wanglab/gogpt-training-data huggingface dataset:
Protein: Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 (E-NPP 3) (Alkaline phosphodiesterase I) (EC 3.1.4.1) (Dinucleoside polyphosphatase) (EC 3.6.1.-) (Nucleotide diphosphatase) (Nucleotide pyrophosphatase) (NPPase) (EC 3.6.1.9) (Phosphodiesterase I beta) (PD-Ibeta) (Phosphodiesterase I/nucleotide pyrophosphatase 3) (CD antigen CD203c) (Q6DYE8)
Organism: Mus musculus (Mouse)
Function: Hydrolase that metabolizes extracellular nucleotides, including ATP, GTP, UTP and CTP (By similarity). Limits mast cell and basophil responses during inflammation and during the chronic phases of allergic responses by eliminating the extracellular ATP that functions as signaling molecule and activates basophils and mast cells and induces the release of inflammatory cytokines. Metabolizes extracellular ATP in the lumen of the small intestine, and thereby prevents ATP-induced apoptosis of intestinal plasmacytoid dendritic cells. Has also alkaline phosphodiesterase activity (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:25692702}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O14638}. Apical cell membrane {ECO:0000250|UniProtKB:O14638}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O14638}. Secreted {ECO:0000250|UniProtKB:O14638}. Note=Detected at the cell surface of basophils (PubMed:25692702). Detected at the apical plasma membrane of bile duct cells. Located to the apical surface in intestinal and kidney epithelial cells. Secreted in serum, and in lumen of epithelial cells (By similarity). {ECO:0000250|UniProtKB:O14638, ECO:0000269|PubMed:25692702}.
Interaction partners:
- Ectonucleoside triphosphate diphosphohydrolase 3
- Phosphodiesterase
- Ectonucleoside triphosphate diphosphohydrolase 1
- 5'-nucleotidase
- Bis
- Ectonucleoside triphosphate diphosphohydrolase 8
- Cytosolic 5'-nucleotidase 3A
- cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
- Adenosine kinase
Sequence:
MDSRLALATEEPIKKDSLKKYKILCVVLLALLVIVSLGLGLGLGLRKPEEQGSCRKKCFDSSHRGLEGCRCDSGCTGRGDCCWDFEDTCVKSTQIWTCNLFRCGENRLETALCSCADDCLQRKDCCADYKTVCQGESPWVTEACASSQEPQCPPGFDLPPVILFSMDGFRAEYLQTWSTLLPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVHLNKNFSLSSVEKSNPAWWSGQPIWLTAMYQGLKAACYYWPGSDVAVNGSFPTIYRNYSNSVPYERRITTLLQWLDLPKADRPSFYTIYVEEPDSAGHSSGPVSAGVIKALQSVDNAFGMLMEGLKQRNLHNCVNIIVLADHGMDQTSCDRVEYMTDYFPKINFYMYQGPAPRIRTRNIPQDFFTFNSEEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKAHLMVDRQWLAFRSKGSSNCGGGTHGYNNEFKSMEAIFLAHGPSFIEKTVIEPFENIEVYNLLCDLLHIEPAPNNGTHGSLNHLLKTPFYKPSHAGELSTPADCGFTTPLPTDPLDCSCPALQNTPGLEEQANQRLNLSEGEVAATVKANLPFGRPRVMQKNGDHCLLYHRDYISGYGKAMKMPMWSSYTVLKPGDTSSLPPTVPDCLRADVRVAPSESQKCSFYLADKNITHGFLYPAIKGTNESRYDALITSNLVPMYKEFKKMWDYFHEVLLIKYAIERNGLNVVSGPIFDYNYDGHFDAPDEITQYVAGTDVPIPTHYFVVLTSCKDQTHTPDSCPGWLDVLPFIVPHRPTNIESCSENKTEDLWVEERFQAHAARVRDVELLTGLDFYQEKAQPVSQILQLKTYLPTFETII
Protein: Type II inositol 3,4-bisphosphate 4-phosphatase (EC 3.1.3.66) (Inositol polyphosphate 4-phosphatase type II) (Q6P1Y8)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of the 4-position phosphate of phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-trisphosphate and inositol 3,4-bisphosphate (By similarity). Plays a role in the late stages of macropinocytosis by dephosphorylating phosphatidylinositol 3,4-bisphosphate in membrane ruffles (By similarity). Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival (By similarity).
Interaction partners:
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- Type II inositol 1,4,5-trisphosphate 5-phosphatase
- Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma
- Synaptojanin-2
- Inositol polyphosphate 5-phosphatase OCRL
- Myotubularin
Sequence:
MEIKEEGTSEEGQHFLPAAQANDPEDIQFTSIQKIPNEPQLEFILACRDLVAPVSDRKLNTVVQISVIHPVEQTLTRYSSTEIVEGTKDPLFLTGVTFPPDYPIYEETRIKLTVYDVKDKSHDTRSFLGCASFKVGELLKSKEQLLSLSLRTSDGGKVVGTIEVSLVKMGEIEDGDTDHITTDVQGQKCALMYESTAPESLSGKENLPFMNAVLRNPVCKLYRFPTSDNKWMRIREQMSESILSFHIPKELISLHIKEDLCRNQELKELGDLSPHWDNLRKNVLSHCDQMVTMYQDILTELSKETGSSFKSSSSKGEKTLEFVPVNLHLQRMQVHSPHLKDALYDVITVGAPAAHFQGFKNGGLRKLLHRFETERRNTGYQFIYYSPENTAKAKEVLSSINQLQPLIATHADLLLTSASQRSPDSLKSSLKLLSEKTELFVHAFKDQLVRSALLALYTARPGGILKKPPSPNVSTEEKSTQHDTPQLRRQDSIPHHSDYDEEEWDRVWANVGKSLNCIIAKVDKLIERDSHNEEGAGGSSSKDGEADHTLEDSITSHPREDWYEQLHPLILTLKECMGEVVNRAKQSLTFVLLQELAYSLPQCLMLTLRRDIVFSQALAGLVCGFIIKLHTSLHDPGFLQQLHTVGLIVQYEGLLSTYSDEIGMLEDMAVGISDLRKVAFKITEATSNDVLPVLTGRREHYVVEVKLPATVFESLPLQIKEGQLLHVYPVLFNVGINEQQTLAERFGDVSLQESINQENFELVQEYYSIFMEKMPPDYISHFQEQTDLKGLLDNLHQNIQAKKRKNVEIMWLAATICRKLNGIRFTCCKSAKDRTSMSVTLEQCSILRDEHQLHKDFFIRALDCMRSRQTQGALNESDDPETGCLTDNKPTSRHFYPVALLLVSSHLLVVWLILSLALLLAKYQ
Protein: Cyclin-B2-2 (Cyc2b-At) (Cyclin-2b) (G2/mitotic-specific cyclin-B2-2) (CycB2;2) (Q39070)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cyclin-dependent kinase B1-2
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B2-2
- Cell division cycle 20.1, cofactor of APC complex
- Cyclin-dependent kinase A-1
- Wee1-like protein kinase
- Mitotic spindle checkpoint protein MAD2
- Cell division cycle 20.2, cofactor of APC complex
- Anaphase-promoting complex subunit 10
Sequence:
MVNPEENNRNLVVKPITEILQDDDKRSRKFGVEMKRQNRRALGVINHNLVGAKAYPCVVNKRRGLSQRKQESCDKKKLDSLHPSISRSQEETKKLKPSGNEFGDCIFIDEEEEKNEEVTLDQPMPMSLEEPYIEFDPMEEEVEMEDMEEEQEEPVLDIDEYDANNSLAAVEYVQDLYDFYRKTERFSCVPLDYMAQQFDISDKMRAILIDWLIEVHDKFELMNETLFLTVNLIDRFLSKQAVARKKLQLVGLVALLLACKYEEVSVPIVEDLVVISDKAYTRTDVLEMEKIMLSTLQFNMSLPTQYPFLKRFLKAAQSDKKLEILASFLIELALVDYEMVRYPPSLLAATAVYTAQCTIHGFSEWNSTCEFHCHYSENQLLECCRRMVRLHQKAGTDKLTGVHRKYSSSKFGYIATKYEAAHFLVSDSH
Protein: Surfeit locus protein 1 (Surfeit 1) (Cytochrome c oxidase assembly protein SURF1) (Protein EMBRYO DEFECTIVE 3121) (Surfeit locus 1 cytochrome c oxidase biogenesis protein) (Q9SE51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably involved in the biogenesis of the COX complex.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Heme A synthase COX15
- Cytochrome c oxidase assembly protein COX11
- Pentatricopeptide repeat-containing protein At3g48810
- Protoheme IX farnesyltransferase, mitochondrial
- Cytochrome c-type biogenesis CcmH-like mitochondrial protein
- ATP synthase subunit a-1
- RING-H2 finger protein ATL48
- Cytochrome c oxidase subunit 6b-1
- Replication factor C subunit 2
- Cytochrome c oxidase 19-1
Sequence:
MATSLSKILTRSNTKRYWCSTTTSISASPSLPKQFWSRHFSAVADSSSSSSAALGSQSSSSAPPQENKRGSKWSQLLLFLPGAITFGLGSWQIVRREEKFKTLEYQQQRLNMEPIKLNIDHPLDKNLNALEFRRVSCKGVFDEQRSIYLGPRSRSISGITENGFFVITPLMPIPGDLDSMQSPILVNRGWVPRSWREKSQESAEAEFIANQSTKAKSPSNEPKSWWKFWSKTPVITKEHISAVKPVEVVGVIRGGENPSIFVPSNDPSTGQWFYVDVPAMARAVGLPENTIYVEDVHEHVDRSRPYPVPKDINTLIRSKVMPQDHLNYSITWYSLSAAVTFMAYKRLKAKPVRR
Protein: Zinc finger protein GLIS2 (GLI-similar 2) (Neuronal Krueppel-like protein) (Zinc finger protein GLI5) (Q8VDL9)
Organism: Mus musculus (Mouse)
Function: Can act either as a transcriptional repressor or as a transcriptional activator, depending on the cell context. Acts as a repressor of the Hedgehog signaling pathway. Represses the Hedgehog-dependent expression of Wnt4. Necessary to maintain the differentiated epithelial phenotype in renal cells through the inhibition of SNAI1, which itself induces the epithelial-to-mesenchymal transition. Represses transcriptional activation by CTNNB1 in the Wnt signaling pathway. May act by recruiting the corepressors CTBP1 and HDAC3. May be involved in neuron differentiation.
Subcellular location: Nucleus speckle. Cytoplasm.
Interaction partners:
- Protein CBFA2T3
- Catenin delta-1
Sequence:
MHSLDEPLDLKLSITKLRAAREKRERTLGVVRHHALHRELGLVDDSPAPGSPGSPPPGFLLNPKFPEKVDGRFSAAPLVDLSLSPPSGLDSPNGSSSLSPECQGNGDLPPLPTAVDFQPLRYLDGVPSSFQFFLPLGSGGALHLPASSFLPPPKDKCLSPELPLAKQLVCRWAKCNQLFELLQDLVDHVNDHHVKPEQDARYCCHWEGCARHGRGFNARYKMLIHIRTHTNEKPHRCPTCNKSFSRLENLKIHNRSHTGEKPYVCPYEGCNKRYSNSSDRFKHTRTHYVDKPYYCKMPGCHKRYTDPSSLRKHIKAHGHFVSHEQQELLQLRPPPKPPLPTPDSGSYVSGAQIIIPNPAALFGGPSLPGLPLPLPPGPLDLSALACGNGGGGGGGIGPGLPGSVLPLNLAKNPLLPSPFGAGGLGLPVVSLLGGSAGSKAEGEKGRGSVPARVLGLEDHKTPLERTERSRSRPSPDGLPLLPGTVLDLSTGNSAASSPEVLTPGWVVIPPGSVLLKPAVVN
Protein: Interferon regulatory factor 7 (IRF-7) (P70434)
Organism: Mus musculus (Mouse)
Function: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Can efficiently activate both the IFN-beta (IFNB) and the IFN-alpha (IFNA) genes and mediate their induction via both the virus-activated, MyD88-independent pathway and the TLR-activated, MyD88-dependent pathway. Induces transcription of ubiquitin hydrolase USP25 mRNA in response to lipopolysaccharide (LPS) or viral infection in a type I IFN-dependent manner. Required during both the early and late phases of the IFN gene induction but is more critical for the late than for the early phase. Exists in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization where along with other coactivators it can activate transcription of the type I IFN and ISG genes. Can also play a role in regulating adaptive immune responses by inducing PSMB9/LMP2 expression, either directly or through induction of IRF1. Binds to the Q promoter (Qp) of EBV nuclear antigen 1 a (EBNA1) and may play a role in the regulation of EBV latency. Can activate distinct gene expression programs in macrophages and regulate the anti-tumor properties of primary macrophages.
Subcellular location: Nucleus {ECO:0000269|PubMed:15361868}. Cytoplasm {ECO:0000269|PubMed:15361868}. Note=The phosphorylated and active form accumulates selectively in the nucleus.
Interaction partners:
- TNF receptor-associated factor 6
- Myeloid differentiation primary response protein MyD88
- Interferon regulatory factor 3
- Interleukin-1 receptor-associated kinase 4
- TNF receptor-associated factor 3
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit epsilon
- Serine/threonine-protein kinase TBK1
- Z-DNA-binding protein 1
- Transcription factor Jun
Sequence:
MAEVRGVQRVLFGDWLLGEVSSGQYEGLQWLNEARTVFRVPWKHFGRRDLDEEDAQIFKAWAVARGRWPPSGVNLPPPEAEAAERRERRGWKTNFRCALHSTGRFILRQDNSGDPVDPHKVYELSRELGSTVGPATENREEVSLSNALPTQGVSPGSFLARENAGLQTPSPLLSSDAGDLLLQVLQYSHILESESGADPVPPQAPGQEQDRVYEEPYAAWQVEAVPSPRPQQPALTERSLGFLDVTIMYKGRTVLQAVVGHPRCVFLYSPMAPAVRTSEPQPVIFPSPAELPDQKQLHYTETLLQHVSPGLQLELRGPSLWALRMGKCKVYWEVGSPMGTTGPSTPPQLLERNRHTPIFDFSTFFRELEEFRARRRQGSPHYTIYLGFGQDLSAGRPKEKTLILVKLEPWVCKAYLEGVQREGVSSLDSSSLGLCLSSTNSLYEDIEHFLMDLGQWP
Protein: Ubiquitin conjugating enzyme (Q9N9Z5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAGSALRRLMAEYKQLTLDPPEGIVAGPISEDNFFEWEALIAGPEGTCFEGGVFPARLIFPTDYPLSPPKMKFTCDMFHPNIFADGRVCISILHAPGDDPMGYELSAERWSPVQSVEKILLSVVSMLAEPNDESGANVDAAIMWREQRDEFNAIADGWCAKLLVYRRKWIMCVTVNTFYPEQHDSNNSLTHSFLKNPSLS
Protein: All-trans-retinol 13,14-reductase (EC 1.3.99.23) (All-trans-13,14-dihydroretinol saturase) (RetSat) (PPAR-alpha-regulated and starvation-induced gene protein) (Q64FW2)
Organism: Mus musculus (Mouse)
Function: Catalyzes the saturation of all-trans-retinol to all-trans-13,14-dihydroretinol. Does not exhibit any activity toward all-trans-retinoic acid, nor 9-cis, 11-cis or 13-cis-retinol isomers. May play a role in the metabolism of vitamin A. Independently of retinol conversion, may regulate liver metabolism upstream of MLXIPL/ChREBP. Required for adipocyte differentiation in a 3T3-L1 cell culture model. This effect seems not to mimic the in vivo situation in which animals show increased adiposity in the absence of RETSAT.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15358783, ECO:0000269|PubMed:19139408}; Peripheral membrane protein {ECO:0000269|PubMed:15358783}.
Interaction partners:
- Lecithin retinol acyltransferase
- Cytochrome P450 26A1
- Retinol dehydrogenase 12
- Retinol dehydrogenase 11
- Short-chain dehydrogenase/reductase 3
- Dehydrogenase/reductase SDR family member 4
- 17-beta-hydroxysteroid dehydrogenase type 6
- Alcohol dehydrogenase 1
- Retinol dehydrogenase 7
- Retinol dehydrogenase 10
Sequence:
MWITALLLAVLLLVILHRVYVGLYAASSPNPFAEDVKRPPEPLVTDKEARKKVLKQAFSVSRVPEKLDAVVIGSGIGGLASAAVLAKAGKRVLVLEQHTKAGGCCHTFGENGLEFDTGIHYIGRMREGNIGRFILDQITEGQLDWAPMASPFDLMILEGPNGRKEFPMYSGRKEYIQGLKKKFPKEEAVIDKYMELVKVVARGVSHAVLLKFLPLPLTQLLSKFGLLTRFSPFCRASTQSLAEVLQQLGASRELQAVLSYIFPTYGVTPSHTAFSLHALLVDHYIQGAYYPRGGSSEIAFHTIPLIQRAGGAVLTRATVQSVLLDSAGRACGVSVKKGQELVNIYCPVVISNAGMFNTYQHLLPETVRHLPDVKKQLAMVRPGLSMLSIFICLKGTKEDLKLQSTNYYVYFDTDMDKAMERYVSMPKEKAPEHIPLLFIAFPSSKDPTWEERFPDRSTMTALVPMAFEWFEEWQEEPKGKRGVDYETLKNAFVEASMSVIMKLFPQLEGKVESVTGGSPLTNQYYLAAPRGATYGADHDLARLHPHAMASIRAQTPIPNLYLTGQDIFTCGLMGALQGALLCSSAILKRNLYSDLQALGSKVKAQKKKM
Protein: Eps15 homology domain containing protein-binding protein 1, isoform F (A4UZL3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD39986p
- LD06095p
- AT21416p
- LD44762p
- Exocyst complex component 6
- Rab11
Sequence:
MASVWKRLQRNFKRAAKFQFTASYHDLHLETTAKWRPSNLSIVWTRRSRRVASAPLPWEPDMMNPLVGNISWPVPDNHTISVTLFKDPRTHELEDKDWTFVIEDVTPMGKKRVLANASINMRKYASIESTQQSFTLSLKPVSKKITAASLELTISCVFLREGKATDEDMQSVVSMMSVNNNDVAPLDDLEDIPDLDGFSEITDNFNDFTQQLEHMTTSLNGCIDVATPQSVPSLSEDPTPLAESFNPLHFELDADGKREAANKLDLPTAASGGSSGAEESLKTPNGLQHVVDQTPIKSPDEVKQPKQTPVESLRSKTNEDFDKMVTSTPLEPNVNKDDVKPKKKRALFFTEKEDEQDLRVESVKEDTTKTIGDNSTTKEKPKEESQSSKDASSVVVPSAKRPELQPLNLKKSYEPSQTPESAPVPASVINESIGSCFSTSGSLNNSLKPVEKIVLKENTPGQDLLEWCKEVTKDYPNVKVTNLTTSWRNGMAFCAIIHHFVPELIDMSKLSAHDVVGNCRIGFDAAESLGIPRVIEPRDMNMLTVPDKLAVMTYLHQLRAHFTGKQLKIEQIGSTADESSYVIGDYKSDNLSQNRINFSHPKSLLLHQNSFDEEINGSNKSEQLSPTSKKDVKNLILYNSKNILDKVLSPTKDKNSINASQHANQSPMLSCQTTPPQDESLDKGSQPGGKENSSITTIDPQAASEERQQRLLEQARRLILETRVKSGGSIESPTRPKLERTISPIHNGAEEFYAEHAKKLELKEPGSPSHRLSDPKVLQSFNAIVERVSPKHEKRGDKLSYIDSELEALEREQEAIDQKASNLEAKLRAVMGGNPSNNRRGGARNSNPFLRLIRNSIGGGDVIRIKLLDSDDESLFGGGAGSGGGRSGACSEDDDRDTSSDSVCNSGDELHTRLRPRPRSHSCFVNKNHQSTINTPAHLRPHHVHHVVPYTHMLDSSPSALSSQQSSCDNLPACSDDDEVLAVAANGRAASLRRQQDRHRRRRQRRERRSHLCHTPNHCETEETEEQLLSQWFTLVNKKNALLRRQMQLNILEQEKDLERKYTMLNQELRAAQSVEDWRKTEVQREKERLLLEELMTIVDKRDQLVQHLHNQEIAIEDDQEIARKLEHVDISAEKDKCVLQ
Protein: Monocarboxylate transporter 10 (MCT 10) (Aromatic amino acid transporter 1) (Solute carrier family 16 member 10) (T-type amino acid transporter 1) (Q3U9N9)
Organism: Mus musculus (Mouse)
Function: Sodium- and proton-independent thyroid hormones and aromatic acids transporter. Mediates both uptake and efflux of 3,5,3'-triiodothyronine (T3) and 3,5,3',5'-tetraiodothyronine (T4) with high affinity, suggesting a role in the homeostasis of thyroid hormone levels (By similarity). Responsible for low affinity bidirectional transport of the aromatic amino acids, such as phenylalanine, tyrosine, tryptophan and L-3,4-dihydroxyphenylalanine (L-dopa). Plays an important role in homeostasis of aromatic amino acids.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16245314}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:16245314}; Multi-pass membrane protein {ECO:0000255}. Note=Detected in basolateral membrane of kidney proximal tubule starting at he beginning of the proximal tubule epithelium within the glomerular capsule and extending to the S1 and S2 segments. Also localizes to the basolateral membrane of small intestine enterocytes and to sinusoidal side of perivenous hepatocytes. {ECO:0000269|PubMed:16245314}.
Interaction partners:
- Monocarboxylate transporter 8
- Solute carrier organic anion transporter family member 1C1
- Large neutral amino acids transporter small subunit 2
Sequence:
MVPSQEEPAAERETNEAQPPGPAPSDDAPLPGPGPSDVSDVAAEKVEVELTRSAGSEPPVPPEGGWGWLVMLAAMWCNGSVFGIQNAYGVLFVSMLDTFKAKDDDNMAFKTAWVGSLSMGMIFFCCPIVSVFTDMFGCRRTAVVGAAVGFIGLMSSSFVSSIEPLYLTYGIIFACGCSFAYQPSLVILGHYFKKRLGLVNGIVTAGSSVFTILLPLLLGNLISSVKLFNTLRILCIFMFVLFLAGFTYRPLVPSTKEKESGGSRSSFFSRRKLSPPKKVFNFALFKETTYAVWAAGIPLALFGYFVPYVHLMNHVKERFQDVNNKEVLFMCIGITSGVGRLLFGRIADYLPGVKKVYLQVLSFFFIGLMSMMIPLCSAFGALIAVCLAMGLFDGCFISIMAPIAFELVGPQDASQAIGFLLGFMSIPMTVGPPIAGLLHDKLGTYDVAFYLAGIPPFVGGVVLCLIPWIHSKKQRKISKNAGGEKMEKMLENQSSLLSGSSGIFKKDSASII
Protein: Cytochrome c oxidase subunit 4 isoform 1, mitochondrial (Cytochrome c oxidase polypeptide IV) (Cytochrome c oxidase subunit IV isoform 1) (Q86WV2)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
Sequence:
MLATRVFSLVGKRAISTSVCVRAHESVVKSEDFSLPAYMDRRDHPLPEVAHVKHLSASQKALKEKEKASWSSLSMDEKVECGY
Protein: Exported protein family 1 (B9ZSJ2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MHSMKERRYYSIYKKDNKMEDLGNKNKNKIHFISVSLMNCLSVIMFIILYIISLHIFFYKTNSFHLSLREPVPYANRTYNRILYSTEKKKVNRREQIRTQREPQKSNYKASMKNYLKCVKSAPYIDDAKYGALISEEEEREMKMIKKMELEELEKRDELMEKRRLRRIERMKKKEEEKRIKEEEERIKEEEKRIKEEEERIKEEEKRLKEEEERRLKEEEERRLKEEEERRLKEEEKERLKMLEEDKLYKEREEQKKNKLNVEEEVVTFERLKSKKMDEKEDTVVEKKENVEDQKDTEEVREEASEDKGDIEEVGKEEASEDKEDTEEVKEQEVSEDKEDAEEVGKGEVSEDIEDKEEEGEKEVSEDIEDKEEEGEKEESEDKGDKEEEGKKEVSEDKENAEEVREEEASEDKEDAEELGKGEVSEDMEDKEEEGKKEESEDKENAEELGKREVSEDKENAEEVREEEASEDKEDAEELGKGEVSEDIEDKEEEGEKEESEDKGDKEEEGKKEESEDKENAEEVGKEEASEDKEDAEELGKGEVSEDIEVQEEEGEKEESEDKGDAEELGKGEVSEDKEDKEKEGKKEESEDKEDTEEVKEEEASEDKENAEEVGKEEASEDKEDAEELGKGEVSEDKEDADEVEKEETSEDVRDNEEVGEGEVSEDIEVQEEEGEKEESEDKGDAEELGKGEVSEDKGDAEELGKEETSEVKGDAEELGKEETSEDKEYTEEVGKEEASEDKEDTEEVKEEEVSEDKGDIEEVEKEETSEDKGDTEEVREDEVSEDIEDSDEVGEGEVSEDIEDSEEVGKEEEPYEKGDYEEVGKEEASYDKGDADEVSEDIEDYEELGKEEEPYEKGDYEEVGKEEASYDKGDAEEIGKEEASDDKGDSEELGKEEEPYEKGDYEEVGKEEASYDKGDAEEIGKEEASDDKGDSEEVGKEEASDDKGYSEEVGKEEGSYDKGDAEEVEDEDEEHIRSKEEVKEPEIGTDIEEENKEKYIKKLDVQDTLYEINVLNGEDITSFLENKNKIIQNEGEEDDDDDEDDEDDEDGEDGKGVYINIVNNVPGNIWNDTIYDDNYNNNTYSSAEEYIFYEKKLDDNTRNNMKRSYYDILDVKEDSDINEIKRKFYNLSLKYYPKMNKDKNLVMNQKFENISEAYQILGYENRRKLYDLGEYDETNKMIIIDPLIFFNLIFTSDMMYEYTGNTQVSTFVKLFFEKNISVEDISYYVGEIMKEMMEGQNIREEKVAELLKDRLDLYIDNEDEWKKLMENEISMLLKSSFSSFILESIGWTYENVSNIFLEEKVNSGKNKKGIYLKEANERIIRNSIVLRQCKSRFISIITNYYPFKEQNNPFIKQAQYVSSSNYVLDDIINNIDYSIDNIHRAIDNLYYEHILNLLEEEKNEILEEILRNILKIILCDVETTVRRSAQKVLQNAEGDTNLMLKRAKGLQSLGKMILQKVN
Protein: C4-dicarboxylate-binding periplasmic protein DctP (Q9HU18)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system DctPQM involved in C4-dicarboxylates uptake.
Subcellular location: Periplasm {ECO:0000250|UniProtKB:P37735}.
Interaction partners:
- C4-dicarboxylate TRAP transporter large permease protein DctM
- C4-dicarboxylate TRAP transporter small permease protein DctQ
- Probable c4-dicarboxylate-binding protein
- Probable C4-dicarboxylate-binding periplasmic protein
- TRAP transporter small permease protein
- TRAP transporter large permease protein
- TRAP transporter large permease protein
Sequence:
MLKHTAKALVCALSLTVAGIVQAADPIVIKFSHVVAEHTPKGQGALLFKKLVEERLPGKVKVEVYPNSSLFGDGKEMEALLLGDVQIIAPSLAKFEQYTKKLQIFDLPFLFDNIQAVDRFQQSPQGKELLTSMQDKGITGLGYWHNGMKQLSANKPLREPKDARGLKFRVQASKVLEEQFKAVRANPRKMSFAEVYQGLQTGVVNGTENPWSNIYSQKMHEVQKYITESDHGVLDYMVITNTKFWNGLPEDVRGVLAKTMDEVTVEVNKQAEALNQGDKQRIVEAKTSEIIELTPEQRAEWRKAMQPVWKKFEGEIGADLIKAAEAANQAQ
Protein: Mitochondrial transcription termination factor family protein (Q0WRV2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Mitochondrial transcription termination factor family protein
- Transcription termination factor family protein
- Transcription termination factor MTEF18, mitochondrial
Sequence:
MELLHTSCNFETLTLISPPLKSCNFSSSSLFFSPRRVTLFPAYHSGRVTVSASLQHGDSNFSSNSSQTNQEAQNSIAGFLRRDTGLSEADSDFISSNCPKYTRMIVEGVRDLEEWNSWKGSGESERVEEGLGFKEKVIYMVKQKGDGGKVAFLESLGLSLSSAMYLAHYVSSESLPILLDKVKYLKEIFFSGSDEKGLVGKYARRMMLYLSIPIDEDVQQTLSFFEKIEARRGGLDMLGSVDASFRFLLESFPRLLLLSEENDMKPMVEFLESIGIPKYCLGKVLLLYPPIMLGKTEEIKRRVATAMEKVSVVNKDSGKLLLKYPWILSPSIQENYSHIGSFFYSESVLKMDIDHAIRRWPLLLGCSASNMEMMVKEFDKLGVRDKRMGKVIPKMPQLLLCKPQEFLKVVCFLEDLGFQKEIVGQILCRCPEIFGCSIEKTLQKKLIFLTRFGVSTTHFPRIIKKYPEFLIYDADKTVLPRLKYLMEIGISEREIAFMIRKFSPILGYSIDKVLRPKFEFLVNSMEKPVREVIEYPRYFSYSLEKRIKPRFRVLKGRNIECTLQEMLGKNDEEFAADFLGLGELQTHSEIS
Protein: Ornithine aminotransferase (EC 2.6.1.13) (Q6FK60)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Arginase
- Protein ARG5,6
- Ornithine decarboxylase
- Multifunctional fusion protein
- Argininosuccinate lyase
- Candida glabrata strain CBS138 chromosome D complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Arginine biosynthesis bifunctional protein ArgJ
- Argininosuccinate synthase
- ornithine carbamoyltransferase
Sequence:
MNFNISSKETVELEQKYSAHNYHPLPVVFHKASGAHVWDPEGKEYLDFLSAYSAVNQGHCHPKIVKALVDQASTLTLSSRAFSNDVFAVFAKYVTEYFGYEMVLPMNTGAEAVETALKLARRWGYEVKKIPDNEAIVLGAQGNFHGRTFGAISLSTDEEDSRKHFGPFLTNTTAKNPSKGQAIRYGHIEDLEQAFESHGDKIAAVILEPIQGEAGIVVPPKGYLLDVQNLCKKYNSLFICDEIQTGIGRTGKLLCFEHTEGVKPDVVLLGKAISGGVLPVSCVLSSREIMSCFTPGSHGSTFGGNPMASRVAIAALDVIKEEKLVERAQKLGDLLQDELRKLQAQSDGMISEVRGVGLLTAIVIDSQKAQGRTAWDLCLLMKDKGVLAKPTHDHIIRLAPPLVISEEDLLKGVQAMKEALVELPSAPISGH
Protein: Spinophilin, isoform G (M9NEY5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MEKPMHHAPAPVGKVSQIANIFQRKPIEIQPVEQLSAVAAAHAAAAAAAAAAHHAHVQGAPAVRTESHSARFNNARALFEKLGVESNSNVSSRLLRSGSREDNLCDGSDRSSSRSSDRSQSPPKRRTPFPSGVSLVHNNNNAAIVAQNGVPPEQRLSNSKFIVEPAAQVVPTSVVKYPQHNISRLKSEEPSPVPPPASGSVSALFASSGGDKPEKPERKFNSRELIEKQKKWTSHFTKTKTTRTHSDLNRCDIIRTVPGTGLIMDSEKVAKPAMEPPQPPPNASPNPPMRAQAPPEIKPRSGKIGSPVKSPPLPPIPAVKPKNVSPVKFNPDRLRQSPTKTADNSPPPPPAKSAAVLQRSLMQEQQELLRNSCDQGVAPIPPEKPRKKSVDLIEDTLPLTNCSTPSSCASPTSSYLMQPAKRGSLDGGSGNGQYPGNGLSGSTNSATSGSPVASASSGPSSPVHTEDEKQENESTEKSEMEYYHGGNYNSVPRRRRSENEGRKSVDESSPSANNSQQQQQHSIPGSAAGSPQRVANKRSSITVNMPAAGLGQRPPSIISTTSQDEGGFNESAPELKAKLQPAYDQTEEQPHSLNYVDVGYRLNPDGSESREVYGSEAELYDTAKVTDMQRKFHGANGFGQESSTVYAIIKPDVQESQPVAPSRSVLIQSPNSSSVEGSPLHRGSYSSPPVGVVSPIRRRNSSNQDQSVGGGGSAKTTPQCSPARSALVKGIAPIASIDAHEEEELDLVEEDEHLAVEYVEVLELQQDEEEEEAPVLPERRAPAQGSLELQDLEYADTSAGEDEEDIINHLKDGDVLDVELIDDVVDEVIKVHVNHSVATAPSIQAATPAAAIPREDSLPDDMTAAEAERLLSSRQQSLLSDEQAKEVEQILNAAPSVGVAVATVVATATSPTSIKNLIEDLPGQSAVAASAANGEQDIQIAAVPAIVEEDEDEEEDFPEDDEEDHARADFDANGGDADGDSDDVEAVDIVGYGHASTALNATFVKADSTETETTTTTPSTATTATTRHDDDEPEWLRDVLEAPKRSLENLLITSATSSRAPGQREELENGYDLHEKHSDLNQTYITGGESLHESIVSVESTQSDATLNQTTTIDDSIISSKHNSTYSLADAEQATSSTVLSTGVTELDDSQYYIPEYPPVRSKEVLVEAGVHYFEDGNFWMEVPGLLDFDDDDCSYPPITVRKNPKVRFSSGPIHVYSTFSVNDYDRRNEDVDPVAASAEYELEKRVEKMHVFPVELMKGPEGLGLSIIGMGVGADAGLEKLGIFVKTITDNGAAARDGRIQVNDQIIEVDGKSLVGVTQAYAASVLRNTSGLVKFQIGRERDPENSEVAQLIRLSLQADREKEERLKRQQEEYLRRTLDYSEDSTQPVSANSSVCEGPSSPVQVEHPMEVEATHSQEVESLKRLLQESEMGCLVKEEIIQNLKRKLVKLETTGNENELLSERLRQSERELGNIRKEAANLQNMLQQSQGQYMALDKKYNKAKRLVREYQQRELDMCHREEFYQQLLQEKDTEYNALVKKLKDRVINLEHELQETQRKAGFPVGLPYDSATLKLTPQMMRKTPPKPLFHKLETELSDTEISDLSPDGDGVKTATVERKVPVKDELDAAVPQHELLDNSINKTKIDLANRQLPSANGNSSTSNGAAVDLGQLSNGNLLKRSRSNSRSSDCTLDDTDEEEEREGSALNLAGAPVAHETISLSNGNSHLLANVNNLLQHHPPAMATVIATPSNGHLGTTTPILLNSTSSASSSSSNQSTAREAQINQLYAQVHKDPSKQQHQQQQQQQQQAQAVTTSIPSIFKNALGSPADNGLNDFHRGSMTTFGTGPATSSNRDLNSSYDSILGSNDKLAENDPAESWMYPSRRRVAPNGSKVPLPGSSFTDQLNQALSDRERRLGDGSSRHSSDDYTEINKSQSAAAINCKTLINEIRQAVNEAQPKVPWQQQHHQQIQQQPSAHTTGPPSPTSMSSGCSSPGYSPSRTLDLSGSSSSFSDRKAMAAGYTYKGGPVHEWTKDQVGHWLMGIELERYIPVFKENNVEGGALLTLDSKDFKTLGICGDDKHRLKKRLKDLKANIEKERKDMERERREREKAIRKAEKKAAKKK