wanglab/gogpt-training-data huggingface dataset:
Protein: Radish, isoform N (Q9I7S4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MECSDFMQQLRSFKPQSLGCAVARRKSSTTLIFPLPPQACSDEFCEEYPHNLMPTPGYWIECSRQKITMPTPHTIWDESDSEHEDIRAGSASDAYLERECSDLYEDDEDSEATPSPRKKTTIEEQWDQQGAFELISVEQETYEKYFYGTEHWNYFTSDEDLGPVILSIKQETLNGRDQFRILVRAGSYTVHGLIPASCVFADRYNREEVVRSLGKEVNLNPPLTLGQLPDTPEELLKLDQVFIKSELKVGVIFVKEDQYTEEQILDNNENSPLFDEFLTLLGDRVRLRGFDKYKGGLDTVHDLTGLFSVYTNWRNIEIMFHVSTLLPYEKHDPQKLQRKRHIGNDIVCVVFLEADNTRFSPACIKSHFLHTFILVRVSARIKHKPTRYEVSVVTRDEVGAYKPYLWEQSVFEKGPMFREWLLTKIVNGERASYSAPKFARMQERTRSQMLEDLVMNLSNHAETGQIPKPYRRGSWRPIGEDEYIKMLHARVLDNNTHHEQQQQLLLQQQHMQHTQHMQHLPSHNICCYCNNNATELHTAGAIHNNNDNNNTTTTTTFTHRHNNNNNNYSEQQQQQLPQQQQHDSQQQQQLLQPQQHQLLHQLQLSTSSLTHTSCCAMLHLCARHSHMRPSSPLLDSVRDQFEDYDQLAKDFTRVFLNEEPSCLTNAHLFDVVFLVGQSKQKARFIGVRAILGVRSRVFQEMLYGIQTGFGSPQIPVAEIFARPAPSLVSPQNQKPKSNNYLTVPDSDSIRPKSVPSSPMVKRAFSRLGTITAGWGRSIRNKNTNQLNPDDKKKWISSTDCSNRDSKDKDKDKPGNNQLAVPRLSVCADAQKVDRAKLAQTEFNIIEFDPDTFRVLLDYLHTGTCPLTCVSIPGLLCAAEHYDLPELLQACFHHCKQFLRIEVVCPMLISLENYYWRYTSASELVNMILSFVESKAHSLFKCPEFLHLSESMVQMIMCRELQTPEIRKFEAMLAWAQHKVGKLKNHPNKDTQFEFECIMERLTRDLNLCRISPSELLTVVLPSKSMKNERIMETLMVQVNLGTYRMPELDAYRQQLRQQESAEATVQVHRAHQNHHNPPPIDARAYAMASLAAALEMQNSSNPLQSNAARDAADEEVELYASFDNAPSTSRVAAQMQAAKEARRKRWAADGASGSSGDGGCASGSSGSGRRY
Protein: Four and a half LIM domains protein 2 (FHL-2) (Skeletal muscle LIM-protein 3) (SLIM-3) (O70433)
Organism: Mus musculus (Mouse)
Function: May function as a molecular transmitter linking various signaling pathways to transcriptional regulation. Negatively regulates the transcriptional repressor E4F1 and may function in cell growth. Inhibits the transcriptional activity of FOXO1 and its apoptotic function by enhancing the interaction of FOXO1 with SIRT1 and FOXO1 deacetylation (By similarity). Negatively regulates the calcineurin/NFAT signaling pathway in cardiomyocytes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q14192}. Nucleus {ECO:0000269|PubMed:20013826}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:22851699}.
Interaction partners:
- Catenin beta-1
- Lymphoid enhancer-binding factor 1
- TNF receptor-associated factor 6
- Titin
- TNF receptor-associated factor 2
- Epidermal growth factor receptor
- Ankyrin repeat domain-containing protein 1
Sequence:
MTERFDCHHCNESLYGKKYILKEENPHCVACFEELYANTCEECGTPIGCDCKDLSYKDRHWHEGCFHCSRCGSSLVDKPFAAKEEQLLCTDCYSNEYSSKCQECKKTIMPGTRKMEYKGSSWHETCFTCQRCQQPIGTKSFIPKENQNFCVPCYEKQYALQCVQCKKPITTGGVTYREQPWHKECFVCTACKKQLSGQRFTARDEFPYCLTCFCDLYAKKCAGCTNPISGLGGTKYISFEERQWHNDCFNCKKCSLSLVGRGFLTERDDILCPDCGKDI
Protein: Formyltransferase/hydrolase complex Fhc subunit C (C5B135)
Organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens)
Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Formyltransferase/hydrolase complex subunit D
- Formyltransferase/hydrolase complex Fhc subunit A
- Formyltransferase/hydrolase complex Fhc subunit B
- Methenyltetrahydromethanopterin cyclohydrolase
- NAD
- Tetrahydromethanopterin C1 transfer protein
- Ribofuranosylaminobenzene 5'-phosphate
- Etrahydromethanopterin-linked formaldehyde oxidation protein
- Formamidase
- 
Sequence:
MSTLRLRGDLPERVDLLNITPLALSGLSEAEAGKLAIGTSRRGLTLGDVFEISLDGSDSLVIEGGSARLDRVGAALSQGSIRVEGDVGQRLGEGMAAGSLTVTGSAGPYAGTGATGGTITIEGDAGDHAGGAVYAAKAGLDGATLVIKGAAGDHLGDRMRRGMILAGSAGAFAASRMIAGTIVVSGALGDHPGYGMRRGTLIAGSHGTLLPTFVETGTPDLVFVRLLAQSLKHLGAAQASLLSGTLRRYSGDLATLGKGELFVPA
Protein: Cardiotrophin-like cytokine factor 1 (B-cell-stimulating factor 3) (BSF-3) (Novel neurotrophin-1) (NNT-1) (Q9QZM3)
Organism: Mus musculus (Mouse)
Function: In complex with CRLF1, forms a heterodimeric neurotropic cytokine that plays a crucial role during neuronal development (By similarity). Also stimulates B-cells. Binds to and activates the ILST/gp130 receptor.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Cytokine receptor-like factor 1
- Ciliary neurotrophic factor receptor subunit alpha
- Leukemia inhibitory factor receptor
- Interleukin-6 receptor subunit beta
- Ciliary neurotrophic factor
- Cardiotrophin-1
Sequence:
MDLRAGDSWGMLACLCTVLWHLPAVPALNRTGDPGPGPSIQKTYDLTRYLEHQLRSLAGTYLNYLGPPFNEPDFNPPRLGAETLPRATVNLEVWRSLNDRLRLTQNYEAYSHLLCYLRGLNRQAATAELRRSLAHFCTSLQGLLGSIAGVMATLGYPLPQPLPGTEPAWAPGPAHSDFLQKMDDFWLLKELQTWLWRSAKDFNRLKKKMQPPAASVTLHLEAHGF
Protein: Bifunctional riboflavin kinase/FMN adenylyltransferase (Riboflavin biosynthesis protein RibF) [Includes: Riboflavin kinase (EC 2.7.1.26) (Flavokinase); FMN adenylyltransferase (EC 2.7.7.2) (FAD pyrophosphorylase) (FAD synthase)] (P0AG40)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Interaction partners:
- Riboflavin synthase
- 6,7-dimethyl-8-ribityllumazine synthase
- tRNA pseudouridine synthase B
- Riboflavin biosynthesis protein RibD
- 5-amino-6-
- Isoleucine--tRNA ligase
- 5-amino-6-
- Uncharacterized protein YaaY
- Cytidylate kinase
- FMN reductase
Sequence:
MKLIRGIHNLSQAPQEGCVLTIGNFDGVHRGHRALLQGLQEEGRKRNLPVMVMLFEPQPLELFATDKAPARLTRLREKLRYLAECGVDYVLCVRFDRRFAALTAQNFISDLLVKHLRVKFLAVGDDFRFGAGREGDFLLLQKAGMEYGFDITSTQTFCEGGVRISSTAVRQALADDNLALAESLLGHPFAISGRVVHGDELGRTIGFPTANVPLRRQVSPVKGVYAVEVLGLGEKPLPGVANIGTRPTVAGIRQQLEVHLLDVAMDLYGRHIQVVLRKKIRNEQRFASLDELKAQIARDELTAREFFGLTKPA
Protein: Lactoperoxidase (LPO) (EC 1.11.1.7) (Q5SW46)
Organism: Mus musculus (Mouse)
Function: Heme-containing oxidoreductase which catalyzes the conversion of thiocyanate (SCN(-)) into antimicrobial agent hypothiocyanous acid (OSCN(-)) in the presence of hydrogen peroxide (H2O2) (By similarity). Also involved in the conversion of iodide (I(-)) into hypoiodite (IO(-)) in the presence of H2O2 (By similarity). Responsible for the inactivation of a wide range of micro-organisms and hence, important component of defense mechanism (By similarity). May be implicated in airway host defense against infection (By similarity). May contribute to maintaining an appropriate H2O2 cellular level, therefore protecting cells from H2O2-caused injuries and inflammation.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P22079}. Cytoplasm {ECO:0000269|PubMed:22343415}. Note=Expressed in the cytoplasm in intestinal epithelial cells. {ECO:0000269|PubMed:22343415}.
Interaction partners:
- Alpha-lactalbumin
- Lactotransferrin
Sequence:
MKVLLHLPALLASLTLLQTAASASDDPTAETDIIHDTVEEVKVWVNKAFLDSRDRLKMAMTTKIHSTRHLSDYLKHAKGRTRTAIRSGQVWEESLKKLSQFLTNVTGQGLDLTLLSWEAGCDPPAPTMTCNISSPYRTITGYCNNRKNPALGSANRALARWLPAEYEDGLSLPYGWTPGKMRNGFPLPQPREVSNQIAAYLNEEDVLDQKRSMLFMQWGQIVDHDMDFAPETEMGSDTYTKAQCDEHCIQGDNCFPIMFPPGDPKLKTQGKCMPFFRAGFVCPTPPYKSLAREQINALTSFLDASLVYSPEPSLANRLRNLSSPLGLMAVNEEVSDNGRPFPPFVKMKPSPCEVINATAGVPCFLAGDSRASEQILLATSHTLFIREHNRLATELSRLNPHWDRETLYQEARKIMGAFIQITTFRDYLPILLGDEMQKWIPPYQGYNESVDPRISNVFTFALRFGHLEIPSTVYRLDENYQPWGSESELPLHTVFFNTWRLVKDGGIDPLVRGLLAKNAKLMHQNKMMTGELRNKLFQPNHTIHGFDLASINIQRSRDHGQPGYNSWRAFCGLSQPKTLEELSAVMKNEVLAKKLMDLYGTPSNIDIWLGAVAEPLVHRGRVGPLLTCLLGQQFQRIRDGDRFWWENPGVFTEKQRESLQKMSFSRLVCDNTGIDKVPLNPFQANAYPHGFVDCSSIDKLDLSPWASVKE
Protein: NRR repressor homolog 3 (B7F924)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Binds to and represses NPR1/NH1-mediated transcriptional activation of LG2 in vitro.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5ZEF1}.
Interaction partners:
Sequence:
MDPTMPTPHTISGTSPFPRNSSTAAEMIVTEQEHLQPRHRRSRKRDRPPPTPPSGNIKAAPAPLPEGGGHGHEEEARDEDVDRFYALLDEVREMRELWRRNGDCVATKRTSVDGGQKKQDRQQLWRPTFVMEDFAFELKGSQVVQPEKKVDSAPNLDLSLSM
Protein: Telomere repeat-binding protein 2 (Protein TRF-LIKE 1) (Q9SNB9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds specifically to the plant telomeric double-stranded DNA sequences. At least 2 repeats of telomeric sequences are required for binding. Induces DNA bending.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Protein ALWAYS EARLY 2
- Tryptophan synthase beta chain 1, chloroplastic
- Paired amphipathic helix protein Sin3-like 4
- Tryptophan synthase
- Carbamoyl phosphate synthase small chain, chloroplastic
- Amidase 1
- Aromatic aminotransferase ISS1
- Armadillo repeat only 2
- Tryptophan synthase alpha chain, chloroplastic
Sequence:
MVSHKVLEFGDDGYKLPAQARAPRSLRKKRIYEKKIPGDDKMCAIDLLATVAGSLLLESKSPVNACLVVQNTVKNEYPADENPVKAVPYSESPSLFDNGKCGFSSVITNPNHLLVGDKVGKEVEGFSSLGVSGDVKPDVVASIGSNSSTEVGACGNGSPNESRDDVNLFSRNDDDENFSGYIRTRMTRPVPRIGDRRIRKILASRHWKGGSKNNTDAKPWYCSKRSYYLHHHQRSYPIKKRKYFDSVYDSNSDDYRLQGKTHKGSRTISSMKSRNASFVSRDHHVKLRIKSFRVPELFVEIPETATVGSLKRMVMEAVTTILGDGLRVGLMVQGKKVRDDGKTLLQTGISEENNHLDSLGFSLEPSLETTPQPLLSSYLSDHACDDVTLCHDNALDSSHEPEPSPADSFGKLGTSDHSRALIPVASAAMLAPRPPNRKFKRTEQQLAAQRRIRRPFSVTEVEALVQAVEKLGTGRWRDVKVRAFEDADHRTYVDLKDKWKTLVHTARISPQQRRGEPVPQELLDRVLKAHAYWSQHLMHQLQTEPPSTQVEAL
Protein: Putative tRNA pseudouridine synthase (EC 5.4.99.-) (tRNA pseudouridylate synthase) (tRNA-uridine isomerase) (O22928)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- tRNA
Sequence:
MAVSFLRIPIPSRVFWYPTRLIRVTPALLRFSSSAAFQPSSTSLSPPSSDNFLADKWESYRKKKVVIRIGYVGTDYRGLQIQRDDPSIKTIEGELEVAIYKAGGIRDSNYGDLHKIGWARSSRTDKGVHSLATSISLKMEIPETAWKDDPQGTVLAKCISKHLPENIRVFSVLPSNRRFDPRRECTLRKYSYLLPVDVLGIKNSFTSDEIDYHITDFNEILKEFEGEYPFHNYTQRSRYRRKSEQKIKQRNGRPPREPKSIKASESEFREENHIEIGEEEEEKEVDGESDEHVVTPDSDNSQVYSRAKWLYEPDETDKISGAHFRKVFRCRSGKLENSLGFGFVEISIWGESFMLHQIRKMIGTAVAVKRELLPRDIIRLSLNKFTRIVLPLAPSEVLILRGNSFEVRRLPERPGMEATGESEEVEKEIEEFYRAVMVPQVSIFLDSEKSPWKEWVDHLDRNDGLIDEELEDVRKGWEEWKAAKPWMNLKKTEDDEEALSSVSVPIHQAL
Protein: Uncharacterized transcriptional regulatory protein C3C7.04 (O14130)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
Interaction partners:
- MYND-type zinc finger protein C31F10.10c
- Uncharacterized transcriptional regulatory protein C320.03
- 5'-AMP-activated protein kinase subunit beta
Sequence:
MSHEFSPENTAVLFEAMKQEQHNRRRRVPMERRRRVVLACFNCKARKVRCDGANPCKACASNNLECTYPVKDEKEMDYSKDYFIDLSKRYKCLEYIVERLCSTKVSTYTTPSLIEVCNRISNQKSLLSSDVFSLNSESTNSQRDVDTLTQGALVCSQIQQDPTVVAEDTNNGINADASDQSVDEIMKLIGKIKVDSNGESRYIGASAGEAFVDSVQSELLVDPSFSELSAYSHTHHSYPPNEHDVNAVQKALSLLPPPEVSDFLIKSFYGHVQANFFFFHETLLRYRLNLIMSFQNPSVDPGFLCLLMMIFALGSMFAHMEIRSASNPFDNPGKQFFDTARLLLPQVIQQCKPSLVQASILMGLYLQSTLSQKSSYTYFGLSLSAAVANGLHRSCENPNIDPKTKELRNRLWWSVYTMDRLISIATGRPLSIADSECDAALPTVVPELEIEGSASNVHNIISMSKIAKIMGKTMEQLYGTVNYKKNPINIIESLRADLEEWKRSLPPFQILENLDAEDPLFRANVHLHMTYDQAIIIMSRPVLLHKMKNAKNSPRVDRINEDCILAARHLISLVHLLQNHSQLSCYSFFDYNYTFSSALVVLLHCVTEPCEEDDIAMQYAYSALDYMAEGNEAAKNCARVIRLFDAHLKGARSDGNGNTSQSGFMAWQRWIAEVSAKDEPEKLMSPYNKSIGGGRNSNSLTPNANLGADVSFFPTDDTSFLLDHSKLDDDLEKFASTLDPIKTTPDLANDSSLLNWANTDQGMDIEGSWLGNMHPTWLDYVCP
Protein: Contactin-2 (Axonal glycoprotein TAG-1) (Axonin-1) (Transient axonal glycoprotein 1) (TAX-1) (Q61330)
Organism: Mus musculus (Mouse)
Function: In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Attached to the neuronal membrane by a GPI-anchor and is also released from neurons. {ECO:0000250}.
Interaction partners:
- Contactin-associated protein-like 2
- Neural cell adhesion molecule L1
- Tax1-binding protein 1 homolog
- Potassium voltage-gated channel subfamily A member 1
- Neuronal cell adhesion molecule
- Contactin-associated protein 1
- Amyloid-beta precursor protein
- Potassium voltage-gated channel subfamily A member 2
- Neuropilin-1
- Leucine-rich glioma-inactivated protein 1
Sequence:
MGAPARKRASLLLLLLATMALVSSPGWSFSQGTPATFGPVFEEQPVGLLFPEESAEDQVTLACRARASPPATYRWKMNGTEMNLEPGSRHQLMGGNLVIMSPTKAQDAGVYQCLASNPVGTVVSKEAVLRFGFLQEFSKEERDPVKTHEGWGVMLPCNPPAHYPGLSYRWLLNEFPNFIPTDGRHFVSQTTGNLYIARTNASDLGNYSCLATSHLDFSTKSVFSKFAQLNLAAEDPRLFAPSIKARFPPETYALVGQQVTLECFAFGNPVPRIKWRKVDGSLSPQWGTAEPTLQIPSVSFEDEGTYECEAENSKGRDTVQGRIIVQAQPEWLKVISDTEADIGSNLRWGCAAAGKPRPMVRWLRNGEPLASQNRVEVLAGDLRFSKLNLEDSGMYQCVAENKHGTIYASAELAVQALAPDFRQNPVRRLIPAARGGEISIPCQPRAAPKATILWSKGTEILGNSTRVTVTLDGTLIIRNISRSDEGKYTCFAENFMGKANSTGILSVRDATKITLAPSSADINVGDNLTLQCHASHDPTMDLTFTWTLDDFPVDFDKPGGHYRRASVKETIGDLTILNAQLRHGGTYTCMAQTVVDGASKEATVLVRGPPGPPGGVVVRDIGDTTVQLSWSRGFDNHSPIAKYTLQARTPPSGKWKQVRTNPVNIEGNAETAQVLGLMPWMDYEFRVSASNILGTGEPSGPSSRIRTKEAVPSVAPSGLSGGGGAPGELTINWTPMSREYQNGDGFGYLLSFRRQGSSSWQTARVPGADTQYFVYSNDSIHPYTPFEVKIRSYNRRGDGPESLTAIVYSAEEEPKVAPAKVWAKGSSSSEMNVSWEPVLQDMNGILLGYEIRYWKAGDKEAAADRVRTAGLDSSARVTGLYPNTKYHVTVRAYNRAGTGPASPSADAMTMKPPPRRPPGNISWTFSSSSLSLKWDPVVPLRNESTVTGYKMLYQNDLQPTPMLHLTSKNWIEIPVPEDIGHALVQIRTTGPGGDGIPAEVHIVRNGGTSMMVESSAVRPAHPGPVFSCMVILMLAGCQRL
Protein: Tripartite motif-containing protein 6 (EC 2.3.2.27) (RING finger protein 89) (RING-type E3 ubiquitin transferase TRIM6) (Q9C030)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin ligase that plays a crucial role in the activation of the IKBKE-dependent branch of the type I interferon signaling pathway. In concert with the ubiquitin-conjugating E2 enzyme UBE2K, synthesizes unanchored 'Lys-48'-linked polyubiquitin chains that promote the oligomerization and autophosphorylation of IKBKE leading to stimulation of an antiviral response. Ubiquitinates also MYC and inhibits its transcription activation activity, maintaining the pluripotency of embryonic stem cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17156811, ECO:0000269|PubMed:24882218, ECO:0000269|PubMed:35263596}.
Interaction partners:
- T-cell receptor-associated transmembrane adapter 1
- Gamma-butyrobetaine dioxygenase
Sequence:
MTSPVLVDIREEVTCPICLELLTEPLSIDCGHSFCQACITPNGRESVIGQEGERSCPVCQTSYQPGNLRPNRHLANIVRRLREVVLGPGKQLKAVLCADHGEKLQLFCQEDGKVICWLCERSQEHRGHHTFLVEEVAQEYQEKFQESLKKLKNEEQEAEKLTAFIREKKTSWKNQMEPERCRIQTEFNQLRNILDRVEQRELKKLEQEEKKGLRIIEEAENDLVHQTQSLRELISDLERRCQGSTMELLQDVSDVTERSEFWTLRKPEALPTKLRSMFRAPDLKRMLRVCRELTDVQSYWVDVTLNPHTANLNLVLAKNRRQVRFVGAKVSGPSCLEKHYDCSVLGSQHFSSGKHYWEVDVAKKTAWILGVCSNSLGPTFSFNHFAQNHSAYSRYQPQSGYWVIGLQHNHEYRAYEDSSPSLLLSMTVPPRRVGVFLDYEAGTVSFYNVTNHGFPIYTFSKYYFPTTLCPYFNPCNCVIPMTLRRPSS
Protein: ATP synthase subunit alpha, mitochondrial (P0C520)
Organism: Oryza sativa (Rice)
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. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).
Subcellular location: Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein.
Interaction partners:
Sequence:
MEFSPRAAELTTLLESRMTNFYTNFQVDEIGRVVSVGDGIARVYGLNEIQAGEMVEFASGVKGIALNLENENVGIVVFGSDTAIKEGDLVKRTGSIVDVPAGKAMLGRVVDALGVPIDGKGALSDHERRRVEVKAPGIIERKSVHEPMQTGLKAVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKQMNSRGTNESETLYCVYVAIGQKRSTVAQLVQILSEANALEYSILVAATASDPAPLQFLAPYSGCAMGEYFRDNGMHALIIYDDLSKQAVAYRQMSLLLRRPPGREAFPGDVFYLHSRLLERAAKRSDQTGAGSLTALPVIETQAGDVSAYIPTNVISITDGQICLETELFYRGIRPAINVGLSVSRVGSAAQLKAMKQVCGSLKLELAQYREVAAFAQFGSDLDAATQALLNRGARLTEVSKQPQYEPLPIEKQIVVIYAAVNGFCDRMPLDRISQYEKAILSTINPELLKSFNEKGGLTNERKIELDAFLKQTAKEIN
Protein: Interleukin (Q6UG48)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MCKVLIFGCISVAMLMTTAYGASLSSAKRKPLQTLIKDLEILENIKNKIHLELYTPTETQECTQQTLQCYLGEVVTLKKETEDDTEIKEEFVTAIQNIEKNLKSLTGLNHTGSECKICEANNKKKFPDFLHELTNFVRYLQK
Protein: Prokaryotic phospholipase A2-domain-containing protein (Q2UP83)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
Sequence:
MKNIFVATLGLFAAVSSALPYTTPVNDNPISALQARATTCSAKATDNLIFKVSMKTFQKARKAKNPSKCNWSSDNCSKSPDKPDGYNFIPSCQRHDFGYRNTKKQKRFTKAMKKRIDDNFKKDLYKYCSQFSGWSSWKGVECRRLADVYYTAVRHFGKRDEALEFDPEVEFEKRDEVADVQPDEFDNFDGSEVDPDIEGQVIPEVLEDDGVDVENLDDIENLFLRCCHLKMDRSICEIFDLKSVAVNQ
Protein: 3-dehydroquinate synthase, chloroplastic (EC 4.2.3.4) (Q8RU74)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Catalyzes the second step in the shikimate pathway.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- shikimate dehydrogenase
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic
- Uncharacterized protein
- Uncharacterized protein
- 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic
- 3-phosphoshikimate 1-carboxyvinyltransferase
- 3-phosphoshikimate 1-carboxyvinyltransferase
- Shikimate kinase, chloroplastic
Sequence:
MASSFCPKQALSFTNSTHQLHQSRAIPRDIHVRFPAPVSSPSSRCGLKSKATTRLKVLATSATKVMDHSSSKASSQAPTVVEVDLGTRSYPIYIGAGLLDQPDLLQRHIHGKRVLVVTNTTVAPLYLDKTISALTDGNPNVTVESVILPDGEQFKNMETLMKVFDKAIESRLDRRCTFVALGGGVIGDMCGYAAASYLRGVNFIQIPTTVMAQVDSSVGGKTGINHPLGKNMIGAFYQPQCVLIDTDTLNTLPDRELASGLAEVIKYGLIRDAEFFEWQEQNMPLLLARDPTAFTYAIKRSCENKADVVSQDEKESGVRATLNLGHTFGHAVETGVGYGQWLHGEAVAAGTVMAVDMSRRLGWIDDSLVQRVQKILQQAKLPTSPPETMTVEMFKSIMAVDKKVADGKLRLILLKGSLGNCVFTGDYDQKALDETLRAFSKS
Protein: Serine racemase (EC 5.1.1.18) (D-serine ammonia-lyase) (D-serine dehydratase) (EC 4.3.1.18) (L-serine ammonia-lyase) (L-serine dehydratase) (EC 4.3.1.17) (O59791)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the synthesis of D-serine from L-serine. Has dehydratase activity towards both L-serine and D-serine.
Interaction partners:
- Tryptophan synthase
- Serine hydroxymethyltransferase, mitochondrial
- Probable serine hydroxymethyltransferase, cytosolic
- Probable phosphoserine phosphatase
- Threonine dehydratase, mitochondrial
- CDP-diacylglycerol--serine O-phosphatidyltransferase
- D-serine dehydratase
- Serine palmitoyltransferase 2
- Homoserine O-acetyltransferase
- Probable acetolactate synthase small subunit
Sequence:
MSDNLVLPTYDDVASASERIKKFANKTPVLTSSTVNKEFVAEVFFKCENFQKMGAFKFRGALNALSQLNEAQRKAGVLTFSSGNHAQAIALSAKILGIPAKIIMPLDAPEAKVAATKGYGGQVIMYDRYKDDREKMAKEISEREGLTIIPPYDHPHVLAGQGTAAKELFEEVGPLDALFVCLGGGGLLSGSALAARHFAPNCEVYGVEPEAGNDGQQSFRKGSIVHIDTPKTIADGAQTQHLGNYTFSIIKEKVDDILTVSDEELIDCLKFYAARMKIVVEPTGCLSFAAARAMKEKLKNKRIGIIISGGNVDIERYAHFLSQ
Protein: Heterogeneous nuclear ribonucleoprotein R (A2AW41)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MANQVNGNAVQLKEEEEPMDTSSVTHTEHYKTLIEAGLPQKVAERLDEIFQTGLVAYVDLDERAIDALREFNEEGALSVLQQFKESDLSHVQNKSAFLCGVMKTYRQREKQGSKVQESTKGPDEAKIKALLERTGYTLDVTTGQRKYGGPPPDSVYSGVQPGIGTEVFVGKIPRDLYEDELVPLFEKAGPIWDLRLMMDPLSGQNRGYAFITFCGKEAAQEAVKLCDSYEIRPGKHLGVCISVANNRLFVGSIPKNKTKENILEEFSKVT
Protein: ATP-dependent RNA helicase DDX1 (EC 3.6.4.13) (A0A087X2G1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic granule {ECO:0000256|ARBA:ARBA00004463}.
Interaction partners:
Sequence:
MNPYDRGSAFAIGSDGLCCQSREVKEWHGCRATKGLMKGKHYYEVSCHDQGLCRVGWSTMQASLDLGKKSHNKQFDNYGEEFTMHDTIGCYLDIDKGHVKFSKNGKDLGLAFEIPPHMKNQALFPACVLKNAELKFNFGEEEFKFPPKDGFVALSKAPDGYIVKSQHSGNAQVTQTKFLPNAPKALIVEPSRELAEQTLNNIKQFKKYIDNPKLRELLIIGGVAARDQLSVLENGVDIVVGTPGRLDDLVSTGKLNLSQVRFLVLDEADGLLSQGYSDFINRMHNQIPQVTSDGKRLQVIVCSATLHSFDVKKLSEKIMHFPTWVDLKGEDSVPDTVHHVVVPVNPKTDRLWERLGKSHIRTDDVHAKDNTRPGANSPEMWSEAIKILKGEYAVRAIKEHKMDQAIIFCRTKIDCDNLEQYFIQQGGGPDKKGHQFSCVCLHGDRKPHERKQNLERFKKGDVRFLICTDVAARGIDIHGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAISLVATEKEKVWYHVCSSRGKGCYNTRLKEDGGCTIWYNEMQLLSEIEEHLNCTISQVEPDIKVPVDEFDGKVTYGQKRAAGGGSYKGHVDILAPTVQELAALEKEAQTSFLHLGYLPNQLFRTF
Protein: Electron transport protein HydN (P0AAK4)
Organism: Escherichia coli (strain K12)
Function: Electron transport from formate to hydrogen.
Interaction partners:
- Formate hydrogenlyase subunit 6
- Formate dehydrogenase H
- Formate hydrogenlyase subunit 5
- Carbamoyltransferase HypF
- Formate hydrogenlyase subunit 4
- Formate hydrogenlyase regulatory protein HycA
- Formate hydrogenlyase subunit 7
- Formate hydrogenlyase maturation protein HycH
- Formate hydrogenlyase subunit 2
- Formate hydrogenlyase subunit 3
Sequence:
MNRFIIADASKCIGCRTCEVACVVSHQENQDCASLTPETFLPRIHVIKGVNISTATVCRQCEDAPCANVCPNGAISRDKGFVHVMQERCIGCKTCVVACPYGAMEVVVRPVIRNSGAGLNVRADKAEANKCDLCNHREDGPACMAACPTHALICVDRNKLEQLSAEKRRRTALMF
Protein: Palmitoyltransferase ZDHHC7 (EC 2.3.1.225) (Acyltransferase ZDHHC7) (EC 2.3.1.-) (GABA-A receptor-associated membrane protein 2) (SERZ-beta) (Zinc finger DHHC domain-containing protein 7) (DHHC-7) (Q91WU6)
Organism: Mus musculus (Mouse)
Function: Golgi-localized palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and therefore functions in several unrelated biological processes. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (Probable). Palmitoylates sex steroid hormone receptors, including ESR1, PGR and AR, thereby regulating their targeting to the plasma membrane and their function in rapid intracellular signaling upon binding of sex hormones. Palmitoylates GNAQ, a heterotrimeric G protein, regulating its dynamic localization at the plasma membrane and is thereby involved in GNAQ-dependent G protein-coupled receptor signaling pathways. Functions also in ligand-induced cell death by regulating the FAS signaling pathway through the palmitoylation and stabilization of the receptor at the plasma membrane. In epithelial cells, palmitoylates SCRIB and regulates its localization to the plasma membrane, regulating indirectly cell polarity and differentiation. Also palmitoylates JAM3 and promotes its expression at tight junctions and regulates its function in cell migration (By similarity). Palmitoylates the glucose transporter GLUT4/SLC2A4 and controls the insulin-dependent translocation of GLUT4 to the plasma membrane. In brain, could also palmitoylate SNAP25 and DLG4/PSD95. Could also palmitoylate DNAJC5 and regulate its localization to the Golgi membrane. Could also palmitoylate NCDN. May play a role in follicle stimulation hormone (FSH) activation of testicular Sertoli cells (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:18596047, ECO:0000269|PubMed:25301068}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MQPSGHRLRDIEHHPLLTDNDNYDSASSSSSETDMADRVWFIRDGCGMVCAVMTWLLVVYADFVVTFVMLLPSKDFWYSVVNGVLFNCLAVLALSSHLRTMLTDPGAVPKGNATKEYMESLQLKPGEVIYKCPKCCCIKPERAHHCSICKRCIRKMDHHCPWVNNCVGEKNQRFFVLFTMYIALSSVHALILCGLQFISCVRGQWTECSDFSPPITVILLVFLCLEGLLFFTFTAVMFGTQIHSICNDETEIERLKSEKPTWERRLRWEGMKSVFGGPPSLLWMNPFVGFRLRRLQMRTRKGGPEFSV