7.11.1) (Q9ZSA4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in signal transduction pathways that involve calcium as a second messenger.
Subcellular location: Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Proton pump-interactor 2
- Protein gamma response 1
- Respiratory burst oxidase homolog protein B
Sequence:
MGCFSSKELQQSKRTILEKPLVDITKIYILGEELGRGNFGLTRKCVEKSTGKTFACKTILKTKLKDEECEEDVKREIRIMKQLSGEPNIVEFKNAYEDKDSVHIVMEYCGGGELYDKILALYDVGKSYSEKEAAGIIRSIVNVVKNCHYMGVMHRDLKPENFLLTSNDDNATVKVIDFGCSVFIEEGKVYQDLAGSDYYIAPEVLQGNYGKEADIWSAGIILYILLCGKSPFVKEPEGQMFNEIKSLEIDYSEEPWPLRDSRAIHLVKRMLDRNPKERISAAEVLGHPWMKEGEASDKPIDGVVLSRLKRFRDANKFKKVVLKFIAANLSEEEIKGLKTLFTNIDTDKSGNITLEELKTGLTRLGSNLSKTEVEQLMEAADMDGNGTIDIDEFISATMHRYKLDRDEHVYKAFQHFDKDNDGHITKEELEMAMKEDGAGDEGSIKQIIADADTDNDGKINFEEFRTMMRTESSLQPEGELLPIIN
Protein: Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.24) (A0A1D8PMU9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|RuleBase:RU365032}.
Interaction partners:
- Kinase
- Inositol-pentakisphosphate 2-kinase
Sequence:
MDTDNFEDVKAYTVGPNFCHAETRKSPVVDGIVRRNTHGKEIRYVTELTDEEKTMAKNVSSAFKQTICGFDLLRVNGKSFVIDVNGFSFVKDNNEYYDSCASILRGLFIDAKKSRDLLTRKIPKMLQTSQFEQKAQKWVFKGMVTVIRHADRTPKQKFKYSFRSPVFISLLKGHREEVIIRAVPDLQVVLETVKIAEAKGLEDLNKLKQLRIALEKKMDFPGTKIQLKPTLNAENPEVVDKVQLILKWGGEPTHSAKHQATDVGEQMRQNLQLLNREALDDVKVYTSSERRVIASAQYFSASLLSIDEPLADDFLIVRKDLLDDSNAAKDLMDKVKKKLKPLLREGAEAPPQFTWPPKMPQPFEVIKRVCELMNFYHQIMNYNFETKNVQEFQINWCCGEDPFLFKERWDKLFQEFISVEKTHPSKISELYDTMKYDALHNRHFLQKIFSYDPNDKVLLSRLTETCGSTVNSSGLVSEYPINILAMNNFKLPESASTSANNSSSNLNSNSAAGSLGWVLSGAATTMKCESKDTSASPQTPFDHPTFARLRELYRLSKVLFDFICPQEYGIKDEEKLDIGLLTSLPLAKQILSDIYDMKKNDRPALVNYFTKESHIYTLLNIIYGSQLPMKIARNALPELDYLSQIVFELYEAEDPSSPTGKKHSIRLSLSPGCHTQDPLDVQLDDDHYIGCIPRISLTRHLDMDLVTQRLKSRFSRVSLPKKFTPVNITGPLNSK
Protein: Glycerol-3-phosphate acyltransferase 2, mitochondrial (GPAT-2) (EC 2.3.1.15) (1-acylglycerol-3-phosphate O-acyltransferase GPAT2) (EC 2.3.1.51) (xGPAT1) (Q14DK4)
Organism: Mus musculus (Mouse)
Function: Transfers an acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate producing a lysophosphatidic acid (LPA), an essential step for the triacylglycerol (TAG) and glycerophospholipids. In vitro also transfers an acyl-group from acyl-ACP to the LPA producing a phosphatidic acid (PA). Prefers arachidonoyl-CoA as the acyl donor. Required for primary processing step during piRNA biosynthesis. Molecular mechanisms by which it promotes piRNA biosynthesis are unclear and do not involve its acyltransferase activity.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:17013544, ECO:0000269|PubMed:17689486, ECO:0000269|PubMed:22285183}; Multi-pass membrane protein {ECO:0000269|PubMed:17013544, ECO:0000269|PubMed:17689486, ECO:0000269|PubMed:22285183}.
Interaction partners:
- Glycerol-3-phosphate acyltransferase 4
- Glycerol-3-phosphate acyltransferase 3
- Glycerol-3-phosphate dehydrogenase 1-like protein
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Glycerol-3-phosphate dehydrogenase [NAD
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Glycerol kinase 2
- Glycerol kinase
- glycerol kinase
- Acylglycerol kinase, mitochondrial
Sequence:
MDTMLKSNPQTQQRSNHNGQETSLWSSSFGMKMEAITPFLGKYRPFMGRCCQTCTPKSWESLFHRSIMDLGFCNVILVKEENTRFRGWLVRRLCYFLWSLEQHIPTSFDASQKIMENTGVQNLLSGRVPGAAGEGQAPELVKKEVQRILGHIQTTPRPFLLRLFSWALLWFLNRLFLNVQLHKGQMKMVQKAVQEGSPLVFLSTHKSLLDGFLLPFVLFSQGLGVVRVALDSRTCSPALRALLRKLGGLFLPPEVNLSLDNSEGILARAVVRATVEELLTSGQPLLIFLEEPPGSPGPRLSALGQAWLGVVIQAVQAGIISDATLVPVAIAYDLVPDAPCNMNHDLAPLGLWTGALAVFRRLCNCWGCNRRVCVRVHLAQPFSLQEYTINARSCWDSRQTLEHLLQPIVLGECSVVPDTEKEQEWTPPTGLLLALKEEDQLLVRRLSRHVLSASVASSAVMSTAIMATLLLLKHQKGVVLSQLLGEFSWLTEETLLRGFDVGFSGQLRCLAQHTLSLLRAHVVLLRVHQGDLVVVPRPGPGLTHLARLSMELLPTFLSEAVGACAVRGLLAGRVPPEGPWELQGIELLSQNELYRQILLLLHLLPQDLLLPQPCQSSYCYCQEVLDRLIQCGLLVAEETPGSRPACDTGRQHLSAKLLWKPSGDFTDSESDDFEEPGGRCFRLSQQSRCPDFFLFLCRLLSPILKAFAQAATFLHLGQLPDSEVAYSEKLFQFLQACAQEEGIFECADPNLAISAVWTFKDLGVLQEMPSPTGPQLHLSPTFATRDNQDKLEQFIRQFICS
Protein: Alpha-mannosidase 2 (EC 3.2.1.114) (Golgi alpha-mannosidase II) (AMan II) (Man II) (Golgi alpha-mannosidase IIa) (Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase) (Q24451)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10504337}; Single-pass type II membrane protein {ECO:0000269|PubMed:10504337}.
Interaction partners:
- Alpha-1,3-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Alpha-
- Coatomer subunit beta'
- Metallophosphoesterase, isoform E
- Alpha-mannosidase
- alpha-1,2-Mannosidase
- Fucosyltransferase
Sequence:
MLRIRRRFALVICSGCLLVFLSLYIILNFAAPAATQIKPNYENIENKLHELENGLQEHGEEMRNLRARLAETSNRDDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHKLKVFVVPHSHNDPGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEFVTGGWVMPDEANSHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQRQLEFLWRQIWDNKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVDQWKKKAELYRTNVLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTLSGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKTHVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNTLPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSKPEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSHGDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDSGDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQGVLDNKPVLHIYRLVLEKVNNCVRPSELHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVSVMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYVSSHSS
Protein: C-X-C motif chemokine 14 (Chemokine BRAK) (MIP-2G) (Small-inducible cytokine B14) (O95715)
Organism: Homo sapiens (Human)
Function: Potent chemoattractant for neutrophils, and weaker for dendritic cells. Not chemotactic for T-cells, B-cells, monocytes, natural killer cells or granulocytes. Does not inhibit proliferation of myeloid progenitors in colony formation assays.
Subcellular location: Secreted.
Interaction partners:
- Stromal cell-derived factor 1
- C-X-C motif chemokine 5
- Eotaxin
- C-C motif chemokine 21
- C-X-C motif chemokine 17
- C-X-C motif chemokine 11
- C-X-C motif chemokine 9
- C-C motif chemokine 13
- C-C motif chemokine 5
- C-C motif chemokine 17
Sequence:
MSLLPRRAPPVSMRLLAAALLLLLLALYTARVDGSKCKCSRKGPKIRYSDVKKLEMKPKYPHCEEKMVIITTKSVSRYRGQEHCLHPKLQSTKRFIKWYNAWNEKRRVYEE
Protein: Interferon regulatory factor 2 (K4DIA5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPVERMRMRPWLEEQINSNTIPGLKWLNKEKKIFQIPWMHAARHGWDVEKDAPLFRNWAIHTGKHQPGVDKPDPKTWKANFRCAMNSLPDIEEVKDKSIKKGNNAFRVYRMLPLSERPSKKGKKPKTEKEDKVKHIKQEPVESSLGLSNGVSDLSPEYAVLTSTIKNEVDSTVNII
Protein: DNA-directed RNA polymerase subunit alpha (PEP) (EC 2.7.7.6) (Plastid-encoded RNA polymerase subunit alpha) (RNA polymerase subunit alpha) (P0C499)
Organism: Oryza sativa subsp. indica (Rice)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Uncharacterized protein
- Small ribosomal subunit protein uS8c
- Small ribosomal subunit protein uS2c
- Small ribosomal subunit protein uS12cz/uS12cy
- Small ribosomal subunit protein uS14c
- Large ribosomal subunit protein uL16c
- Large ribosomal subunit protein mL46
- S5 DRBM domain-containing protein
- Small ribosomal subunit protein mS35 mitochondrial conserved domain-containing protein
- Small ribosomal subunit protein uS11c
Sequence:
MVREEVAGSTQTLQWKCVESRVDSKRLYYGRFILSPLRKGQADTVGIALRRALLGETEGTCITHAKFGSVPHEYSTIAGIEESVQEILLNLKEIVLRSNLYGVRTASICVKGPRYITAQDIILPPSVEIVDTAQPIANLTEPTDFRIELRIKRDRGYHTEVRKNTQDGSYPIDAVSMPVRNVNYSIFACGNGNAKYEILFLEIWTNGSLTPKEALYEASRNLIDLFLPFLHTEEEGTRFQENKNRFTSPLLSFQKRLTNLKKNKKRIPLNCIFIDQLELPSRTYNCLKRANIHTLLDLLSKTEEDLMRIDSFRMQDGKQIWDTLEKHLPMDLPKNKF
Protein: Methyl-coenzyme M reductase I subunit alpha (MCR I alpha) (EC 2.8.4.1) (Coenzyme-B sulfoethylthiotransferase alpha) (P11558)
Organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Function: Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2-(methylthio)ethanesulfonate) using coenzyme B (CoB or 7-mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis. Neither N-6-mercaptohexanoylthreonine phosphate (H-S-HxoTP) nor N-8-mercaptooctanoylthreonine phosphate (H-SOcoTP) nor any other thiol compound such as CoA or CoM can substitute for CoB as the electron donor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23533332}. Note=Under growth limiting conditions on nickel-depleted media, a fraction of 70% of the enzyme is localized close to the cytoplasmic membrane, which implies 'facultative' membrane association of the enzyme. {ECO:0000269|PubMed:23533332}.
Interaction partners:
- Methyl-coenzyme M reductase I subunit gamma
- Methyl-coenzyme M reductase I subunit beta
- Tungsten-containing formylmethanofuran dehydrogenase 2 subunit C
- Methyl-coenzyme M reductase I operon protein D
- Methyl-coenzyme M reductase I operon protein C
- Methyl-coenzyme M reductase II subunit beta
- Methyl-coenzyme M reductase II subunit gamma
- Tetrahydromethanopterin S-methyltransferase subunit A 1
- Tetrahydromethanopterin S-methyltransferase subunit H
- Tetrahydromethanopterin S-methyltransferase subunit A 2
Sequence:
MADKLFINALKKKFEESPEEKKTTFYTLGGWKQSERKTEFVNAGKEVAAKRGIPQYNPDIGTPLGQRVLMPYQVSTTDTYVEGDDLHFVNNAAMQQMWDDIRRTVIVGLNHAHAVIEKRLGKEVTPETITHYLETVNHAMPGAAVVQEHMVETHPALVADSYVKVFTGNDEIADEIDPAFVIDINKQFPEDQAETLKAEVGDGIWQVVRIPTIVSRTCDGATTSRWSAMQIGMSMISAYKQAAGEAATGDFAYAAKHAEVIHMGTYLPVRRARGENEPGGVPFGYLADICQSSRVNYEDPVRVSLDVVATGAMLYDQIWLGSYMSGGVGFTQYATAAYTDNILDDFTYFGKEYVEDKYGLCEAPNNMDTVLDVATEVTFYGLEQYEEYPALLEDQFGGSQRAAVVAAAAGCSTAFATGNAQTGLSGWYLSMYLHKEQHSRLGFYGYDLQDQCGASNVFSIRGDEGLPLELRGPNYPNYAMNVGHQGEYAGISQAPHAARGDAFVFNPLVKIAFADDNLVFDFTNVRGEFAKGALREFEPAGERALITPAK
Protein: Serine/threonine-protein phosphatase PGAM5, mitochondrial (EC 3.1.3.16) (Phosphoglycerate mutase family member 5) (Q8BX10)
Organism: Mus musculus (Mouse)
Function: Displays phosphatase activity for serine/threonine residues, and, dephosphorylates and activates MAP3K5 kinase. Has apparently no phosphoglycerate mutase activity. May be regulator of mitochondrial dynamics. Substrate for a KEAP1-dependent ubiquitin ligase complex. Contributes to the repression of NFE2L2-dependent gene expression (By similarity). Acts as a central mediator for programmed necrosis induced by TNF, by reactive oxygen species and by calcium ionophore.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q96HS1}; Single-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96HS1}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Bcl-2-like protein 1
- Kelch-like ECH-associated protein 1
- Mixed lineage kinase domain-like protein
- Dynamin-1-like protein
- FUN14 domain-containing protein 1
- Serine/threonine-protein kinase PINK1, mitochondrial
- Receptor-interacting serine/threonine-protein kinase 1
- Presenilin-associated rhomboid-like protein, mitochondrial
- Prohibitin-2
- Suppressor of cytokine signaling 6
Sequence:
MAFRQALQLAACGLAGGSAAVLFSAVAVGKPRGGGDADTRATEPPAWTGARAGRGVWDTNWDRREPLSLINLKKRNVESGEDELTSRLDHYKAKATRHIFLIRHSQYHVDGSLEKDRTLTPLGREQAELTGLRLASLGLKFNKIVHSSMTRAVETTDIISKHLPGVSRVSTDLLREGAPIEPDPPVSHWKPEAVQYYEDGARIEAAFRNYIHRADARQEEDSYEIFICHANVIRYIVCRALQFPPEGWLRLSLNNGSITHLVIRPNGRVALRTLGDTGFMPPDKITRS
Protein: Coiled-coil-helix-coiled-coil-helix domain containing 1 (A6NJX6)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MATPSLRGRLARFGNPRKPVLKPNKPLILANRVGERRREKGEATCITEMSVMMACWKQNEFRDDACRKEIQGFLDCAARAQVTDGSWGAFSGKEWGR
Protein: CLAVATA3/ESR (CLE)-related protein 16 [Cleaved into: CLE16p] (Q8S8M2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Extracellular signal peptide that regulates cell fate. Represses root apical meristem maintenance. Regulates the transition of protophloem cells from proliferation to differentiation, thus impinging on postembryonic growth capacity of the root meristem; this signaling pathway requires CRN and CLV2.
Subcellular location: [CLE16p]: Secreted, extracellular space {ECO:0000250|UniProtKB:O49519}.
Interaction partners:
- CLAVATA3/ESR
- F-box protein At4g02733
- Defensin-like protein 8
- Putative defensin-like protein 3
- CLAVATA3/ESR
- F-box protein At4g00893
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
- CLAVATA3/ESR
Sequence:
MEACSRKRRRRRAYTTSTTGYAAVFFCGIFVFAQFGISSSALFAPDHYPSLPRKAGHFHEMASFQAPKATVSFTGQRREEENRDEVYKDDKRLVHTGPNPLHN
Protein: Chemokine CK-1 (Q9W691)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MISCRVCVLAALFSLLIITLIPTTQSADCCLKFTRRPVHCRWLKGYTFQDITSSCDLNAVIFQNLRNKFVCADPSQDWTKRVQRCLRKRQEKKSQLKKRV
Protein: dual-specificity kinase (EC 2.7.12.1) (H3BUL5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MHHCKRYRSPEPDPYLSYRWKRRRSYSREHEGRLRYPSRREPPPRRSRSRSHDRLPYQRRYRERRDSDTYRCEERSPSFGEDYYGPSRSRHRRRSRERGPYRTRKHAHHCHKRRTRSCSSASSRSQQSSKRSSRSVEDDKEGHLVCRIGDWLQERYEIVGNLGEGTFGKVVECLDHARGKSQVALKIIRNVGKYREAARLEINVLKKIKEKDKENKFLCVLMSD
Protein: TERF1 interacting nuclear factor 2 (H0YKA6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEKLLFEYLCQLEKALPTPQAQQLQDVLSWMQPGVSITSSLAWRQYGVDMGWLLPECSVTDSVNLAEPMEQNPPQQQRLALHNPLPKAKPGTHLPQGPSSRTHPEPLAGRHFNLAPLGRRRVQSQWASTRGGHKERPTVMLFPFRN
Protein: Alpha-defensin 20 (Cryptdin-4) (Defensin-related cryptdin-20) (Q45VN2)
Organism: Mus musculus (Mouse)
Function: May have microbicidal activities.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Cysteine-rich protein 2
Sequence:
MKTLVLLSALVLLAFQVQADPIQNTDEETNTEEQPGEEDQAVSVSFGDPEGSALHEKSSRDLICYCRKGGCNRGEQVYGTCSGRLLFCCRRRHRH
Protein: Trafficking protein particle complex subunit 5 (Q9CQA1)
Organism: Mus musculus (Mouse)
Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Trafficking protein particle complex subunit 4
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit 2
- Trafficking protein particle complex 8
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex subunit 3
- Trafficking protein particle complex subunit 6A
- Trafficking protein particle complex subunit 9
- Trafficking protein particle complex subunit 10
- Trafficking protein particle complex subunit 6B
Sequence:
MEARFTRGKSALLERALVRPRTEVSLSAFALLFSELVQHCQSRVFSVAELQARLAALGRQVGARVLDALVAREKGARRETKVLGALLFVKGAVWKALFGKEADKLEQANDDARTFYIIEREPLINTYISVPKENSTLNCASFTAGIVEAVLTHSGFPAKVTAHWHKGTTLMIKFEEAVIARDRALEGR
Protein: Tail fiber protein (A8E283)
Organism: Enterococcus phage phiEF24C (Enterococcus bacteriophage phi-EF24C)
Function: Structural protein, a component of a tail fiber.
Subcellular location: Virion {ECO:0000269|PubMed:22046321}.
Interaction partners:
Sequence:
MNKLVKRRFQAGLGSEIKRVYKEGQQINTLLLAQVIQVNYKYNTVDLLALQHKEVFQNSYANEGRFSARLPMEFGGRNIVGQPYGQVNPIAVGTVVLVGFINSDKDMPIVISVYNNNDVSKQLSRTQFSNSDPKDLELIGDMHQKFSLYPSLTYDSVDGEGGRVVTFSGKSFIAFDTKEVANSSTTDAGYGTKYEDLETSYYNNGDLIEPMKGRAPNVLFKHQGVLDDDGKPDLHDLLIHINPDGTYRTSMMNKEEDWRTLFEMTPDGRVKLRKQDSINIDGGIEISELGINNEGFVYLRNGDMDLEVRKDGIYSQGKLFTADVDLSDVYDKLNGLSIQIKETNGQLEIIANGVEEQNGKISELSTEITIVAGKVESKVTKTEVQDMIDSSFVDMSDAIKKAQEDADKANKVIADMSSDNRLTPSEKIDLLKEWDIIKNEYPSYLEQAETYEVDSKDYTAKYNSLELFVTPILADMESTSSVDGATLRKTFNSYYTARIALLNSISKKLKDGITEAMKKASQASLDATQAMADASQAKIDADNANKLISDIASDNKLTPSEKYQLKKEWDVIVKEYPTTIAQAEKYAVDTAEYTAKYKALELFVEPLFKDMDETSIVDGERLRATFSDYYASKIALLKEVTDSAKTELDAYGNKISVMETNITQTSEAITLLATRVQTVEDGVQSNKAQIEIQAEQISQKVTASEVKGIVDDSINNLTLGGTNLFVIKTQTAGLLNENDGTVGTAVDNSVVSDYIKVNQKTPYIATLYGNTGTNMIITDWYDKNRTFISGEAVADSGDFSKKYVSPENAVYARVSYKKANSVNIKFEAGTKATDYSPSWEDIKGDQTALEEYIKKVEEQAKKAQQDAENAKNDAENANNAIADMSNDNMLAPNEKKQILLQWEQIKTEYPINLDQATKFGVSSQQYTTAYNALDEYLKPILADMTTTSVVVGSTLRNTFNNYYDKRTTLLNRISDVAKNVADKAQETADTINDNLQNIGGYNYVGFSSGDNMLPRLMIKNVGYYTLGSSTTEFIDSMVAVKGDATTQPFDYTVGTSDKEIAGGGLADYRMKEVKEGQWLTASANVQVIDGGSARLAIYTLEGDNWVGSNSTPIQVSDGLKRVVAQRKVTGLTKGVLIRIESADTNVKEFRFGNVQLEVGIIPTPWKKSDIDIQEDINNVVQNIKTYTAWANDLQGLDFTREKVEGKTYMYVGTSMKDSDNYSDYTWRLTDEHIEGQINGKEGAWIYSPTAPTNPSQGLIWVDLSKVPNQPKRWVDSETGWVALTPEEVKDLPWGEDGTNLADWVAQAEQRISSDSIINTVLGSEDFTSVFDTKANTTDLDNLATYEDLDSIKEDYNRLIKEGINGIDFTPYVTNSELQQLKDSFNFSVQQAGGVNMLKNSLGFSGLDFWDGTVGKNLLPNSTWNLGFGRWGGASIASFEILPPEDDKPTSHILGSIGSRSSTKEIGNRPHPLKVNSGETYTISFDYKEEALAYDKDRPILVVRNYPDKDTDQWMEYSIEGWAVMANGSTTDLTVWRRFTKTFTIGTSGYLDILPKTIVESWTHRSFWRELKIEEGSQATTWVPNKEDGAFTGGIVETTQTEELANLGFGSGFVSSKRPSSSLTQSVELPEIGANLEYSLSFYMKVTTDNPVADFKCGIRVYEGDTLTYTLGIEDATQPIPLGFQQYKLVFTPTSTSTKIEMFVENGQEASVIISGIMYNIGNIPLKWQPYPSEIYNTNVKIDINGVTVKNNQTDGYTMITPQEFSGYSRIDGNIERIFTLNGQVTEVKMLKAEKRITMEPVSVFAMNTVTDTKRIRGWAFVPSFE
Protein: Prothrombin (EC 3.4.21.5) (Coagulation factor II) [Cleaved into: Activation peptide fragment 1; Activation peptide fragment 2; Thrombin light chain; Thrombin heavy chain] (P00735)
Organism: Bos taurus (Bovine)
Function: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing (By similarity).
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Fibrinogen alpha chain
- Antithrombin-III
- Serpin family D member 1
- Fibrinogen beta chain
- Thrombomodulin
- Fibrinogen gamma-B chain
- Proteinase-activated receptor 1
- Proteinase-activated receptor 3
- Coagulation factor V
- Proteinase-activated receptor 4
Sequence:
MARVRGPRLPGCLALAALFSLVHSQHVFLAHQQASSLLQRARRANKGFLEEVRKGNLERECLEEPCSREEAFEALESLSATDAFWAKYTACESARNPREKLNECLEGNCAEGVGMNYRGNVSVTRSGIECQLWRSRYPHKPEINSTTHPGADLRENFCRNPDGSITGPWCYTTSPTLRREECSVPVCGQDRVTVEVIPRSGGSTTSQSPLLETCVPDRGREYRGRLAVTTSGSRCLAWSSEQAKALSKDQDFNPAVPLAENFCRNPDGDEEGAWCYVADQPGDFEYCDLNYCEEPVDGDLGDRLGEDPDPDAAIEGRTSEDHFQPFFNEKTFGAGEADCGLRPLFEKKQVQDQTEKELFESYIEGRIVEGQDAEVGLSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTVDDLLVRIGKHSRTRYERKVEKISMLDKIYIHPRYNWKENLDRDIALLKLKRPIELSDYIHPVCLPDKQTAAKLLHAGFKGRVTGWGNRRETWTTSVAEVQPSVLQVVNLPLVERPVCKASTRIRITDNMFCAGYKPGEGKRGDACEGDSGGPFVMKSPYNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDRLGS
Protein: At5g64156 (RNA methyltransferase family protein) (Q9FMI5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Multifunctional methyltransferase subunit TRM112 homolog A
- Multifunctional methyltransferase subunit TRM112 homolog B
- Peptide chain release factor APG3, chloroplastic
- Peptide chain release factor PrfB1, chloroplastic
- Class I peptide chain release factor
- Peptide chain release factor PrfB2, chloroplastic
- Peptide chain release factor PrfB3, chloroplastic
- Iron-sulfur assembly protein IscA-like 2
- Peptide chain release factor 1
- T10F20.8 protein
Sequence:
MIRIFPSLRLTSLLSAAKPLCSSSPAKKPPQYTSLTESKSSRPTKSLSITPKTPLYLRTPSHATSLSEVWKWHDWAKDLASSVEESSKNSEDTLDSVILHRELKWLIEDSIVDDPLVILHRSEIADNGEKNVKLRASLEELYDLWRQRIEKRRPFQYVVGCEHWRDLVLCVEEGVLIPRPETELIVDMVEELVTRDEWFKKDIWADLGTGSGAIAIGIAKVLGSRGRVIATDLSPVAIAVAGHNVQRYSLEGMIEVREGSWFEPLKDLEGKLVGLVSNPPYIPSDDIPGLQAEVGRHEPKLALDGGIDGTDSLFHLCHGASRMLQPGGFFVFETNGEKQSKMIVDYMMTSDLKDCFSDLKIVSDFAGINRFVTGFRL