wanglab/gogpt-training-data huggingface dataset:
Protein: D-amino-acid oxidase (DAAO) (DAMOX) (DAO) (EC 1.4.3.3) (P00371)
Organism: Sus scrofa (Pig)
Function: Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids.
Subcellular location: Peroxisome matrix {ECO:0000269|PubMed:33725110}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P14920}. Presynaptic active zone {ECO:0000250|UniProtKB:O35078}. Secreted {ECO:0000250|UniProtKB:P18894}. Note=Transiently present in the cytosol before being delivered to the peroxisomes (By similarity). In the cerebellum, a fraction of protein localizes to the presynaptic active zone, where its activity is regulated by protein BSN (By similarity). Secreted into the lumen of the small intestine (By similarity). {ECO:0000250|UniProtKB:O35078, ECO:0000250|UniProtKB:P14920, ECO:0000250|UniProtKB:P18894}.
Interaction partners:
- Glycine cleavage system P protein
- Sarcosine dehydrogenase, mitochondrial
- Serine hydroxymethyltransferase
- Serine hydroxymethyltransferase
- Alanine--glyoxylate aminotransferase
- trans-L-3-hydroxyproline dehydratase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Threonine aldolase 1
- FAD dependent oxidoreductase domain-containing protein
- 5-aminolevulinate synthase
Sequence:
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDVKVYADRFTPFTTTDVAAGLWQPYTSEPSNPQEANWNQQTFNYLLSHIGSPNAANMGLTPVSGYNLFREAVPDPYWKDMVLGFRKLTPRELDMFPDYRYGWFNTSLILEGRKYLQWLTERLTERGVKFFLRKVESFEEVARGGADVIINCTGVWAGVLQPDPLLQPGRGQIIKVDAPWLKNFIITHDLERGIYNSPYIIPGLQAVTLGGTFQVGNWNEINNIQDHNTIWEGCCRLEPTLKDAKIVGEYTGFRPVRPQVRLEREQLRFGSSNTEVIHNYGHGGYGLTIHWGCALEVAKLFGKVLEERNLLTMPPSHL
Protein: Acylglycerol kinase, mitochondrial (EC 2.7.1.107) (EC 2.7.1.138) (EC 2.7.1.94) (Multiple substrate lipid kinase) (A0A3B3ISY9)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
Sequence:
MDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPTQ
Protein: L-selectin (CD62 antigen-like family member L) (Leukocyte adhesion molecule 1) (LAM-1) (Leukocyte-endothelial cell adhesion molecule 1) (LECAM1) (Lymph node homing receptor) (Lymphocyte antigen 22) (Ly-22) (Lymphocyte surface MEL-14 antigen) (CD antigen CD62L) (P18337)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes. Promotes initial tethering and rolling of leukocytes in endothelia (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1693096, ECO:0000269|PubMed:2646713}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Hematopoietic progenitor cell antigen CD34
- P-selectin glycoprotein ligand 1
- Glycosylation-dependent cell adhesion molecule 1
- Mucosal addressin cell adhesion molecule 1
- Protein N-terminal asparagine amidohydrolase
- CD44 antigen
- P-selectin
- E-selectin
- Vascular cell adhesion protein 1
- C-C motif chemokine 19
Sequence:
MVFPWRCEGTYWGSRNILKLWVWTLLCCDFLIHHGTHCWTYHYSEKPMNWENARKFCKQNYTDLVAIQNKREIEYLENTLPKSPYYYWIGIRKIGKMWTWVGTNKTLTKEAENWGAGEPNNKKSKEDCVEIYIKRERDSGKWNDDACHKRKAALCYTASCQPGSCNGRGECVETINNHTCICDAGYYGPQCQYVVQCEPLEAPELGTMDCIHPLGNFSFQSKCAFNCSEGRELLGTAETQCGASGNWSSPEPICQVVQCEPLEAPELGTMDCIHPLGNFSFQSKCAFNCSEGRELLGTAETQCGASGNWSSPEPICQETNRSFSKIKEGDYNPLFIPVAVMVTAFSGLAFLIWLARRLKKGKKSQERMDDPY
Protein: ORF 75 (P88964)
Organism: Human herpesvirus 8 type M
Subcellular location: Virion tegument {ECO:0000256|ARBA:ARBA00004535}.
Interaction partners:
Sequence:
MAYDVTGLWLESDLTADEEAFVNFYTSRTGTLTLVPGGTGGYYLLWITFRRPPTSREERERRDVEIQTVLAVLSPLLGYPHVIRRSVPRGSERVVSFGYGPNMHHRPTTLSTELAVLLQELGLQEWARVEVGRHLVSKITQTLLEPHPPQFIRAFTQNTDLVPYEGLEVPEGPQPVARPHIEDDVIMQAVMISLGADLLPLAVQASTGDNYNVARYFVIPGRCTMERWPWNCARQAFGIHGAYTHVHSSVQRGIRGLGNLLFHSTLFPGGQTQGALTGLYATEPALGPRAHSRFRRIFAKGVQQAEMLQGAGVPTLGGFLKTVRTIATTPGNALAVCSISTTTSKECISLRRMIPQQTVVCLGRFEPTDGPDTYPNLYRDSSDNAVRILETLKLVQRLAKGPIFSGLNRSHDPAPVVRHLQALAPRTGLELFVSKLPDEVRTHLPADPAAGPDAVKAAVAEHFLNVYCSLVFAVVAESGAVPGDLGETPLEVLQRAARLCACQVTVLGRTSEHPGIRIVDDLTGETTRVFSVDQPSSTPPSPWLALSDGVRVSGHPEDVDWGLFATGSTIHQLLRHSTVGSKEFFTRHMDRCSNGLIAQQAGVGPLDIPVSDYHLVLHSSMLAERVAPRVPDTVEAITPSMANLLHKDFETWVKALPQELLPVPAWRGQAMAMGEQAYKMATNVSTGATYAITEALTNLMFSPVSKLQDVVLTGAVAWSPEDHQAGLLQECLFACKEFCRELGVALSISSAASSPTLSERHVRITQQQETVEVLPFNSVVFTSWAEVKGSRYRVTPDVKVEGNALVYLAVNQSCLIAGSTFEHNFLASRHPIPPLNPSTVASLFMLVKYLMSKRLIVSGHDIGDGGLLPSAIEMALAGCRGLQLSLPAHPNPLELMVSETPGALVEVPQVHLSEVLRAARDYRCVAHPLGTVGPEGQGNNVTVLQNETVVFQETLTSLQVSWTSFSDEMWNLVTPPLHPLEDMHRKDLGRLEHHLGSLRAMCLGSQLRLFSCPTSPRRVAALVLPGSSAPYALMAALQNTGFEVATVTVEELKRGQSLSGFSGLITCLRTGCQASYASARGWVLALCNDPTCASTLTEFLNRPDTFSICCGEVGFQLLVALGVVGRSESSPYTYGPTPPQRWAVNLETNVSKLYDSHWLNIQIPQNTKSVFLRVLRGTVLPSWAQGEYLGVRYEQDALEYILRQRGEITLTYHGNAADETLPARHYPRNPTGNSTVAGLTSSDGRHAALIIDPSLMFHPWQWQHVPPDLTPLSMSPWAMAFQSIYLWSVKKINDHH
Protein: Dynein regulatory complex protein 9 (IQ domain-containing protein G) (A3KQH2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes (By similarity). Binds calmodulin when cellular Ca(2+) levels are low and thereby contributes to the regulation of calcium and calmodulin-dependent protein kinase IV (camk4) activity; contributes to the regulation of camk4 signaling cascades. Plays a role in the regulation of definitive hematopoiesis via its effects on camk4.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q80W32}. Cell projection, cilium, flagellum {ECO:0000250|UniProtKB:Q80W32}. Cell projection, cilium {ECO:0000250|UniProtKB:Q80W32}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q80W32}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8HQ54}.
Interaction partners:
- Tubulin--tyrosine ligase-like protein 5
- Dynein regulatory complex subunit 3.
- T-complex-associated-testis-expressed 1.
- Dynein regulatory complex subunit 4
- F-box and leucine-rich repeat protein 13.
- Leishmanolysin-like peptidase
- Cilia- and flagella-associated protein 161
- Meiosis-specific nuclear structural protein 1
Sequence:
MTSVEELRACALLQDCADQLSVLGNIIRPGAETQQRTELHLKTAQLMAGSSLSNFSGELKSQKHFKIQQTLLASDNLAKVQKDRQFVSDVINALLEELQKKNNFQSLFSAVAEERKKKAELLDIINREEEGRRQIKKLQKQLLDIRKEKTEECERLEEEVAILKDQVQDMRVRTNQQGKFVKSCAEQLVYQESKHNSYKENELEDEVKMLQEKIEEEKNVHFETEAFLKQQHANLKQKLQYWIHRYEKDMEEKEQEITALQNKRNSSQTRIQDLSKKCKDMENVVIEDRIEKEHLRAQMEKEQREKNAATKIQAWWRGTLVRKGPRSKKADKSKKKDGKKGKKKRK
Protein: Peptidyl-prolyl cis-trans isomerase CYP21-4 (PPIase CYP21-4) (EC 5.2.1.8) (Cyclophilin of 21 kDa 4) (Cyclophilin-21-4) (Q9C835)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase CYP21-1
- ER membrane protein complex subunit 6
- Heptahelical transmembrane protein 4
- Peptidyl-prolyl cis-trans isomerase CYP18-2
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
- Protein IQ-DOMAIN 6
- At2g20330/F11A3.12
- At1g80930/F23A5_23
- Initiation factor eIF-4 gamma, MA3
Sequence:
MAKIKPQALLNQSKKKKGPSRISISTIIVCNLVVAVVILSLVTTYRHWSQRSRNTIEHETRSQRFEDTNTASGQKTYDLPGFADINTSKGLITVELFKEGSPEVVDKFLDLCQKDHFKGMPFQRVIKNYLVQAGHSPSSIPVEEWTAKGKLRGRLHIGPKHEAFMLGTPKNKGNNKDFELLITTAPIPDLNDQLIVFGRVLKGEDVVQEIEEVDTDEHFQPKSPIGITGVVLKLET
Protein: Metabotropic GABA-B receptor subtype 3, isoform H (X2J962)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MRIIQPVQGTRYGPWPAVGLRLVLALAWATSAAAAMESSAELQALGYEAIRPGAASISTSSPSSSPPGESASTVTAGGTPIPPRSDWKYKRTKVKRRQQRLNSHSNLPGSTNASHAHHLLNLPPRQRYLKVNQVFESERRMSPAEMQRNHGKIVLLGLFELSTSRGPRPDGLSELGAATMAVEHINRKRLLPGYTLELVTNDTQCDPGVGVDRFFHAIYTQPSTRMVMLLGSACSEVTESLAKVVPYWNIVQVSFGSTSPALSDRREFPYFYRTVAPDSSHNPARIAFIRKFGWGTVTTFSQNEEVHSLAVNNLVTELEAANISCAATITFAATDFKEQLLLLRETDTRIIIGSFSQELAPQILCEAYRLRMFGADYAWILHESMGAPWWPDQRTACSNHELQLAVENLIVVSTHNSIVGNNVSYSGLRRLSCPSRCPVLSVLLCVSEMK
Protein: Isopenicillin N synthase (IPNS) (EC 1.21.3.1) (Isopenicillin cyclase) (Penicillin biosynthetis cluster protein ipnA) (P08703)
Organism: Penicillium chrysogenum (Penicillium notatum)
Function: Isopenicillin N synthase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. IpnA catalyzes the cyclization of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) to form isopenicillin N (IPN) that contains the beta-lactam nucleus. The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase aatA to yield penicillin in the peroxisomal matrix (Probable).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:12223189, ECO:0000269|PubMed:1899377}.
Interaction partners:
Sequence:
MASTPKANVPKIDVSPLFGDNMEEKMKVARAIDAASRDTGFFYAVNHGVDVKRLSNKTREFHFSITDEEKWDLAIRAYNKEHQDQIRAGYYLSIPEKKAVESFCYLNPNFKPDHPLIQSKTPTHEVNVWPDEKKHPGFREFAEQYYWDVFGLSSALLRGYALALGKEEDFFSRHFKKEDALSSVVLIRYPYLNPIPPAAIKTAEDGTKLSFEWHEDVSLITVLYQSDVANLQVEMPQGYLDIEADDNAYLVNCGSYMAHITNNYYPAPIHRVKWVNEERQSLPFFVNLGFNDTVQPWDPSKEDGKTDQRPISYGDYLQNGLVSLINKNGQT
Protein: Meiosis expressed gene 1 protein homolog (Q5JSS6)
Organism: Homo sapiens (Human)
Function: Essential for spermiogenesis.
Interaction partners:
- Parkin coregulated gene protein
- Sperm-associated antigen 6
- Sperm-associated antigen 16 protein
- PACRG-like protein
Sequence:
MASSDVKPKSVSHAKKWSEEIENLYRFQQAGYRDETEYRQVKQVSMVDRWPETGYVKKLQRRDNTFYYYNKQRECDDKEVHKVKIYAY
Protein: Protein YIP4a (YPT/RAB GTPase-interacting protein 4a) (YIP4a) (O64614)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with YIP4B, involved in the regulation of cell elongation during root and hypocotyl growth. YIP4A and YIP4B are central trafficking components in Rho-of-plant (ROPs, e.g. ARAC4/ROP2, ARAC5/ROP4 and ARAC3/ROP6) small GTPases-dependent root hair formation, thus contributing to activation and plasma membrane accumulation of ROPs during hair initiation. The ECH/YIP4 complex is involved in the modulation of the trans-Golgi network (TGN)-mediated trafficking of some proteins and cell wall components (e.g. pectin and hemicellulose) to the cell wall in dark-grown hypocotyls and in secretory cells of the seed coat.
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23832588}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Golgi apparatus membrane protein-like protein ECHIDNA
- Protein YIP
- Ras-related protein RABA5c
- Syntaxin-61
- PRA1 family protein B6
- Guanosine nucleotide diphosphate dissociation inhibitor 1
- V-type proton ATPase subunit a1
- PRA1 family protein B3
- Ras-related protein RABA1b
- Ras-related protein RABA1a
Sequence:
MSQGDTVPLHPSSQSDIDEIENLINESVQSGPGTVLAARPPSPTRPSIPVSSSSSSSPFMQSNLPPLHPSSSAQKVTHVPVPPPLPAVSNSSNFQGASAFGSPPNTLTEPVWDTVKRDLSRIVSNLKLVVFPNPYREDPGKALRDWDLWGPFFFIVFLGLTLSWSASVKKSEVFAVAFALLAAGAVILTLNVLLLGGHIIFFQSLSLLGYCLFPLDVGAVICMLKDNVILKMVVVSVTLAWSSWAAYPFMSSAVNPRRKALALYPVFLMYVSVGFLIIAIN
Protein: Serpin B5 (Maspin) (Peptidase inhibitor 5) (PI-5) (P36952)
Organism: Homo sapiens (Human)
Function: Tumor suppressor. It blocks the growth, invasion, and metastatic properties of mammary tumors. As it does not undergo the S (stressed) to R (relaxed) conformational transition characteristic of active serpins, it exhibits no serine protease inhibitory activity.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- 14-3-3 protein sigma
- Histone deacetylase 1
- Cellular tumor antigen p53
Sequence:
MDALQLANSAFAVDLFKQLCEKEPLGNVLFSPICLSTSLSLAQVGAKGDTANEIGQVLHFENVKDVPFGFQTVTSDVNKLSSFYSLKLIKRLYVDKSLNLSTEFISSTKRPYAKELETVDFKDKLEETKGQINNSIKDLTDGHFENILADNSVNDQTKILVVNAAYFVGKWMKKFSESETKECPFRVNKTDTKPVQMMNMEATFCMGNIDSINCKIIELPFQNKHLSMFILLPKDVEDESTGLEKIEKQLNSESLSQWTNPSTMANAKVKLSIPKFKVEKMIDPKACLENLGLKHIFSEDTSDFSGMSETKGVALSNVIHKVCLEITEDGGDSIEVPGARILQHKDELNADHPFIYIIRHNKTRNIIFFGKFCSP
Protein: Inositol 3-kinase (EC 2.7.1.64) (Myo-inositol kinase) (OsMIK) (Protein LOW PHYTIC ACID) (Q84R36)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Kinase that phosphorylates myo-inositol to produce multiple myo-inositol monophosphates. Participates in phytic acid biosynthesis in developing seeds. Phytic acid is the primary storage form of phosphorus in cereal grains and other plant seeds.
Interaction partners:
- Inositol-3-phosphate synthase 1
- Inositol-3-phosphate synthase 1
- Inositol-1-monophosphatase
- Os06g0492000 protein
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Os09g0322900 protein
- histidinol-phosphatase
- Inositol-1-monophosphatase
- Os06g0258900 protein
- Os02g0467700 protein
Sequence:
MAPSPAAAMPLAAEPDEVVVEVEEEEERGVKGGGGVAGLDEVEGLVVGSYCHDVLLRGGRVVGETLGGAAAFVSNVLDAASPAGASLAVVSKVGHDFAYATAAAPARHPPVLCASPTTSFHARFSDDAASAHAPDRQLRRVHACDPIYPADLPDRRFAYGLAVGVAGEVLPETLERMIRLCRAVLVDAQALIRAFDGEAKGGGAVRHVALEATPYARLLPRVAFLKASSEEAPYVGVETARRRCCVIVTEGRDGCRLYWDGGEARVAPFPAVQVDPTGAGDSFLAGFASGLLWGLSATDAALLGNFFGAAAVSQVGVPTFDPKMLQAVKQILEKAVKRPCTHINGNTFTFQRSSMHDELHKSLQEAAMLVCEQKQANSPATDNGDVCSINELTSLPS
Protein: Serine/threonine-protein kinase TAO3 (EC 2.7.11.1) (Thousand and one amino acid protein 3) (E1BHE1)
Organism: Bos taurus (Bovine)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MRKGVPRDPEIADLFYKDDPEELFIGLHEIGHGSFGAVYFKWQDILKEVKFLQQLRHPNTIEYKGCYLKEHTAWLVMEYCLGSASDLLEVHKKPLQEMEIAAITHGALQGLAYLHSHALIHRDIKAGNILLTEPGQVKLADFGSASMASPANSFVGTPYWMAPEVILAMDEGQYDGKVDIWSLGITCIEMAERKPPLFNMNAMSALYHIAQNDSPTLQSNEWTDSFRRFVDYCLQKMPQERPTSAELLRHDFVRRDRPLRVLIDLIQRTKDAVRELDNLQYRKMKKILFQETRNGPLNESQEDEEDSEHGTSLSRELDSLGSNHSIPSMSVSTGSQGSSVNSMQEVMDDSSSELVMMHDDESPVNSTPSVVHKKDHVFIRDEAGHGDPRPEPRPTQSVQSQALHYRNRERFATIKSASLVTRQIHEHEQENELREQMSGYKRMRRQHQKQLIALENKLKAEMDEHRLKLQKEVETHANNSSIELEKLAKKQVAIIEKEAKVAAADEKKFQQQILAQQKKDLTTFLESQKKQYKICKEKIKEEMNEDHSTPKKEKQERISKHKENLQHTQAEEEAHLLTQQRLYYDKNCRFFKRKIMIKRHEVEQQNIREELNKKRTQKEMEHAMLIRHDESTRELEYRQLHTLQKLRMDLIRLQHQTELENQLEYNKRRERELHRKHVMELRQQPKNLKAMEMQIKKQFQDTCKVQTKQYKALKNHQLEVTPKNEHKTILKTLKDEQTRKLAILAEQYEQSINEMMASQALRLDEAQEAECQALRLQLQQEMELLNAYQSKIKMQTEAQHERELQKLEQRVSLRRAHLEQKIEEELAALQKERSERIKYLLERQEREIETFDMESLRMGFGNLVTLDFPKEDYR
Protein: Guanidinoacetate N-methyltransferase (EC 2.1.1.2) (O35969)
Organism: Mus musculus (Mouse)
Function: Converts guanidinoacetate to creatine, using S-adenosylmethionine as the methyl donor. Important in nervous system development.
Subcellular location: Cell projection, microvillus {ECO:0000269|PubMed:8312439}. Note=Detected in microvilli of the epithelial cells lining the caput epididymis.
Interaction partners:
- Glycine amidinotransferase, mitochondrial
- Methyl-CpG-binding protein 2
- Sodium- and chloride-dependent creatine transporter 1
- Phosphatidylethanolamine N-methyltransferase
- Ribosome biogenesis protein BRX1 homolog
- Ribosome production factor 2 homolog
- GTP-binding protein 4
Sequence:
MSSSAASPLFAPGEDCGPAWRAAPAAYDASDTHLQILGKPVMERWETPYMHALAAAAASRGGRVLEVGFGMAIAASRVQQAPIEEHWIIECNDGVFQRLQDWALRQPHKVVPLKGLWEEVAPTLPDGHFDGILYDTYPLSEEAWHTHQFNFIKNHAFRLLKTGGVLTYCNLTSWGELMKSKYTDITTMFEETQVPALQEAGFLKENICTEVMALVPPADCRYYAFPQMITPLVTKH
Protein: Gingipain R2 (EC 3.4.22.37) (Arg-gingipain) (Gingipain 2) (RGP-2) (P95493)
Organism: Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Function: Thiol protease. Acts synergistically with RgpA to catalyze the maturation of fimbrial subunits, such as FimA (By similarity). Its proteolytic activity is a major factor in both periodontal tissue destruction and in evasion of host defense mechanisms (Probable).
Subcellular location: Secreted {ECO:0000269|PubMed:9705298}.
Interaction partners:
- Protease PrtH
- Peptidylarginine deiminase
- Uncharacterized protein
- Zinc carboxypeptidase, putative
- Uncharacterized protein
Sequence:
MKKNFSRIVSIVAFSSLLGGMAFAQPAERGRNPQVRLLSAEQSMSKVQFRMDNLQFTGVQTSKGVAQVPTFTEGVNISEKGTPILPILSRSLAVSETRAMKVEVVSSKFIEKKDVLIAPSKGVISRAENPDQIPYVYGQSYNEDKFFPGEIATLSDPFILRDVRGQVVNFAPLQYNPVTKTLRIYTEIVVAVSETAEAGQNTISLVKNSTFTGFEDIYKSVFMNYEATRYTPVEEKENGRMIVIVPKKYEEDIEDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNDLTYVLLVGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDLKTQIDRTIHYERNITTEDKWLGQALCIASAEGGPSADNGESDIQHENIIANLLTQYGYTKIIKCYDPGVTPKNIIDAFNGGISLANYTGHGSETAWGTSHFGTTHVKQLTNSNQLPFIFDVACVNGDFLYNVPCFAEALMRAQKDGKPTGTVAIIASTINQSWASPMRGQDEMNEILCEKHPNNIKRTFGGVTMNGMFAMVEKYKKDGEKMLDTWTVFGDPSLLVRTLVPTKMQVTAPANISASAQTFEVACDYNGAIATLSDDGDMVGTAIVKDGKAIIKLNESIADETNLTLTVVGYNKVTVIKDVKVEGTSIADVANDKPYTVAVSGKTITVESPAAGLTIFDMNGRRVATAKNRMVFEAQNGVYAVRIATEGKTYTEKVIVK
Protein: Plasmolipin (Plasma membrane proteolipid) (Q9Y342)
Organism: Homo sapiens (Human)
Function: Appears to be involved in myelination. Could also participate in ion transport events as addition of plasmolipin to lipid bilayers induces the formation of ion channels, which are voltage-dependent and K(+)-selective (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26002055}; Multi-pass membrane protein {ECO:0000255}. Myelin membrane {ECO:0000269|PubMed:26002055}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P47987}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus {ECO:0000269|PubMed:26002055}. Note=In polarized cells, localized predominantly in the apical membrane (By similarity). Located in lipid raft (By similarity). Recycled between the plasma membrane and the Golgi complex (PubMed:26002055). PLLP is continuously recirculating in the cell (PubMed:26002055). {ECO:0000250|UniProtKB:A3KQ86, ECO:0000250|UniProtKB:P47987, ECO:0000269|PubMed:26002055}.
Interaction partners:
- Myeloid-associated differentiation marker
- Chemokine-like factor
- Myelin proteolipid protein
Sequence:
MAEFPSKVSTRTSSPAQGAEASVSALRPDLGFVRSRLGALMLLQLVLGLLVWALIADTPYHLYPAYGWVMFVAVFLWLVTIVLFNLYLFQLHMKLYMVPWPLVLMIFNISATVLYITAFIACSAAVDLTSLRGTRPYNQRAAASFFACLVMIAYGVSAFFSYQAWRGVGSNAATSQMAGGYA
Protein: Chaperone protein DNAJ, putative (Q389A5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEDAKYRTFPAKVLLACDERIHQFIDASIYNDWNAAVQEWREQKQARVSLQRQKPPEPKGEYAPGNKLTQFSDEEFLKLTQQLEEITSAIAGPSAALPGPTFSDGGDGAGSNDCCHSGAKHDLYTLDSSMYSASLDDKQLSLCQKAAELYKVGDYSEAARNFSAVIDSCLPTVLNAAMVSNRAMCYLCCGSYRCSLRDAIRSCEMNNQYVLGARRAVRIHICCGKCSEARGLIDTYSKTCGHGFEEELANITLYENSTALFDRNEHATALKQLNELLKRAPCAPFEALKVQLVAVELGSRAALLHAEECLRRYPNFPELMYWNVQLRFLECSNESELVAILSLSRVSASADCAARFRQVNSRIQQCIDLCRELEKTSAAKNWPQLVELCTKALQRPFIGDRLRAAVLSQRAQALYHSGCLYECVDDLDVALRNVEGVRDRAELLLLKALCEEKLSRWTDAMHSVERSMREERLPAAVDMWRRLKGRKKTSDQRERQGEKKEEERKWTKPVAPTSLAQLYSRLALPDGAGAEKVRKSYRALAMKWHPDKWCSASAQEQKEAEEKFKLVKAAYDQLIGIIVD
Protein: SIT4-associating protein SAP4 (P53036)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Associates with the SIT4 phosphatase in a cell cycle dependent manner. May be directly or indirectly involved in SIT4-dependent functions in budding and in normal G1 cyclin expression (By similarity).
Interaction partners:
- Serine/threonine-protein phosphatase PP1-1
- SIT4-associating protein SAP185
- SIT4-associating protein SAP190
- SIT4-associating protein SAP155
- Uncharacterized protein YGL230C
- Serine/threonine-protein phosphatase PP2A-like PPG1
- Type 2A phosphatase-associated protein 42
Sequence:
MSLWPFGETLSHSGIDSILEEYYLIFRSLEGNETSSTDDKKNEPSMESESEFGTESRDRSDLNQSFIDRILLETALLDELNGAANDRLVDFICLGYFYDDRSQQVRHMDYLVDMLMAYLKDIDRTGYRTPFLLENSFHQTGEYEDQDDEDPMLYVNIISSIFCSKSAPIVEALVQNTPFLSSLFEVFQFENIEAENCPILAVFLKINETLLFEQTSSYLEFFKSQPNIVDKFLYHIEVSPLVEFLIKIMLTDQVESPTNIIDFLYHQDLIPKCLNLLENSKYSPGIQNSSGELLKALISISTNFKLDTLWIGPNRLTRQLASPQYVDQLINIILFQRGHAMGVAVSIIIELIRKNNSDYDEVDLLSTTIVDNPPSQRDPVYLGHLLYELTMHMEDFYALLIKLENDDDDDHDTASKALPSVKHHLLENQLHESFRPLGFERVKITELISEMLHCSNMGLMNSKRGEKIARTRDKCRDTLDQNSLEKAMKNLNINDNTITSNTLEDKCNNNDSNDSNDNQKQKKNIKKKFHDNELYSTFDTSDDNIDDDDDMSFEIPYVSETQNLKIRKNPTIGDLFKIKLHDLGFFPKFLQLFLRYPWNNFWHNIVFDIIQQIFNGRMDFSYNSFLVYSLFDFKKSTRFIPKPLYGSNQKLPVKDFHIISDFILQGHKDSFEFYEKEKTNLGYMGQLVLIAEEIAKYSKIYKTDLIAPDIYAFLQDEVWMSYSSDILNETRTMCSIILGGGQFCAESDENTNQDFLEKADMSKPAHPSTMDENEIVHEEDVKLHDKVAELIDELGQLTELDIHDKIKDVIVDHHSDLN
Protein: FH1/FH2 domain-containing protein 1 (Formin homolog overexpressed in spleen 1) (FHOS) (Formin homology 2 domain-containing protein 1) (Q9Y613)
Organism: Homo sapiens (Human)
Function: Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton. Cell projection, bleb. Note=Predominantly cytoplasmic.
Interaction partners:
- Nesprin-2
- Nesprin-1
- Rho-associated protein kinase 2
Sequence:
MAGGEDRGDGEPVSVVTVRVQYLEDTDPFACANFPEPRRAPTCSLDGALPLGAQIPAVHRLLGAPLKLEDCALQVSPSGYYLDTELSLEEQREMLEGFYEEISKGRKPTLILRTQLSVRVNAILEKLYSSSGPELRRSLFSLKQIFQEDKDLVPEFVHSEGLSCLIRVGAAADHNYQSYILRALGQLMLFVDGMLGVVAHSDTIQWLYTLCASLSRLVVKTALKLLLVFVEYSENNAPLFIRAVNSVASTTGAPPWANLVSILEEKNGADPELLVYTVTLINKTLAALPDQDSFYDVTDALEQQGMEALVQRHLGTAGTDVDLRTQLVLYENALKLEDGDIEEAPGAGGRRERRKPSSEEGKRSRRSLEGGGCPARAPEPGPTGPASPVGPTSSTGPALLTGPASSPVGPPSGLQASVNLFPTISVAPSADTSSERSIYKARFLENVAAAETEKQVALAQGRAETLAGAMPNEAGGHPDARQLWDSPETAPAARTPQSPAPCVLLRAQRSLAPEPKEPLIPASPKAEPIWELPTRAPRLSIGDLDFSDLGEDEDQDMLNVESVEAGKDIPAPSPPLPLLSGVPPPPPLPPPPPIKGPFPPPPPLPLAAPLPHSVPDSSALPTKRKTVKLFWRELKLAGGHGVSASRFGPCATLWASLDPVSVDTARLEHLFESRAKEVLPSKKAGEGRRTMTTVLDPKRSNAINIGLTTLPPVHVIKAALLNFDEFAVSKDGIEKLLTMMPTEEERQKIEEAQLANPDIPLGPAENFLMTLASIGGLAARLQLWAFKLDYDSMEREIAEPLFDLKVGMEQLVQNATFRCILATLLAVGNFLNGSQSSGFELSYLEKVSEVKDTVRRQSLLHHLCSLVLQTRPESSDLYSEIPALTRCAKVDFEQLTENLGQLERRSRAAEESLRSLAKHELAPALRARLTHFLDQCARRVAMLRIVHRRVCNRFHAFLLYLGYTPQAAREVRIMQFCHTLREFALEYRTCRERVLQQQQKQATYRERNKTRGRMITETEKFSGVAGEAPSNPSVPVAVSSGPGRGDADSHASMKSLLTSRPEDTTHNRRSRGMVQSSSPIMPTVGPSTASPEEPPGSSLPSDTSDEIMDLLVQSVTKSSPRALAARERKRSRGNRKSLRRTLKSGLGDDLVQALGLSKGPGLEV