wanglab/gogpt-training-data huggingface dataset:
Protein: Keratin-associated protein, putative (DUF819) (Similarity to unknown protein) (Q9LTG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein At5g13720)
- Plastid transcriptionally active 18
- Proline-rich receptor-like protein kinase PERK15
- At5g62720
- AT5g24690/MXC17_8)
- Plastidal glycolate/glycerate translocator 1, chloroplastic
- Dicarboxylate transporter 2.2, chloroplastic
- Protein high chlorophyll fluorescent 107
- A-kinase anchor-like protein
- 1-acyl-sn-glycerol-3-phosphate acyltransferase LPAT1, chloroplastic
Sequence:
MATSLPLLNVIGNSLPSSSRLFRRRSYIVSRQDLPEFSAKSTSSRLSFSPASLSQFRNGTDRFLSPESSSPIRSVTVSSLSTPLISPNDEWGTWTALFATGALGLWSEKTKVGAAMSGALVSTLVGLAASNLGIISSQAPAFAVVLNFLLPLAVPLLLFRADLRRVVQSTGKLLLAFLIGSVATTVGTALAYYLVPMKSLGPDSWKIAAALMGRHIGGAVNYVAISNALGVTPSVLAAGLAADNVICAVYFTTLFALGSKIPAEAVPPPTTIVDAETNEASETKNKIPVLLIATGIAVSLAICKAGALLTKYFGISGGSLPAITAVVVILATVFPSQFGRLAPSGEAMALILMQVFFTVVGASGNIWSVINTAPSIFLFALVQIGTHLAVILGIGKLLNIELRLLLLASNANVGGPTTAAGMATAKGWNSLIVPGILAGIFGIAIATFIGIAFGVKVLKFM
Protein: Cytochrome c oxidase subunit ApiCOX26, putative (Q8IL73)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MLIFQNAQHYFNFFRNFNGCYTDNKLLKFFFKKSYNNWFNDPSQYNYYFISYYAVALSMCIILRNLLFNPDVHFRRQDKRRNIIDRYQHHAYSLPYFNHWLRNFSQSFKSSLIDNEPDYQDVDPWSFRPNRIQFYGRFPFFFEIPKYHIDDPTFDKNSYKYMQNYYEEIGYVQKPENMRV
Protein: Cytochrome c oxidase subunit 5B, mitochondrial (Cytochrome c oxidase polypeptide Vb) (A0A384NL93)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
Sequence:
MASRLLRGAGTLAAQALRARGPSGAAAMRSMASGGGVPTDEEQATGLEREIMLAAKKGLDPYNVLAPKGASGTREDPNLVPSISNKRIVGCICEEDNTSVVWFWLHKGEAQRCPRCGAHYKLVPQQLAH
Protein: Phosphoacetylglucosamine mutase (PAGM) (EC 5.4.2.3) (Acetylglucosamine phosphomutase) (N-acetylglucosamine-phosphate mutase) (Phosphoglucomutase-3) (PGM 3) (O95394)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation.
Interaction partners:
- Glucosamine 6-phosphate N-acetyltransferase
- UDP-N-acetylhexosamine pyrophosphorylase
- UDP-N-acetylhexosamine pyrophosphorylase-like protein 1
- N-acetyl-D-glucosamine kinase
- N-acetylglucosamine-6-phosphate deacetylase
- Phosphoglucomutase-1
- Phosphoglucomutase-like protein 5
- Glutamine--fructose-6-phosphate aminotransferase 1
- Phosphopentomutase
- Immunoglobulin lambda-like polypeptide 1
Sequence:
MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQDMQRVLIDISEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKATIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKGKLNHLCGADFVKSHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELLVEIGESLNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKQSAEQLEDKKRKAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGIGERPQPGF
Protein: Berberine bridge enzyme-like 9 (AtBBE-like 9) (EC 1.1.1.-) (Q9SA86)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:18796151}.
Interaction partners:
- rhamnogalacturonan endolyase
- Glycoside hydrolase family 28 protein / polygalacturonase
- Pectin lyase-like superfamily protein
- Peroxidase 43
- Peroxidase 36
- Peroxidase 69
- Aspartyl protease family protein At5g10770
- Peroxidase 33
- Probable xyloglucan endotransglucosylase/hydrolase protein 33
Sequence:
MTSLTTQTLIITIFLLTIPTSFASPPSLEDVFAQCVTDFKPSNPKSPIQNYIYTQRSPNFLTILNNYVRNLRYFNNMTRKPVAIVAAADVTHIQATITCAKKLGLQLRIRSGGHDYDGMSYLSTIDFVVLDMFNLRSINIDPKLDTAWVQSGATLGEIYYGVANKSNDLRGFPAGICPGLGAGGHFSGGGYGNMMRKYGLSIDNIIDAKIVDAKGRVLDRSSMGEDLFWALRGGGAASFCVVLAWKIKLVPVPAKVTVFNIETFGNTGSVNTTELVAKWQEIADKIDNDLFIRLTLGSSNKTVKASFMGMYLGNSSNLLEIMNAKFPELGLIKRECIEMKWIESVLFWLGIPPGTAPTTSMLNRIPQKQIYLKRKSDYVQKPISRTGLESIFKIMTENENVTMAFNPYGGRMSEIPSTETAFPHRAGNMFKIQYAANWFVPGEAVAKDCLSQTERLFEAMSPYVSKNPREAFLNYRDVDIGKSLNSTYEEGKVYGFKYFKDNFEKLVKIKSRVDPDNFFRYEQSIPVLSSH
Protein: Zinc finger protein 628 (Q5EBL2)
Organism: Homo sapiens (Human)
Function: Transcriptional activator. Binds DNA on GT-box consensus sequence 5'-TTGGTT-3'. Plays a role in spermiogenesis.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MSGVMVGSHADMAPASTAEGAGEKPGPAAPAPAAQYECGECGKSFRWSSRLLHHQRTHTGERPYKCPDCPKAFKGSSALLYHQRGHTGERPYQCPDCPKAFKRSSLLQIHRSVHTGLRAFICGQCGLAFKWSSHYQYHLRQHTGERPYPCPDCPKAFKNSSSLRRHRHVHTGERPYTCGVCGKSFTQSTNLRQHQRVHTGERPFRCPLCPKTFTHSSNLLLHQRTHGAAPAPGTASAAPPPQSREPGKVFVCDAYLQRHLQPHSPPAPPAPPPPPPPVVPELFLAAAETTVELVYRCDGCEQGFSSEELLLEHQPCPGPDAAPQPQEAPAEAPKADQPPSPLPQPPPPAAAPAPGFACLPCGKSFRTVAGLSRHQHSHGAAGGQAFRCGSCDGSFPQLASLLAHQQCHVEEAAAGRPPPQAEAAEVTCPQEPLAPAAPVPPPPPSAPASAERPYKCAECGKSFKGSSGLRYHLRDHTGERPYQCGECGKAFKRSSLLAIHQRVHTGLRAFTCGQCGLTFKWSSHYQYHLRLHSGERPYACGECGKAFRNTSCLRRHRHVHTGERPHACGVCGKSFAQTSNLRQHQRVHTGERPFRCPLCPKTFTHSSNLLLHQRTHSAERPFTCPICGRGFVMAAYLQRHLRTHAPANTPPSTTAPAAGPQPPAPLAAARAPPATQDVHVLPHLQATLSLEVAGGTAQAPSLGPAAPNSQTFLLVQTAQGLQLIPSSVQPPTPPPPPAPPKLILLPSSSAGAGGGRARQGPRAVGKAGQGAGVVWLPGPGGLGVQGAASAGASGTGQSLIVLQNVGGGEAGPQEMSGVQLQPLRPAPEVTTVQLQPAQEVTTVQLQPAQEVTTVQLQPAQEVTTVQLQPVAGQLSNSSGGAVATEAPNLLVVQSGAAEELLTGPGPGEAGDGEASTGVVQDVLFETLQTDEGLQSVLVLSGADGEQTRLCVQEVETLPPGLTEPPATGPPGQKLLIIRSAPATELLDSSNTGGGTATLQLLAPPPSGPASGPAGLPGAPASQMVQVVPAGAGPGVMTPQGLPSIQIVQTLPAVQLVHTF
Protein: Snake venom metalloproteinase leucurolysin-A (Leuc-A) (SVMP) (EC 3.4.24.-) (P84907)
Organism: Bothrops leucurus (Whitetail lancehead)
Function: Non-hemorrhagic metalloproteinase that hydrolyzes the alpha chains of fibrinogen, as well as fibrin, fibronectin and casein. Beta and gamma chains are also hydrolyzed, but more slowly. Thrombolytic activity is also observed. Induces detachment of endothelial cells followed by death, and inhibits endothelial cell adhesion to fibronectin. Induces edema in mouse paw. Inhibits ADP-induced platelet aggregation on human platelet-rich plasma with an IC(50) of 2.8 uM.
Subcellular location: Secreted {ECO:0000269|PubMed:16139412}.
Interaction partners:
Sequence:
QQFSPRYIELVVVADHGMFKKYNSNLNTIRKWVHEMLNTVNGFFRSMNVDASLVNLEVWSKKDLIKVEKDSSKTLTSFGEWRERDLLPRISHDHAQLLTVIFLDEETIGIAYTAGMCDLSQSVAVVMDHSKKNLRVAVTMAHELGHNLGMRHDGNQCHCNAPSCIMADTLSKGLSFEFSDCSQNQYQTYLTKHNPQCILNKP
Protein: Actin filament-associated protein 1 (110 kDa actin filament-associated protein) (AFAP-110) (Q8N556)
Organism: Homo sapiens (Human)
Function: Can cross-link actin filaments into both network and bundle structures (By similarity). May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton. Seems to play a role in the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells.
Subcellular location: Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:15485829}.
Interaction partners:
- Proto-oncogene tyrosine-protein kinase Src
Sequence:
MEELIVELRLFLELLDHEYLTSTVREKKAVITNILLRIQSSKGFDVKDHAQKQETANSLPAPPQMPLPEIPQPWLPPDSGPPPLPTSSLPEGYYEEAVPLSPGKAPEYITSNYDSDAMSSSYESYDEEEEDGKGKKTRHQWPSEEASMDLVKDAKICAFLLRKKRFGQWTKLLCVIKDTKLLCYKSSKDQQPQMELPLQGCNITYIPKDSKKKKHELKITQQGTDPLVLAVQSKEQAEQWLKVIKEAYSGCSGPVDSECPPPPSSPVHKAELEKKLSSERPSSDGEGVVENGITTCNGKEQVKRKKSSKSEAKGTVSKVTGKKITKIISLGKKKPSTDEQTSSAEEDVPTCGYLNVLSNSRWRERWCRVKDNKLIFHKDRTDLKTHIVSIPLRGCEVIPGLDSKHPLTFRLLRNGQEVAVLEASSSEDMGRWIGILLAETGSSTDPEALHYDYIDVEMSASVIQTAKQTFCFMNRRVISANPYLGGTSNGYAHPSGTALHYDDVPCINGSLKGKKPPVASNGVTGKGKTLSSQPKKADPAAVVKRTGSNAAQYKYGKNRVEADAKRLQTKEEELLKRKEALRNRLAQLRKERKDLRAAIEVNAGRKPQAILEEKLKQLEEECRQKEAERVSLELELTEVKESLKKALAGGVTLGLAIEPKSGTSSPQSPVFRHRTLENSPISSCDTSDTEGPVPVNSAAVLKKSQAAPGSSPCRGHVLRKAKEWELKNGT
Protein: E3 ubiquitin-protein ligase COP1 (EC 2.3.2.27) (Constitutive photomorphogenesis protein 1 homolog) (mCOP1) (RING finger and WD repeat domain protein 2) (RING-type E3 ubiquitin transferase RFWD2) (Q9R1A8)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in JUN ubiquitination and degradation. Directly involved in p53 (TP53) ubiquitination and degradation, thereby abolishing p53-dependent transcription and apoptosis. Ubiquitinates p53 independently of MDM2 or RCHY1. Probably mediates E3 ubiquitin ligase activity by functioning as the essential RING domain subunit of larger E3 complexes. In contrast, it does not constitute the catalytic RING subunit in the DCX DET1-COP1 complex that negatively regulates JUN, the ubiquitin ligase activity being mediated by RBX1. Involved in 14-3-3 protein sigma/SFN ubiquitination and proteasomal degradation, leading to AKT activation and promotion of cell survival. Ubiquitinates MTA1 leading to its proteasomal degradation. Upon binding to TRIB1, ubiquitinates CEBPA, which lacks a canonical COP1-binding motif.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:10395541}. Cytoplasm {ECO:0000269|PubMed:10395541}. Note=In the nucleus, it forms nuclear speckles.
Interaction partners:
- DET1 homolog
- DNA damage-binding protein 1
- DNA damage-binding protein 2
- Cullin-4A
- E3 ubiquitin-protein ligase RBX1
- Cellular tumor antigen p53
- DNA excision repair protein ERCC-8
- Cullin-4B
- Tribbles homolog 3
- Tribbles homolog 2
Sequence:
MSGSRQAGSGSAGTSPGSSAASSVTSASSSLSSSPSPPSVAASAATLVSGGVAPAAGSGGLGGPGRPVLVAAAVSGSASAGGAVSAGQSRLSCAARPSAGVGGSSSSLGSSSRKRPLLVPLCNGLLNSYEDKSNDFVCPICFDMIEEAYMTKCGHSFCYKCIHQSLEDNNRCPKCNYVVDNIDHLYPNFLVNELILKQKQRFEEKRFKLDHSVSSTNGHRWQIFQDLLGTDQDNLDLANVNLMLELLVQKKKQLEAESHAAQLQILMEFLKVARRNKREQLEQIQKELSVLEEDIKRVEEMSGLYSPVSEDSTVPQFEAPSPSHSSIIDSTEYSQPPGFSGTSQTKKQPWYNSTLASRRKRLTAHFEDLEQCYFSTRMSRISDDSRTASQLDEFQECLSKFTRYNSVRPLATLSYASDLYNGSSIVSSIEFDRDCDYFAIAGVTKKIKVYEYGTVIQDAVDIHYPENEMTCNSKISCISWSSYHKNLLASSDYEGTVILWDGFTGQRSKVYQEHEKRCWSVDFNLMDPKLLASGSDDAKVKLWSTNLDNSVASIEAKANVCCVKFSPSSRYHLAFGCADHCVHYYDLRNTKQPIMVFKGHRKAVSYAKFVSGEEIVSASTDSQLKLWNVGKPYCLRSFKGHINEKNFVGLASNGDYIACGSENNSLYLYYKGLSKTLLTFKFDTVKSVLDKDRKEDDTNEFVSAVCWRALSDGESNVLIAANSQGTIKVLELV
Protein: Serine/Arginine-related protein 53 (SRrp53) (Arginine/serine-rich coiled-coil protein 1) (Q96IZ7)
Organism: Homo sapiens (Human)
Function: Has a role in alternative splicing and transcription regulation. Involved in both constitutive and alternative pre-mRNA splicing. May have a role in the recognition of the 3' splice site during the second step of splicing.
Subcellular location: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Shuttles between the nucleus and cytoplasm. {ECO:0000250}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein eS8
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein uL5
Sequence:
MGRRSSDTEEESRSKRKKKHRRRSSSSSSSDSRTYSRKKGGRKSRSKSRSWSRDLQPRSHSYDRRRRHRSSSSSSYGSRRKRSRSRSRGRGKSYRVQRSRSKSRTRRSRSRPRLRSHSRSSERSSHRRTRSRSRDRERRKGRDKEKREKEKDKGKDKELHNIKRGESGNIKAGLEHLPPAEQAKARLQLVLEAAAKADEALKAKERNEEEAKRRKEEDQATLVEQVKRVKEIEAIESDSFVQQTFRSSKEVKKSVEPSEVKQATSTSGPASAVADPPSTEKEIDPTSIPTAIKYQDDNSLAHPNLFIEKADAEEKWFKRLIALRQERLMGSPVA
Protein: Phosphatidylglycerol/phosphatidylinositol transfer protein (PG/PI-TP) (Q9C0X9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol.
Interaction partners:
- 2-hydroxyacyl-CoA lyase
- Probable sterol O-acyltransferase 2
Sequence:
MRLTTFIYAITCLPIFISASSWFSSFSFGESKSTDLVSSTSEKIPGANPASYCADWDRGDDHVVVDYINLIPNPPAAGKNLTIETEINVGTTVLNGSYVDIQVKYGFVRIVNERLDICDKAYELAAVECPVEPGIITKQATISLPWAIPPGRYHVLATAYNADGEQLTCVSASVSFSHFGFQLINQDH
Protein: L-gulono-1,4-lactone dehydrogenase (EC 1.1.2.-) (P9WIT3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Oxidizes L-gulono-1,4-lactone to L-xylo-hexulonolactone which spontaneously isomerizes to L-ascorbate. Can use both cytochrome c and phenazine methosulfate as exogenous electron acceptors, but molecular oxygen does not serve as a substrate. Is very specific for the L-gulono-1,4-lactone substrate, since it cannot oxidize L-galactono-1,4-lactone, D-glucurono-3,6-lactone, D-glucuronate, D-arabinose, or D-xylose.
Interaction partners:
- Conserved protein
- Conserved protein
- Probable oxidoreductase
- DAPG hydrolase PhiG domain-containing protein
- PE-PGRS family protein PE_PGRS31
Sequence:
MSPIWSNWPGEQVCAPSAIVRPTSEAELADVIAQAAKRGERVRAVGSGHSFTDIACTDGVMIDMTGLQRVLDVDQPTGLVTVEGGAKLRALGPQLAQRRLGLENQGDVDPQSITGATATATHGTGVRFQNLSARIVSLRLVTAGGEVLSLSEGDDYLAARVSLGALGVISQVTLQTVPLFTLHRHDQRRSLAQTLERLDEFVDGNDHFEFFVFPYADKALTRTMHRSDEQPKPTPGWQRMVGENFENGGLSLICQTGRRFPSVAPRLNRLMTNMMSSSTVQDRAYKVFATQRKVRFTEMEYAIPRENGREALQRVIDLVRRRSLPIMFPIEVRFSAPDDSFLSTAYGRDTCYIAVHQYAGMEFESYFRAVEEIMDDYAGRPHWGKRHYQTAATLRERYPQWDRFAAVRDRLDPDRVFLNDYTRRVLGP
Protein: S-methyl-5'-thioadenosine phosphorylase (EC 2.4.2.28) (5'-methylthioadenosine phosphorylase) (MTA phosphorylase) (MTAP) (MTAPase) (A0A384ME80)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03155}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03155}.
Interaction partners:
Sequence:
MASGTTTTAVKIGIIGGTGLDDPEILEGRTEKYVDTPFGKPSDALILGKIKNVDCVLLARHGRQHTIMPSKVNYQANIWALKEEGCTHVIVTTACGSLREEIQPGDIVIIDQFIDRTTMRPQSFYDGSHSCARGVCHIPMAEPFCPKTREVLIETAKKLGLRCHSKGTMVTIEGPRFSSRAESFMFRTWGADVINMTTVPEVVLAKEAGICYASIAMATDYDCWKEHEEAVSVDRVLKTLKENANKAKSLLLTTIPQIGSTEWSETLHNLKNMAQFSVLLPRH
Protein: Dilute class unconventional myosin (Q94882)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VKEVELKADGSDLPPLRNPAILVGQNDLTTLSYLHEPGVLHNLRVRFCKRQIIYTYCGIILVAINPYAEMPLYGPSIIRAYRGHAMGDLEPHIFALAEEAYTKLERENCNLSIIVSGESGAGKTVSAKYAMRYFAAVGGSESETQVERKVLASSPIMEAFGNAKTTRNDNSSRFGKFTNLLFRNQMGVMFLQGPTMHTYLLEKSRVVYQAQGDRNYHIFYQLCAARSKYPELVLDHQDKFQFLNMGGAPEIERVSDAEQFNETVQAMTVLGFSIQQIADIVKILAGILHLGNIQVSKKFNEGSEEEDSDSCDIFHNDIHLQITADLLRVSADDLRRWLLMRKIESVNEYVLIPNSIEAAQAARDALAKHIYAKLFQYIVGVLNKSLNNGSKQCSFIGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEEYLKEGITWTMIDFYDNQPCIDLIESRLGVLDLLDEECRMPKGSDESWAGKLIGKCNKFPHFEKPRFGTTSFFIKHFSDTVEYDVNGFLEKNRDTVSKELTQVLSESNMSLAKQVMTLEEIDTLCVDSAKSSTLGGRVVISAGRKQVVPSKQHRKTVGSQFQESLASLISTLHATTPHYVRCIKPNDDKVAFKWETAKIIQQLRACGVLETVRISAAGFPSRWLYPDFYMRYQLLVYRSKLDKNDMRLSCRNIVMKWIQDEDKYRFGNTQIFFRAGQVAFLEQVRANLRKKYITIVQSVVRRFVYRRQVLRIQKVINGIQKHARGYLARERTQKMREARAGLILSKYARGWLCRRRYLRLRHSISGIQTYARGMLARNKFHAMRDHYRAVQIQRFVRGALARRAYQKRRRNIIICQAAIRRFLARRKFKRMKAEAKTISHMENKYMGLENKIISMQQRIDELNRDNSNLKHKTSEISVLKMKLELKKTLEAEFKNVKAACQDKDKLIEALNKQLEAERDEKMQLLEENGHAQEEWISQKQTWRQENEELRRQIDEIIDMAKNAEVNQRNQEDRMLAEIDNRELNEAYQRAIKDKEVIENENFMLKEELSRLTAGSFSLHGRKASNASSQNEDDVGYASAKNTLDINRPPDLLSKNYSYNDSTSLVVKLRSILEEEKQKHKVLQEQYIKLSSRHKPTEDSFRVSELEVENEKLRRRYDQLRTSIKHGVEINELNAQHAALQEEVRRRREECIQLKAVLLQQSQSMRSLEPESLQMRGNDVNELMEAFHSQKLINRQLESELKAITEEHNSKLVEMTQEIERLNNEKDELQKVMFESIDEFEDSNVDTLRQNDRYLRRELQKAVAQFLLVQEELKLANAKLKAYRQDGGQLEHKIEEEMIRNKSNGTSADVGANVTKQKSQNPQGLMKFHSSDLDKILQRLLSALTPRTVVGLLPGFPAYLIFMCIRYTDLTNADDDVRELLSKFVIQIKKMHRTPHPIENRVIWLVNSITLLNLMKQYGDVDEYVKFNTEKQNQQQLKNFNLFEYRRVILDLFVNLYQALIMQIQGLLDPKIVPAILNNDEIQRGRQAHGMRSRATSIGASSSPEHGGGPAWKQLIGQLEHFYKQFQHFGLDNCYAEQIFHQLLYFICAVALNCLMLRGDICIWETGMIIRYNIGCIEDWVRSKKMSNDVLTALAPLNQVSQLLQSRKSEQDVQTICDLCTSLSTAQVLKVMKSYKLDDYESEITNVFLEKLTEKLNARQMQKSNSDEFTIDQKFIQPFKVVFRYSDIKLEDIELPSHLNLDEFLTKI
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q9FN35)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEATPVFNYHIDVNPERKKIGTIQVYVSFVGSANMSPILTRSNFSCSLPANELTDDEDSPHKQRLYYFLTDSAVDSQDAYTLILKLTQLARDLTSNSFEYCPRYALSVWLTLDVAPLNEYERNSEYRPASNLRVGALSRRIYKRKQKTSSIANKSTRYMRKRETYSSGEYKCAICFQEFKTGREVATLLCGHEFDNKCIMEWFKVRYNCPLCRFELPREDDHIPQRTTDL
Protein: Lysosomal acid lipase/cholesteryl ester hydrolase (Acid cholesteryl ester hydrolase) (LAL) (EC 3.1.1.13) (Cholesteryl esterase) (Diacylglycerol lipase) (Lipase A) (Sterol esterase) (Triacylglycerol ester hydrolase) (Triacylglycerol lipase) (Q9Z0M5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the deacylation of triacylglyceryl and cholesteryl ester core lipids of endocytosed low density lipoproteins to generate free fatty acids and cholesterol.
Subcellular location: Lysosome {ECO:0000250|UniProtKB:Q64194}.
Interaction partners:
- 7-dehydrocholesterol reductase
- Bile salt-activated lipase
- Delta
- Cholesterol 25-hydroxylase
- Cytochrome P450 7A1
- Sterol 26-hydroxylase, mitochondrial
- Apolipoprotein B-100
- Cholesterol 24-hydroxylase
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Sulfotransferase 2B1
Sequence:
MQLQGLVFVFTIGILLSRVPTGTVSAVDPEVNMNVTEIIMRWGYPGEEHSVLTGDGYILSIHRIPRGRKNHFGKGPRPVVYLQHGLLADSSNWVTNIDNSSLGFLLADAGFDVWMGNSRGNTWSLKHKTLSVSQDEFWAFSFDEMAKYDLPASINYILNKTGQEQIYYVGHSQGCTIGFIAFSQMPELAKKIKMFLVLAPVLSLNFASGPLLQLGRLPDPLLKDMFGQKQFLPQSAMLKWLSIHVCTHVIMKELCANVFFLLCGFNEKNLNMSRVDVYTTHCPAGTSVQNMLHWGQVFKYRKLQAFDWGSSEKNYFHYNQSFPPSYNIKNMRLPTALWSGGRDWLADINDITILLTQIPKLVYHKNIPEWDHLDFIWGLDAPWKLYDEIISLMKKYQ
Protein: Prolyl endopeptidase (EC 3.4.21.-) (Q9V9P5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI08533p
- Mitochondrial 2-oxodicarboxylate carrier
Sequence:
MSRSDALVQSPTDLSRSVEEASLRIVYPEARKDGRFEEMIHGYKIKDVYRWLEDPDSVDTQQFVNAQNNISQSFLERSAERENINSKLTKLWNFPKYGCPMRHGNYYYFFKNTGLQNQSVLMQQKTLESPESIFLDTNSISSDGTTAISHIKFSEDGAFMAYGLSESGSDWNKIRIRNTKEGIDLPEILEKVKFSNVSWTKDSKGFFYGRYTDQDGIFDGSETKLAENQKLYYHLLGESPHQDILIAEFPEHPSWRFKTDISDCGKYLILSISHTVRDNMLYYAELGSEEKNAFQLELKPIVDKFEADFDYITNEGSNLYFHTNKDAPNYRVIVIDVNNPAEEHWTTPIPEHKKDVLEWAKCVDGNKLVVCYNCDVKHILQARDLSTGKLIRQFGLDIGSINGISGKKSNSEIFYGFSSFLSPGIIFYYDFAKPSEKPTVLREISLNLEGFSRDNYSVEQVFYKSTDDTDIPMFIVQRKRDIAEPRPCLLYGYGGFNYSLMPSFGILSLMFMDTFDGVLAFPNLRGGGEYGMEWHNGGRMLSKQNVFNDFQAAAEFLTKNNYTTKDRLAIQGASNGGLLVGACINQRPDLFGAAVAQVGVMDMLRFHKFTIGHAWCSDYGNPDEKVHFANLIKFSPLHNVHIPLNPNQEYPSTLILTADHDDRVSPLHSYKFVAALQEAVRYSEYQLNPILLRVYTKAGHGAGKPTKMRISEATDIITFFKKTLNVDCINL
Protein: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase sqv-8 (EC 2.4.1.135) (Glucuronyl transferase I) (GlcAT-I) (Squashed vulva protein 8) (Vulval invagination protein sqv-8) (Q09363)
Organism: Caenorhabditis elegans
Function: Glycosyltransferase required for the biosynthesis of the tetrasaccharide (GlcA-Gal-Gal-Xyl-)Ser core linker of heparan sulfate and chondroitin sulfate. May be involved in the biosynthesis of the HNK-1 carbohydrate epitope on glycoproteins. Required for embryonic development. Involved in the elongation of the pharyngeal isthmus during the later stages of embryonic development. Involved in vulval epithelium invagination.
Subcellular location: Membrane {ECO:0000269|PubMed:11005858}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Beta-1,3-galactosyltransferase sqv-2
- Xylosylprotein 4-beta-galactosyltransferase
- Acid phosphatase-like protein 2
- UDP-glucuronate decarboxylase
- Coiled-coil domain-containing protein 130 homolog
- UDP-sugar transporter sqv-7
- Exostosin-like-3 homolog
- Chondroitin sulfate synthase mig-22
- Putative steroid dehydrogenase 4
- CYtochrome P450 family
Sequence:
MFPSRLLEKWWLRAFIALVIFFVWQLFYAINRVQSLEEERATLQATIEVLTRKSDGLRTQIFEKERNLVRLNGKVEEIDTQIRDHLSLLPRVNRSTPFIYFITPTHFRAAQRADLTRLSYTLSHVPNLHWIVVEDSDELTPSIAGILKRSKIPNTHLNARTPSDQKMRYDDPNWTLPRGVEQRNRALLWIQNQLSGVKEGVVYFGDDDNTYDLKIFGEMRKVKNAGVWPVGIVGGMFVETPILEKNGSISHFNAVWKPERPFPIDMAAFAVNISLVLSNANALFSFDVPRGYQESTFLENLGIHRYNMEPLAEMCTKVYVWHTRTEKPKLSKESIDRLTKKTGFNSLEAHALGVDN
Protein: Factor interacting with poly(A) polymerase 1 (Q9VN31)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- LD24014p
- Cleavage and polyadenylation specificity factor subunit 4
- Symplekin
- Probable cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 1
- Cleavage and polyadenylation specificity factor 73
- Protein suppressor of forked
- Cleavage stimulation factor 64 kD subunit
- polynucleotide adenylyltransferase
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
Sequence:
MADDTNEDSWLYGTSNPDSTTGELGNGGDSLTAEHESAAAEAQALAELVAGEKPGASAGTNSTEDSPRCPKEEVPEYSEFDDPAQEMEEDEDALPNTDSRSRRERDRERDRGRCADRADARSSPDPEDDEMSDGPAARRERNGSGSDDDEDDDSDDDINVVIGDIKQAPSTYNIKQRPNLLAGGTGAAGDKAKPAGQAGKFSIEDFEGAGTINGVAVHEFSIDSLEEKPWRKPGADITDYFNYGFNEETWRAYCERQKRFRVAESGVGLASLTQNVNQNAPIGILTDGGMGMGPPGMHSIQSMVGMGGESGMQMPPPGMPPPMMQHQSRSGMGLMQRPPRPISTTGGDRGGDRERAVKENAIQVMTAECREYSRGGLGPMAPNFPLPGASEEPFFHEPEPFDYGYEPTQESQWNNDNAGWVPSGIKELTPGHAHMQQPPPGMPPPGMSVPPPQMGGPPPNLRGIMPPNMRMPPNMNMGPPPGMMMGGNAPPQMRMGMAPPQRLAMGDRGAYDDDRERRRREKEKLLKKDQLRKDFLDMLRERHDIERHTRWYDIKKKFEADPRYRALDSSYREEYFEDYLHLLKEEKRKERDLKERERHRDKERSRDKDKDKDKEKDKDKDKDKEKDKEKDKDKDKEKEKDKESSRRERSRSREKSSRRKSKSREKDRSERSSKSSSSNTGGSSSRSEKKKSHRKDKEEDD
Protein: Uncharacterized Na(+)/H(+) antiporter C15A10.06 (O13726)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative cation exchanger C3A12.06c
- General alpha-glucoside permease
- Na
- Tyrosine-protein phosphatase yvh1
Sequence:
MLDTILINVFRRDGDDDDDDGQDPALQELYSSWALFILLVLLIGALLTSYYVQSKKIRAIHETVISVFVGMVVGLIIRVSPGLIIQNMVSFHSTYFFNVLLPPIILNSGYELHQSNFFRNIGTILTFAFAGTFISAVTLGVLVYIFSFLNFENLSMTFVEALSMGATLSATDPVTVLAIFNSYKVDQKLYTIIFGESILNDAVAIVMFETLQQFQGKTLHFFTLFSGIGIFIITFFISLLIGVSIGLITALLLKYSYLRRYPSIESCIILLMAYTSYFFSNGCHMSGVVSLLFCGITLKHYAFFNMSYKAKLSTKYVFRVLAQLSENFIFIYLGMSLFTQVDLVYKPIFILITTVAVTASRYMNVFPLSNLLNKFHRQRNGNLIDHIPYSYQMMLFWAGLRGAVGVALAAGFEGENAQTLRATTLVVVVLTLIIFGGTTARMLEILHIETGVAADVDSDTEIGMLPWQQSPEFDLENSAMELSDASAEPVVVDQQFTTEHFDEGNIAPTLSKKVSSTFEQYQRAAGAFNQFFHSSRDDQAQWLTRFDEEVIKPVLLERDNLKNGTKK
Protein: Cyclin-dependent kinase 5 homolog (EC 2.7.11.22) (CDC2-like serine/threonine-protein kinase CRP) (Cell division protein kinase 5) (P34117)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Ankyrin repeat-containing protein
- Uncharacterized protein
- F-box domain-containing protein
- Histone H1
- Uncharacterized protein
- Glycerophosphodiester phosphodiesterase
- Uncharacterized protein
- Anaphase-promoting complex subunit cdh1
- G2/mitotic-specific cyclin-B
- Anaphase-promoting complex subunit cdc20
Sequence:
MEKYSKIEKLGEGTYGIVYKAKNRETGEIVALKRIRLDSEDEGVPCTAIREISLLKELKHPNIVRLHDVIHTERKLTLVFEYLDQDLKKYLDECGGEISKPTIKSFMYQLLKGVAFCHDHRVLHRDLKPQNLLINRKGELKLADFGLARAFGIPVRTYSHEVVTLWYRAPDVLMGSRKYSTPIDIWSAGCIFAEMASGRPLFPGSGTSDQLFRIFKILGTPNEESWPSITELPEYKTDFPVHPAHQLSSIVHGLDEKGLNLLSKMLQYDPNQRITAAAALKHPYFDGLEPIN