wanglab/gogpt-training-data huggingface dataset:
Protein: CX3C chemokine receptor 1 (C-X3-C CKR-1) (CX3CR1) (Fractalkine receptor) (P35411)
Organism: Rattus norvegicus (Rat)
Function: Receptor for the C-X3-C chemokine fractalkine (CX3CL1) present on many early leukocyte cells; CX3CR1-CX3CL1 signaling exerts distinct functions in different tissue compartments, such as immune response, inflammation, cell adhesion and chemotaxis. CX3CR1-CX3CL1 signaling mediates cell migratory functions. Responsible for the recruitment of natural killer (NK) cells to inflamed tissues. Acts as a regulator of inflammation process leading to atherogenesis by mediating macrophage and monocyte recruitment to inflamed atherosclerotic plaques, promoting cell survival. Involved in airway inflammation by promoting interleukin 2-producing T helper (Th2) cell survival in inflamed lung. Involved in the migration of circulating monocytes to non-inflamed tissues, where they differentiate into macrophages and dendritic cells. Acts as a negative regulator of angiogenesis, probably by promoting macrophage chemotaxis. Plays a key role in brain microglia by regulating inflammatory response in the central nervous system (CNS) and regulating synapse maturation. Required to restrain the microglial inflammatory response in the CNS and the resulting parenchymal damage in response to pathological stimuli. Involved in brain development by participating in synaptic pruning, a natural process during which brain microglia eliminates extra synapses during postnatal development. Synaptic pruning by microglia is required to promote the maturation of circuit connectivity during brain development. Acts as an important regulator of the gut microbiota by controlling immunity to intestinal bacteria and fungi. Expressed in lamina propria dendritic cells in the small intestine, which form transepithelial dendrites capable of taking up bacteria in order to provide defense against pathogenic bacteria. Required to initiate innate and adaptive immune responses against dissemination of commensal fungi (mycobiota) component of the gut: expressed in mononuclear phagocytes (MNPs) and acts by promoting induction of antifungal IgG antibodies response to confer protection against disseminated C.albicans or C.auris infection (By similarity). Also acts as a receptor for C-C motif chemokine CCL26, inducing cell chemotaxis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P49238}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Fractalkine
- C-C motif chemokine 2
- C-C motif chemokine 5
- Stromal cell-derived factor 1
- OX-2 membrane glycoprotein
- C-C motif chemokine 3
- C-X-C motif chemokine 10
- C-C motif chemokine
- C-C motif chemokine
- Guanine nucleotide-binding protein G
Sequence:
MPTSFPELDLENFEYDDSAEACYLGDIVAFGTIFLSIFYSLVFTFGLVGNLLVVLALTNSRKSKSITDIYLLNLALSDLLFVATLPFWTHYLISHEGLHNAMCKLTTAFFFIGFFGGIFFITVISIDRYLAIVLAANSMNNRTVQHGVTISLGVWAAAILVASPQFMFTKRKDNECLGDYPEVLQEIWPVLRNSEVNILGFVLPLLIMSFCYFRIVRTLFSCKNRKKARAIRLILLVVVVFFLFWTPYNIVIFLETLKFYNFFPSCGMKRDLRWALSVTETVAFSHCCLNPFIYAFAGEKFRRYLRHLYNKCLAVLCGRPVHAGFSTESQRSRQDSILSSLTHYTSEGEGSLLL
Protein: Tyrosine aminotransferase (TyrAT) (EC 2.6.1.5) (Aromatic-amino-acid transaminase) (EC 2.6.1.57) (Aspartate aminotransferase) (EC 2.6.1.1) (O85746)
Organism: Klebsiella pneumoniae
Function: catalyzes the formation of methionine from 2-keto-4-methylthiobutyrate (KMTB) primarily using aromatic amino acids (tyrosine, phenylalanine and tryptophan) or glutamate as the amino donors. Histidine, leucine, asparagine, or arginine are also functional amino donors but to a lesser extent. Can also use alpha-ketoglutarate, oxaloacetate and pyruvate as the amino acceptors.
Interaction partners:
Sequence:
MFQKVDAYAGDPILSLMERFKEDPRSDKVNLSIGLYYNDDGIIPQLQAVAEAEARLNAEPHGASLYLPMEGFSGYRQAIAPLLFGAEHTALKQNRIASIQTVGGSGALKVGADFLKRYFPESHVWVSDPTWENHIAIFEGAGFEVSTYPWFDKATNGVRFENLLAMLQTLPARDIVLLHPCCHNPTGADLTPAQWDRVVEVLKARQLIPFLDIAYQGFGGGLEEDAYAIRAIASAGMPMLVSNSFSKIFSLYGERVGGLSVVCEDSETAGRVLGQLKATVRRNYSSPPSFGAQVVATVLNDAALKATWQAEVDAMRAHILTMRQALVDALQQVAPGSKVDYLLKQRGMFSYTGFSAAQVDRLRDEFGVYLIASGRMRVAGLNSRNVQQVAKAFVAVM
Protein: Mitotic spindle checkpoint component MAD2 (Mitotic MAD2 protein) (P40958)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Central component of the spindle assembly checkpoint which is a feedback control that prevents cells with incompletely assembled spindles from leaving mitosis. Thought to be recruited to unattached kinetochores by MAD1. During checkpoint activity, MAD2 is relayed from the MAD1-MAD2 complex to the mitotic checkpoint complex (MCC). MCC and presumably the MAD2-CDC20 subcomplex inhibit the ubiquitin ligase activity of the anaphase promoting complex/cyclosome (APC/C) by preventing its activation by CDC20.
Subcellular location: Nucleus.
Interaction partners:
- Spindle assembly checkpoint component MAD3
- Spindle assembly checkpoint protein BUB3
- Spindle assembly checkpoint serine/threonine-protein kinase BUB1
- Serine/threonine-protein kinase MPS1
- Spindle assembly checkpoint component MAD1
- APC/C activator protein CDC20
- APC/C activator protein CDH1
- Anaphase-promoting complex subunit CDC16
- Mitotic check point protein BUB2
- Anaphase-promoting complex subunit DOC1
Sequence:
MSQSISLKGSTRTVTEFFEYSINSILYQRGVYPAEDFVTVKKYDLTLLKTHDDELKDYIRKILLQVHRWLLGGKCNQLVLCIVDKDEGEVVERWSFNVQHISGNSNGQDDVVDLNTTQSQIRALIRQITSSVTFLPELTKEGGYTFTVLAYTDADAKVPLEWADSNSKEIPDGEVVQFKTFSTNDHKVGAQVSYKY
Protein: Phosphoinositide phospholipase C (EC 3.1.4.11) (A0A1D8PRE4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- 1-phosphatidylinositol-4-phosphate 5-kinase
- Kinase
- Phosphatidylinositol 4-kinase PIK1a
- 1-phosphatidylinositol 4-kinase
- phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol 4-kinase
- Phosphatidylinositol 3-kinase VPS34
- phosphoinositide 5-phosphatase
- phosphoinositide 5-phosphatase
Sequence:
MLESLNRRNSIDSNQGDNDNDNDNHSNDELSPSELYYSPSGSPPKSQLLLRKSSSPSSYSPIKSDLPNIYSHLRSNDSESPPQPSPKQQSSLSSSSSSSSSSNTKSSTTKNIFKKLLRINKSSDNIDESRSIVSNNGGSPMSDSTTVTSTLSTDTAPKRGKSIQRSQILHHTDSDSLYLENQIELRPEISKSIGNIKIPSIFTNDGMPLLKISHKSKKRILFWIDPSCFKFSWRMANSTTTTTSATTSATTSGLPQGITNTTALSNSAIISTPAIATSAIHRLSITNRTTHEFVLDDIKSIYIQNEGSGYREELNISQKLEKNWITIIYFNHKKNSLKSLHLITDNDHDFKKLISAIYNLKQLRSQLAKEFLIDLNELDENYVKMLLNKELLAGDNGNVDGNEVDIQKSHKHVREFLSFNDILKYSKRLNINVNTNHLQQIFDQVLLLSSATTEKPVSTPLFEKGLNFEQFKQFVSILKDRKDLQEIWDSLAQGKEVLQFDEIKNFIINIQKENFSDDDDNSTINLIFQKYCSNDNGWNKESLNEYLLSSYSTPYREITQTQTNYYDYPLNEYFISSSHNTYLTGRQVAGDSSVEGYIRTLQRGCRCVEIDIWNGDSNTTTTTVIGTKDDDDKNEYEPIVNHGRTFTKPISFANVIRAIKKFAFIVSPWPLILSLEIHCSPECQIKVVNILKDILGENMIIAPIDIDSVILPSPAELKHKFIIKVKKTTSFQNLIETENGSFTTSTTTTTTTTTTTTTTATSLSEDNENNKSNSSSTSSFIIRRRKNKSPKIINELSNLGIYTQGIKFRNFSLPESKTFNHCFSLGEKSINRMIKDDDKKISLDKHNRRYLMRVYPSGTRLKSSNFNPLPYWSHGVQMVATNWQTYDLGQQLNEALFENKIFQGYVLKPSVLRKPTLKSSSSNVDTRTSLTTTNSKTIRFNFEIISGHQLPKFPKDDYKDQAINPYISFEIIGAQDVQWDNNDSSPIAPTTSSSPFIRTTKIIRENGFNPNFNTKFSGSIITTTNDLIFIKFVVYASTSLNYPDYGENFPIAILVTKLNYLKQGYRYIYLNDLLGEQLVYSSIFIKIEYDEDLLNEFINK
Protein: Eukaryotic translation elongation factor 1 delta (E9PN71)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSGKASCTLETVWEDKHKYEEAERRFYEHEATQAAASAQQLPAEGPAMNGPGQDDPEDADEAEAPDGGSRRDPRKSQDSRKPLQKKRKRSPKSGLGPADLALLGLSAERVWLDKSLFDQAESSYRQKLADVAAQAAWPPALAPWGLCTHGNQVACHHVTWGIWVNKSSFDQAERAFVEWSQALLLAPDG
Protein: C2H2-type domain-containing protein (Q5AI92)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MSNPNESEPHTQPEINNASHIVKPEGSQTVNTGFICRWSDCTENTYNNLTSLVNHLNSKHIAQLPPGSNTKYICYWENCARYGLDQPSRFALISHCRTHTGEKPYFCPVPECEKHFTRSDALTKHVKAVHDLHSVKDQLNLLKDKARKGQIELGVNVEDLSEEDYLRIIEQDYEIQKPWWFTNEFLDVIRAGETDKLEEHNKDDDLDKQLEALPFDLKQYQLANSRYKQFINSLTSARASNEIEDEDEVDGLIPRSDDNNSVINVVRKQLQHEKPNKKFPRVMSNPVLERLSNDTKKLAHDYIRHENDQNDDDIDKISDLETLKTLHDKLANQLNTAYKINKVLANQLTSNIKMKRKLWVYTQLLMDANIQVGLPPEATSAPQRVMQDEYDEELLRG
Protein: Probable galacturonosyltransferase 10 (EC 2.4.1.-) (Like glycosyl transferase 4) (Q9SKT6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in pectin and/or xylans biosynthesis in cell walls.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- AT4g38500/F20M13_60
- AT5g42660/MJB21_3
- Alkaline-phosphatase-like family protein
- Probable LRR receptor-like serine/threonine-protein kinase At1g63430
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Transmembrane protein
- Transmembrane protein
- RING-type E3 ubiquitin transferase
- Receptor-like serine/threonine-protein kinase NCRK
- Putative DNA-binding protein At1g48610
Sequence:
MRRRGGDSFRRAGRRKISNVVWWVLSGIALLLFFLILSKAGHIEPRPSIPKRRYRNDKFVEGMNMTEEMLSPTSVARQVNDQIALAKAFVVIAKESKNLQFAWDLSAQIRNSQLLLSSAATRRSPLTVLESESTIRDMAVLLYQAQQLHYDSATMIMRLKASIQALEEQMSSVSEKSSKYGQIAAEEVPKSLYCLGVRLTTEWFQNLDLQRTLKERSRVDSKLTDNSLYHFCVFSDNIIATSVVVNSTALNSKAPEKVVFHLVTNEINYAAMKAWFAINMDNLRGVTVEVQKFEDFSWLNASYVPVLKQLQDSDTQSYYFSGHNDDGRTPIKFRNPKYLSMLNHLRFYIPEVFPALKKVVFLDDDVVVQKDLSSLFSIDLNKNVNGAVETCMETFHRYHKYLNYSHPLIRSHFDPDACGWAFGMNVFDLVEWRKRNVTGIYHYWQEKNVDRTLWKLGTLPPGLLTFYGLTEALEASWHILGLGYTNVDARVIEKGAVLHFNGNLKPWLKIGIEKYKPLWERYVDYTSPFMQQCNFH
Protein: LD16058p (Ribbon) (Ribbon, isoform B) (Q7KF43)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00320}.
Interaction partners:
Sequence:
MGGPTAPVASSGEVGQTYCLRWNNHQTNLVQILHALHEVGSYVDCSLVVDDEQFQAHRVVLAANSPYFQHILKDVPQDHCSIILPGVKGFEIAALLQYMYTGETTVTKSQEPEILRTAKELQVKGLYDNLMKFNHASVTPTSSSGAGGAKPQNGSASNHSSSVISTSTHISPSAAISSSCSPPPPPQFGYQPGYSHYPQQQPMSASQIPAGEAPLTPTQATPHSAASGAGEAGGQWPLTPSAAAAMLNSVYESAADMNPLKRKKLSAISSMLLSGNRDTPILRNVLAQANPADSSQPGPMNANGEKTPTHPHQNTQLPAGLGVSGGERNHSFNGSDYGGDKEPLSPYTDRSFEEETGQSGGKKPEWKRYKQYTRADMMCAIQAVREGMSALQASRKYGLPSRTLYDKVRKLNITTGRGTHRTPKRSPPGAESSQGFSYSAAAAAAAHNYGHGHGHHSEVKRDQKVDHVPAHHGMPPTIPPSAAALLDHAFLQQALENRGGDMAGREALHAMALAAAAHAAANRLSSSPAEMDQRSNGHGMRSPSPQGRHYPHEQEAMDLEMEKHEQNIIKRERDQDEREDADDEEDHEQEHVEDLSLARKERPPSPYSPQPTEAGAGVIMHASSASANGKDHVDYPSSPQFVPIGLKRELMEGEDAQARAD
Protein: Sperm equatorial segment protein 1 (SP-ESP) (Equatorial segment protein) (ESP) (Glycosylated 38 kDa sperm protein C-7/8) (Q6UW49)
Organism: Homo sapiens (Human)
Function: Involved in fertilization ability of sperm.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:12773409}. Note=Small proacrosomal granules (during the Golgi phase), enlarged acrosomal vesicles (during the cap phase), acrosome (during the elongating phase), equatorial segment of the acrosome (during the maturation phase) (PubMed:12773409). After acrosome reaction localizes to the equatorial segment region in both noncapacitated and capacitated, acrosome-reacted sperm (By similarity). {ECO:0000250|UniProtKB:Q9D5A0, ECO:0000269|PubMed:12773409}.
Interaction partners:
Sequence:
MKPLVLLVALLLWPSSVPAYPSITVTPDEEQNLNHYIQVLENLVRSVPSGEPGREKKSNSPKHVYSIASKGSKFKELVTHGDASTENDVLTNPISEETTTFPTGGFTPEIGKKKHTESTPFWSIKPNNVSIVLHAEEPYIENEEPEPEPEPAAKQTEAPRMLPVVTESSTSPYVTSYKSPVTTLDKSTGIGISTESEDVPQLSGETAIEKPEEFGKHPESWNNDDILKKILDINSQVQQALLSDTSNPAYREDIEASKDHLKRSLALAAAAEHKLKTMYKSQLLPVGRTSNKIDDIETVINMLCNSRSKLYEYLDIKCVPPEMREKAATVFNTLKNMCRSRRVTALLKVY
Protein: Acyl-CoA desaturase 1 (EC 1.14.19.1) (Delta(9)-desaturase 1) (Delta-9 desaturase 1) (Fatty acid desaturase 1) (Stearoyl-CoA desaturase 1) (P07308)
Organism: Rattus norvegicus (Rat)
Function: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates. Catalyzes the insertion of a cis double bond at the Delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA. Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids. Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides. Required for normal development of sebaceous glands. Required for the biosynthesis of normal levels of Delta-9 unsaturated fatty acids and 1-alkyl-2,3-diacylglycerol in the Harderian gland. Required for normal production of meibum, an oily material that prevents drying of the cornea (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00767}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000269|PubMed:2892838}; Multi-pass membrane protein {ECO:0000269|PubMed:2892838}.
Interaction partners:
- Fatty acid synthase
- Sterol regulatory element-binding protein 1
- Diacylglycerol O-acyltransferase 2
- Acetyl-CoA carboxylase 1
- Cytochrome b5 type B
- Cytochrome b5
- Very long chain fatty acid elongase 6
- ATP-citrate synthase
- Diacylglycerol O-acyltransferase 1
- Peroxisome proliferator-activated receptor alpha
Sequence:
MPAHMLQEISSSYTTTTTITEPPSGNLQNGREKMKKVPLYLEEDIRPEMREDIHDPSYQDEEGPPPKLEYVWRNIILMALLHVGALYGITLIPSSKVYTLLWGIFYYLISALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGGKLDMSDLKAEKLVMFQRRYYKPGLLLMCFILPTLVPWYCWGETFLHSLFVSTFLRYTLVLNATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHAFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAVLARIKRTGDGSHKSS
Protein: Secreted protein P60-related protein (P71594)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized HTH-type transcriptional regulator Rv0023
- Possible penicillin-binding lipoprotein
- Uncharacterized protein Rv0025
Sequence:
MNYSEVELLSRAHQLFAGDSRRPGLDAGTTPYGDLLSRAADLNVGAGQRRYQLAVDHSRAALLSAARTDAAAGAVITGAQRDRAWARRSTGTVLDEARSDTTVTAVMPIAQREAIRRRVARLRAQRAHVLTARRRARRHLAALRALRYRVAHGPGVALAKLRLPSPSGRAGIAVHAALSRLGRPYVWGATGPNQFDCSGLVQWAYAQAGVHLDRTTYQQINEGIPVPRSQVRPGDLVFPHPGHVQLAIGNNLVVEAPHAGASVRVSSLGNNVQIRRPLSGR
Protein: Condensin-2 complex subunit H2 (Non-SMC condensin II complex subunit H2) (A0A0A6YYG7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEDVEARFAHLLQPIRDLTKNWEVDVAAQLGEYLEELDQICISFDEGKTTMNFIEAALLIQGSACVYSKKVEYLYSLVYQALDFISGKRRAKQLSSVQEDRANGVASSGVPQEAENEFLSLDDFPDSRTNVDLKNDQTPSEVLIIPLLPMALVAPDEMEKNNNPLYSRQGEVLASRKDFRMNTCVPHPRGAFMLEPEGMSPMEPAGVSPMPGTQKDTGRTEEQPMEVSVCRSPVPALGFSQEPGPSPEGPMPLGGGEDEDAEEAVELPEASAPKAALEPKESRSPQQSAALPRRYMLREREGAPEPASCVKETPDPWQSLDPFDSLESKPFKKGRPYSVPPCVEEALGQKRKRKGAAKLQDFHQWYLAAYADHADSRRLRRKGPSFADMEVLYWTHVKEQLETLRKLQRREVAEQWLRPAEEDHLEDSLEDLGAADDFLEPEEYMEPEGADPREAADLDAVPMSLSYEELVRRNVELFIATSQKFVQETELSQRIRDWEDTVQPLLQEQEQHVPFDIHTYGDQLVSRFPQLNEWCPFAELVAGQPAFEVCRSMLASLQLVSSLGYVGGGDGPQTLLMCHPCRPMTTQWR
Protein: MIP04739p (Q9VUU8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Meru, isoform A
Sequence:
MARGHQKIQSQAKASEKQAKLKKQQGHSANDQKKAAQKALVYVCAVCKSQMPDPKTYKQHFENKHPKNDIPEELKEV
Protein: EMBRYO SURROUNDING FACTOR 1-like protein 8 (A8MR88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- EMBRYO SURROUNDING FACTOR 1-like protein 10
- EMBRYO SURROUNDING FACTOR 1.2
- EMBRYO SURROUNDING FACTOR 1.3
- EMBRYO SURROUNDING FACTOR 1.1
- GDSL esterase/lipase EXL4
- GDSL esterase/lipase EXL5
- Probable inactive peroxygenase-like protein
- Probable peroxygenase 7
- Tapetal oleosin GRP-16
- Oleosin family protein
Sequence:
MSSSQFFILCIILISSFPLHECENGKSVEASNAAKTLCMSVNCDNKDRNLTCACCLAKSKNRCYSSKSECVADCKD
Protein: Pyridoxal kinase (EC 2.7.1.35) (Pyridoxine kinase) (Q55EK9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Required for synthesis of pyridoxal-5-phosphate from vitamin B6.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Pyridoxine-5'-phosphate oxidase
- Probable pyridoxal 5'-phosphate synthase subunit pdx2
- Probable pyridoxal 5'-phosphate synthase subunit pdx1
- Proliferating cell nuclear antigen
- Pyridoxal phosphate homeostasis protein
- 2Fe-2S ferredoxin-type domain-containing protein
- Metalloenzyme domain-containing protein
Sequence:
MEPKVLSIQSWVCHGYVGNKCAVFALQHLGIEVDPINSVHLSNNTAYPTWKGESLTPNKLGDLFQGLEDNHLTSNYTHVLTGYNNSVQTLHTVLKIVKKLKSENPNLIYVCDPVLGDNNELYVPEDLVEVYKNEVIPNADYIFPNQTEVEFLTGIKIKNDQDALKAIDQFHKMGVKNVVITSLFFDTNPNDIIVIGSTINDDDNNNKYNQFKIKVGPKFNDYYTGTGDLLSSLLLGWSIREPTDLSLVCEKAISILYNIINETHNSKKSIPSNKEKQYYELRLVQSRKFIENSEIRFKSEKL
Protein: Chromodomain helicase DNA binding protein 9 (H3BSP3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTDPMMDFFDDANLFGETLEGLSDDAFVQPGPVSLVDELNLGAEFEPLHIDSLNHVQGTPTHQKMTDFEQLNQFDSIKFHHVNQSFGSPAEHVLSPHSQFNCSPIHPQNQPNGLFPDVSDGSPMWGHQTATTISNQNGSPFHQQGHSHSMHQNKSFVAHHDFALFQANEQQTQCTSLRSQQNRNNLNPGQNSLSQSKNFMNVSGPHRVNVNHPPQMTNASNSQQSISMQQFSQTSNPSAHFHKCSSHQEGNFNGPSPNMTSCSVSNSQQFSSHYSFSSNHISPNSLLQSSAVLASNHTNQTLSDFTGSNSFSPHRGIKQESTQHILNPNTSLNSNNFQILHSSHPQGNYSNSKLSPVHMNFPDPVDSGTQMGHFNDHVETNGFSSLEENLLHQVESQTEPFTGLDPEDLLQEGLLPHFDESTFGQDNSSHILDHDLDRQFTSHLVTRPSDMAQTQLQSQARSWHSSFSNHQHLHDRNHLCLQRQPPSSKKSDGSGTYTKLQNTQVRVMSEKKQRKKVESESKQEKANRIISEAIAKAKERGERNIPRVMSPENFPTASVEGKEEKKGRRMKSKPKDKDSKKTKTCSKLKEKTKIGKLIITLGKKQKRKNESSDEISDAEQMPQHTLKDQDSQ
Protein: ABC transporter G family member 16 (ABC transporter ABCG.16) (Q54HM0)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MKLTNSISPTNLDGEINKNSQPSNDNQQQQQPKINKIINKFSESINSVSKTIGKGIGDLTSSNALDEHIKNHNSNFIDPFYNEEAVVVVDDENIRSLIGDNCSSIGNIGVNGIEAFYGEHNNKKSELIKQFLKINSTNNKSNQTIVVDHMDYSVMERQSSSSSSSSSRSTGVSKLIPFLKRKEKIEILKDLSFYLKPGMMVLLLSEAGSGVSTLFKCLTNRIPKRGSINGDILFDNEPIDGESHHSQYLFVQQSDHHISTLTVKETLEFSIECQSNLSREAKKQLSSNILSILGISHVADTYIGNQSIRGISGGQKKRMTVAVELVKGAKAIMIDQATNGLDSTSAFELLNSIQMISKVSNVPALVSLLQPSPEIFSLFSHILMMKDGEITFFGEKHQIFDHFSDYGLECKDKQNPAEFLSSIYHQAQLDPDCQLKSSSDFIVAYKQSQYYKDCLIKISQERLSNHKFSGDKSIKIIENEKEQQQQEIYQLSLIKQIQLNLKRAFLTTIRDRASILSRVIKSSLLGLLIGTLFFQLDSSQKSANLLPSLSFFLLTFVVFGSLAGVGQVFSERPVFYDQKIGKYYKSIAYFFAGLVSDLIWNFIDVIIFCSISYWLIGLNHSADRFFFFLLAIYLLDCLVNRVSKMVSIYSPNAAIASTIAPLYFSLFLLMAGYLIHRNSIPIYWRWMHYISPFKWVFEAILSNQLHGQTFTCKSDELLPPIGYPLLNVSFPDGYSGSQVCPIIDGIEILKSKDINSDYSYKYYSVWIILSMYLLFSILSIIGLSNITFDNIISNKEKNNGNGNNNYNGKESINEESIKLSIKQHQQKQFESNEKCYLTFKNLTYKVLIKKKNHQKVSRTLLHDINGYVKPGSMVALIGSSGAGKSTLLDILANRKDQGIISGEILLNGKARDKCFNRYVAYVEQEDTLPDFQTVREAITFSALLRLPNDTMTHQDKLDTVDYILDVLELNSIANTLIGKVDHGITQEQRKRVNIAIEMASLPDILFLDEPTTGLTSVAAELIMQLIKRVALDGRSVICTIHQPSETIFKKFDSILLLTQGGFVAYFGELGPNCRTVLNYCSDLGFNCPQGKNPADFLLDFSASFNSASRLASNDKMIPSIRSRIKNVGNYCFDGSSNLNNKNEIKQQQTTTQNVNLGNEDKQQQQQEEANDDNNIQEATSSNSNNNNNNDIIDNYQFSNLNRDTIEIIDSGLPIGFISKTFKEKNATSFLFQFFMLLFRFFVCAIRRRNLIMTRIIRSILLSVVTGTLYLQLKNDQDGVMDRISFIFFTSTFASISCLSNIPTVFEDRFLFYHELNSNTYRHLSYILAMILADLPFTIMYSLLFSAPIYWIVGLQNDVDKFLFFIFVYYLYLQVLVSFSQLLGMVSPTLATANEITGISFSVFSLFAGFIIKKDDIPSYYKWLNYVSITRYLVEPLTVNEMTGSVSFHCEPHQLIPVPIHYTPTNATASEPTKLVFKSFCPITQGNQVLYQFDINDTDKFEDTFVLIGLFIGFLLLILIFSKILKFKK
Protein: Inhibin beta B chain (Activin beta-B chain) (P27093)
Organism: Gallus gallus (Chicken)
Function: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, erythroid differentiation, insulin secretion, nerve cell survival, embryonic axial development or bone growth, depending on their subunit composition. Inhibins appear to oppose the functions of activins.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Follistatin
- Activin receptor type-2A
- Activin receptor type-2B
- Inhibin beta A chain
- Receptor protein serine/threonine kinase
- Activin receptor type-1
- receptor protein serine/threonine kinase
- Bone morphogenetic protein receptor type-1B
- Transforming growth factor beta-3 proprotein
- Inhibin subunit beta C.
Sequence:
MDGAARRGVLAALLACGLLLLGAAATPTPPPAGSSPQDTCTSCGFRRPEEPGKVDGDFLEAVKRHILSRLQMRDRPNITHAVPKAAMVTALRKLHAGKVREDGRVEIPSLDGQASAGPPAHDPVSEIISFAETDDLASSRVRLYFFISNEGNQNLFVVQASLWLYLKLLPYVLEKGSRRKVRVKVYFQDPDTSNKWNVVEKKVDLKRSGWHTFPMTEAIQALFERGERRLNLDVQCEGCEEYSVLPIYVDPGEESHRPFLVVQARLADNKHRIRKRGLECDGRTNLCCRQQFYIDFRLIGWNDWIIAPSGYYGNYCEGSCPAYLAGVPGSASSFHTAVVNQYRMRGLNPGTVNSCCIPTKLSTMSMLYFDDEYNIVKRDVPNMIVEECGCA
Protein: Heat stress transcription factor A-6b (AtHsfA6b) (AtHsf-07) (Q9LUH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator that specifically binds DNA sequence 5'-AGAAnnTTCT-3' known as heat shock promoter elements (HSE).
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- Dehydration-responsive element-binding protein 2A
- Heat shock 70 kDa protein 4
- Probable methyltransferase PMT19
Sequence:
MDPSFRFIKEEFPAGFSDSPSPPSSSSYLYSSSMAEAAINDPTTLSYPQPLEGLHESGPPPFLTKTYDLVEDSRTNHVVSWSKSNNSFIVWDPQAFSVTLLPRFFKHNNFSSFVRQLNTYGFRKVNPDRWEFANEGFLRGQKHLLKNIRRRKTSNNSNQMQQPQSSEQQSLDNFCIEVGRYGLDGEMDSLRRDKQVLMMELVRLRQQQQSTKMYLTLIEEKLKKTESKQKQMMSFLARAMQNPDFIQQLVEQKEKRKEIEEAISKKRQRPIDQGKRNVEDYGDESGYGNDVAASSSALIGMSQEYTYGNMSEFEMSELDKLAMHIQGLGDNSSAREEVLNVEKGNDEEEVEDQQQGYHKENNEIYGEGFWEDLLNEGQNFDFEGDQENVDVLIQQLGYLGSSSHTN
Protein: Autophagy-related protein (F4HX35)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MANSSFKLEHPLERRQIESSRIREKYPDRIPVIVERAERSDVPNIDKKKYLVPADLTVGQFVYVVRKRIKLSAEKAIFVFVKNTLPPTGKHTTS
Protein: Tropomyosin alpha-1 chain (Alpha-tropomyosin) (Tropomyosin-1) (P04692)
Organism: Rattus norvegicus (Rat)
Function: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7568216}. Note=Associates with F-actin stress fibers (PubMed:7568216). {ECO:0000269|PubMed:7568216}.
Interaction partners:
- Troponin T, cardiac muscle
- Troponin I, cardiac muscle
- Actin, alpha cardiac muscle 1
- Myosin light chain 1/3, skeletal muscle isoform
- Troponin T, fast skeletal muscle
- Myosin-6
- Myosin regulatory light chain 11
- Troponin T, slow skeletal muscle
- Myosin light chain 3
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
Sequence:
MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
Protein: Succinate dehydrogenase subunit 8, mitochondrial (Q9SKE0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Succinate dehydrogenase subunit 7A
- Succinate dehydrogenase subunit 7B
- Succinate dehydrogenase subunit 5
- Succinate dehydrogenase subunit 4
- Succinate dehydrogenase subunit 6
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Succinate dehydrogenase subunit 3-2
- Succinate dehydrogenase subunit 3-1
Sequence:
MIYRKWSLLSGPPVILGGAVIAAVAVGFVLQNVTKGEQKKNVSTNK
Protein: Frequenin-2 (Q9VWX8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25074811}.
Interaction partners:
- Phosphatidylinositol 4-kinase beta
- Protein cycle
- Chaperone Ric-8
Sequence:
MGKKNSKLKQDTIDRLTTDTYFTEKEIRQWHKGFLKDCPNGLLTEQGFIKIYKQFFPDGDPSKFASLVFRVFDENNDGAIEFEEFIRALSITSRGNLDEKLHWAFRLYDVDNDGYITREEMYNIVDAIYQMVGQQPQTEDENTPQKRVDKIFDQMDKNHDDRLTLEEFREGSKADPRIVQALSLGGD