wanglab/gogpt-training-data huggingface dataset:
Protein: Rho GTPase activating protein 4 (E9PCM6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAHGKLRRERGLQAEYETQVKEMRWQLSEQLRCLELQGELRRELLQELAEFMRRRAEVELEYSRGLEKLAERFSSRGGRLGSSREHQSFRKEPSLLSPLHCWAVLLQHTRQQSRESAALSEVLAGPLAQRLSHIAEDVGRLVKKSRDLEQQLQDELLEVVSELQTVAEICVEMELRDEILPRAQNIQSRLDRQTIETEEVNKTLKATLQALLEVVASDDGDVLDSFQTSPSTESLKSTSSDPGSRQAGRRRGQQQETETFYLTKLQEYLSGRSILAKLQAKHEKLQEALQRGDKEEQEVSWTQYTQRKFQKSRQPRPSSQYNQRLFGGDMEKFIQSSGQPVPLVVESCIRFINLNGLQHEGIFRVSGAQLRVSEIRDAFERGEDPLVEGCTAHDLDSVAGVLKLYFRSLEPPLFPPDLFGELLASSELEATAERVEHVSRLLWRLPAPVLVVLRYLFTFLNHLAQYSDENMMDPYNLAVCFGPTLLPVPAGQDPVALQGRVNQLVQTLIVQPDRVFPPLTSLPGPVYEKCMAPPSASCLGDAQLESLGADNEPELEAEMPAQEDDLEGVVEAVACFAYTGRTAQELSFRRGDVLRLHERASSDWWRGEHNGMRGLIPHKYITLPAGTEKQVVGAGLQTAGESGSSPEGLLASELVHRPEPCTSPEAMGPSGHRRRCLVPASPEQHVEVDKAVAQNMDSVFKELLGKTSVRQGLGPASTTSPSPGPRSPKAPPSSRLGRNKGFSRGPGAPASPSASHPQGLDTTPKPH
Protein: Citrate lyase, subunit2 (Q8KDG2)
Organism: Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS) (Chlorobium tepidum)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Citrate lyase, subunit1
- Succinate--CoA ligase subunit beta
- Malate dehydrogenase
- Aconitate hydratase B
- Succinate/fumarate oxidoreductase, iron-sulfur protein, putative
- Pyruvate flavodoxin/ferrodoxin oxidoreductase
- Succinate dehydrogenase, iron-sulfur protein
- Acetyl-coenzyme A synthetase
- succinate dehydrogenase
- NADH-quinone oxidoreductase subunit D
Sequence:
MSILANKDTRAVIIGGVAGVNAAKRMAQFDYLINRPLTVQAFVYPPEAGQQKEIFRGGELKNVTVYPSLAPALNEHPDINTALIYLGASRATEAAMEALESPNIQLVSMITEGVPEKDAKRLKKLAQKLGKMLNGPSSIGIMSAGECRLGVIGGEYRNLKLCNLYRQGSFGVLTKSGGLSNEAMWLCAQNGDGITSAVAIGGDAYPGTDFVTYLEMFEKDPATKAVVMIGEVGGNLEEEAAEWLAAEPRRIKLIAAIGGTCQEVLPQGMKFGHAGAKEGKKGAGSARSKMNALREAGALVPDTFGGLSKAIKQVYEELLASGAIKPKPEIDEALLPELPPSVQEVMKQGEVVVEPLIRTTISDDRGEEPRYAGYAASELCSKGYGIEDVIGLLWSKKLPSREESEIIKRIIMISADHGPAVSGAFGTILAACAGIDMPQAVSAGMTMIGPRFGGAVTNAGKYFKMGVKEYPNDIPGFLAWMKKNVGPVPGIGHRVKSLRNPDQRVKYLVSYVKNETSLHTPILNYALEVEKITTAKKENLILNVDGTIGCILMDLGFPEHSLNGFFVLARTIGMIGHWIDQNNQNSRLIRLYDYLINYAVKPERPVPDKK
Protein: Nuclear RNA export factor 1 (Tip-associated protein) (Tip-associating protein) (mRNA export factor TAP) (Q99JX7)
Organism: Mus musculus (Mouse)
Function: Involved in the nuclear export of mRNA species bearing retroviral constitutive transport elements (CTE) and in the export of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of the TREX complex. ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1 heterodimer for export. Also involved in nuclear export of m6A-containing mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A-containing mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export.
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus speckle {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q9UBU9}. Nucleus envelope {ECO:0000250|UniProtKB:Q9UBU9}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q9UBU9}. Note=Localized predominantly in the nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of the nuclear pore complex. Shuttles between the nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. The association with the TREX complex seems to occur in regions surrounding nuclear speckles known as perispeckles. Nucleus; nuclear rim. {ECO:0000250|UniProtKB:Q9UBU9}.
Interaction partners:
- NTF2-related export protein 1
- mRNA export factor
- Serine/arginine-rich splicing factor 3
- THO complex subunit 4
- Aly/REF export factor 2
- THO complex subunit 5 homolog
- Spliceosome RNA helicase Ddx39b
- NTF2-related export protein 2
- Eukaryotic initiation factor 4A-III
- Serine/arginine-rich splicing factor 1
Sequence:
MADEGKSYNEHDDRVSFPQRRKKGRGPFRWKCGEGNRRSGRGGSGVQSSRFEEDDGDVAMNDPQDGPRVRYNPYTNRPNRRGDGWHDRDRIHITVRRDRAPAERGGAGTSQDGTTKNWFKITIPYGRKYDKTWLLSMIQSKCSVPFNPIEFHYENTRAHFFVEDATTASALKGVNHKIQDRENRRISIIINASAPPYTVQNELKPEQIEQLKLIMSKRYDGNQQALDLKGLRSDPDLVAQNIDVVLNRRSCMAATLRIIEENIPELLSLNLSSNRLYKLDDMSSIVQKAPNLKTLNLSGNELKTERELDKIKGLKLEELWLDRNPMCDNFGDQSSYISAIRERFPKLLRLDGHELPPPISFDVEAPTMLPPCKGSYFGTENLKSLVLRFLQQYYVIYDSGDRQGLLYAYHDGACCSLSIPYNPQNPVRKNLAEYVKDSRNVKKLKEPTQRFRLLKHTRLNVVAFLNELPKTQHDVNAFVVDISAQTSTLLCFSVNGVFKEVDGKSRDSLRAFTRTFIAVPASNSGLCIVNDELFVRNASPEEIQRAFAMSAPTPSSSPVPTLSPEQQEMLQAFSTQSGMNLEWSQKCLQDNNWDYTRSAQAFTLLKAKGEIPEVAFMK
Protein: Nuclear factor 1 (O70186)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPNSPAAGSRTWHERDQDMSSPTTMKKPEKPLFSSTSPQDSSPRLSTFPQHHHPGIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQPNSSGQVVGKVPGHFTPVLAPSPHPSAVRPVTLTMTDTKPITTSTEAYTASGTSQANRYVGLSPRDPSFLHQQQSWYLG
Protein: Paired amphipathic helix (PAH2) superfamily protein (Q9LFQ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00810}.
Interaction partners:
Sequence:
MAECRAYFMEVKDTFHDQIEKYDMFKNILLDLKARRIGRHTAFAQLKELFKEHNELIIGFNTFLPTGYKIALDDDVEDSFSSTARNY
Protein: Mevalonate-3-phosphate 5-kinase (EC 2.7.1.186) (Q9HK44)
Organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Function: Phosphorylates mevalonate 3-phosphate to form mevalonate 3,5-bisphosphate. Functions in an alternative mevalonate pathway, only present in extreme acidophiles of the Thermoplasmatales order, which passes through mevalonate 3-phosphate rather than mevalonate 5-phosphate.
Interaction partners:
- Mevalonate 3-kinase
- Mevalonate 3,5-bisphosphate decarboxylase
- Isochorismatase-like domain-containing protein
- PIN domain-containing protein
Sequence:
MNSRIMFIGGVPGVGKTSISGYIARNTDIDIVLSSDYLREFLRPFAPQESHLETSVYDAWKFYGDMSDDNIIRGYLDQARPIMGGINRVIARALANGEDLIIESLYFVPDMMDEMVLKNAFLAYVYIDDPDLHRSRLEDRINYTHRNSPGSRLAAHLKEYRTIMDYSMDMARGRGIGLYSTDDYALARQRLLDDFRKFVDRR
Protein: Integrin alpha-X (CD11 antigen-like family member C) (Leu M5) (Leukocyte adhesion glycoprotein p150,95 alpha chain) (Leukocyte adhesion receptor p150,95) (CD antigen CD11c) (P20702)
Organism: Homo sapiens (Human)
Function: Integrin alpha-X/beta-2 is a receptor for fibrinogen. It recognizes the sequence G-P-R in fibrinogen. It mediates cell-cell interaction during inflammatory responses. It is especially important in monocyte adhesion and chemotaxis.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Integrin beta-2
- Intercellular adhesion molecule 1
- Complement C3
- Integrin beta-1
- Integrin alpha-L
- T-cell surface glycoprotein CD4
- Receptor-type tyrosine-protein phosphatase C
- T-cell surface glycoprotein CD8 alpha chain
- Vascular cell adhesion protein 1
- Interferon gamma
Sequence:
MTRTRAALLLFTALATSLGFNLDTEELTAFRVDSAGFGDSVVQYANSWVVVGAPQKITAANQTGGLYQCGYSTGACEPIGLQVPPEAVNMSLGLSLASTTSPSQLLACGPTVHHECGRNMYLTGLCFLLGPTQLTQRLPVSRQECPRQEQDIVFLIDGSGSISSRNFATMMNFVRAVISQFQRPSTQFSLMQFSNKFQTHFTFEEFRRSSNPLSLLASVHQLQGFTYTATAIQNVVHRLFHASYGARRDAAKILIVITDGKKEGDSLDYKDVIPMADAAGIIRYAIGVGLAFQNRNSWKELNDIASKPSQEHIFKVEDFDALKDIQNQLKEKIFAIEGTETTSSSSFELEMAQEGFSAVFTPDGPVLGAVGSFTWSGGAFLYPPNMSPTFINMSQENVDMRDSYLGYSTELALWKGVQSLVLGAPRYQHTGKAVIFTQVSRQWRMKAEVTGTQIGSYFGASLCSVDVDSDGSTDLVLIGAPHYYEQTRGGQVSVCPLPRGWRRWWCDAVLYGEQGHPWGRFGAALTVLGDVNGDKLTDVVIGAPGEEENRGAVYLFHGVLGPSISPSHSQRIAGSQLSSRLQYFGQALSGGQDLTQDGLVDLAVGARGQVLLLRTRPVLWVGVSMQFIPAEIPRSAFECREQVVSEQTLVQSNICLYIDKRSKNLLGSRDLQSSVTLDLALDPGRLSPRATFQETKNRSLSRVRVLGLKAHCENFNLLLPSCVEDSVTPITLRLNFTLVGKPLLAFRNLRPMLAADAQRYFTASLPFEKNCGADHICQDNLGISFSFPGLKSLLVGSNLELNAEVMVWNDGEDSYGTTITFSHPAGLSYRYVAEGQKQGQLRSLHLTCDSAPVGSQGTWSTSCRINHLIFRGGAQITFLATFDVSPKAVLGDRLLLTANVSSENNTPRTSKTTFQLELPVKYAVYTVVSSHEQFTKYLNFSESEEKESHVAMHRYQVNNLGQRDLPVSINFWVPVELNQEAVWMDVEVSHPQNPSLRCSSEKIAPPASDFLAHIQKNPVLDCSIAGCLRFRCDVPSFSVQEELDFTLKGNLSFGWVRQILQKKVSVVSVAEITFDTSVYSQLPGQEAFMRAQTTTVLEKYKVHNPTPLIVGSSIGGLLLLALITAVLYKVGFFKRQYKEMMEEANGQIAPENGTQTPSPPSEK
Protein: ENT domain-containing protein (Q385P5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSASGSGVAAIYGRAEEAQNAPVKLQPVPAFELYKAAREEELCSYRSLCRVLCMHSGGKLTKQQRRILEDMREELCLPTERAEAELAAAREDVLVTSVAASGVLKRRQDFFDGVTDVPLDTLSYAESAKDDNNSLYVAQTKVARTEQIVGGVHGRHAAPSKMSIREIHKNLERIGREVAATSSKLLYCTSVVDQQAYRNVLQQKREQLQAMLREVEDAPPDMSGIASVMPSEHVY
Protein: B-cell receptor CD22 (B-lymphocyte cell adhesion molecule) (BL-CAM) (Sialic acid-binding Ig-like lectin 2) (Siglec-2) (T-cell surface antigen Leu-14) (CD antigen CD22) (P20273)
Organism: Homo sapiens (Human)
Function: Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20172905}; Single-pass type I membrane protein.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase C
- Tyrosine-protein phosphatase non-receptor type 6
- B-lymphocyte antigen CD19
- B-cell antigen receptor complex-associated protein alpha chain
- Tyrosine-protein kinase Lyn
- B-cell antigen receptor complex-associated protein beta chain
- Tyrosine-protein kinase SYK
- Cell surface glycoprotein CD200 receptor 1
- B-lymphocyte antigen CD20
- T-cell surface glycoprotein CD5
Sequence:
MHLLGPWLLLLVLEYLAFSDSSKWVFEHPETLYAWEGACVWIPCTYRALDGDLESFILFHNPEYNKNTSKFDGTRLYESTKDGKVPSEQKRVQFLGDKNKNCTLSIHPVHLNDSGQLGLRMESKTEKWMERIHLNVSERPFPPHIQLPPEIQESQEVTLTCLLNFSCYGYPIQLQWLLEGVPMRQAAVTSTSLTIKSVFTRSELKFSPQWSHHGKIVTCQLQDADGKFLSNDTVQLNVKHTPKLEIKVTPSDAIVREGDSVTMTCEVSSSNPEYTTVSWLKDGTSLKKQNTFTLNLREVTKDQSGKYCCQVSNDVGPGRSEEVFLQVQYAPEPSTVQILHSPAVEGSQVEFLCMSLANPLPTNYTWYHNGKEMQGRTEEKVHIPKILPWHAGTYSCVAENILGTGQRGPGAELDVQYPPKKVTTVIQNPMPIREGDTVTLSCNYNSSNPSVTRYEWKPHGAWEEPSLGVLKIQNVGWDNTTIACAACNSWCSWASPVALNVQYAPRDVRVRKIKPLSEIHSGNSVSLQCDFSSSHPKEVQFFWEKNGRLLGKESQLNFDSISPEDAGSYSCWVNNSIGQTASKAWTLEVLYAPRRLRVSMSPGDQVMEGKSATLTCESDANPPVSHYTWFDWNNQSLPYHSQKLRLEPVKVQHSGAYWCQGTNSVGKGRSPLSTLTVYYSPETIGRRVAVGLGSCLAILILAICGLKLQRRWKRTQSQQGLQENSSGQSFFVRNKKVRRAPLSEGPHSLGCYNPMMEDGISYTTLRFPEMNIPRTGDAESSEMQRPPPDCDDTVTYSALHKRQVGDYENVIPDFPEDEGIHYSELIQFGVGERPQAQENVDYVILKH
Protein: Tubulin polyglutamylase TTLL5 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 5) (Q8CHB8)
Organism: Mus musculus (Mouse)
Function: Polyglutamylase which modifies tubulin, generating polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Preferentially mediates ATP-dependent initiation step of the polyglutamylation reaction over the elongation step. Preferentially modifies the alpha-tubulin tail over a beta-tail. Required for CCSAP localization to both polyglutamylated spindle and cilia microtubules (By similarity). Increases the effects of transcriptional coactivator NCOA2/TIF2 in glucocorticoid receptor-mediated repression and induction and in androgen receptor-mediated induction (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Nucleus {ECO:0000250|UniProtKB:Q6EMB2}. Cytoplasm {ECO:0000250, ECO:0000250|UniProtKB:Q6EMB2}. Note=In osteosarcoma cells, found in both cytoplasm and nucleus in the absence of steroid but located exclusively in the nucleus in the presence of steroid (By similarity). Localized to the base of the connecting cilium between the basal body and the adjacent daughter centriole of the cilium. {ECO:0000250|UniProtKB:Q6EMB2}.
Interaction partners:
Sequence:
MPVVMARDLEETASSSEDEDLANQEDHPCIMWTGGCRRIPVLVFHAEAILTKDNNIRVIGERYHLSYKIVRTDSRLVRSILTAHGFHEVHPSSTDYNLMWTGSHLKPFLLRTLSEAQKVNHFPRSYELTRKDRLYKNIIRMQHTHGFKAFHILPQTFLLPAEYAEFCNSYSKDRGPWIVKPVASSRGRGVYLINNPNQISLEENILVSRYINNPLLIDDFKFDVRLYVLVTSYDPLVIYLYEEGLARFATVRYDQGSKNIRNQFMHLTNYSVNKKSGDYVSCDDPEVEDYGNKWSMSAMLRYLKQEGKDTTALMAHVEDLIIKTIISAELAIATACKTFVPHRSSCFELYGFDVLIDNTLKPWLLEVNLSPSLACDAPLDLKIKASMISDMFTVVGFVCQDPAQRTSNRSIYPSFESSRRNPFQKPQRTRPLSASDAEMKNLVASAREKVPGKLGGSVLGLSMEEIKVLRRVKEENDRRGGFIRIFPTSETWEIYGSYLEHKTSMNYMLATRLFQDRGNPRRSLLTGRARVSTEGAPELKVESMNSKAKLHAALYERKLLSLEVRKRRRRSGRLRAMRPKYPVIAQPAEMNIKTETESEEEEEVGLDNDDEEQEASQEESAGSLGENQAKYTPSLTVIVENSPRDNAMKVAEWTNKGEPCCKIEAQEPESKFNLMQILQDNGNLSKVQARLAFSAYLQHVQIRLTKDSGGQTLSPSWAAKEDEQMELVVRFLKRASSNLQHSLRMVLPSRRLALLERRRILAHQLGDFIGVYNKETEQMAEKKSKKKLEEEEEDGVNAESFQEFIRQASEAELEEVLTFYTQKNKSASVFLGTHSKSSKNSSSYSDSGAKGDHPETIQEVKIKQPKQQQATEIHADKLSRFTTSSGKEAKLVYTNCSSFCSPAAVLLQRLPSSHLSSVITTSALSAGPGHHASLSQIPPAVPSLPHQPALLLSPVPDNAPPSIHSGTQNVSPAGLPRCRSGSYTIGPFSSFQSAAHIYSQKLSRPSSAKAAGSCHPHKHHSGIAKTQKEGEDVSLNRRYNQSLVTAELQRLAEKQAARQYSPASHISLLTQQVTNLNLASSVINRSSASTPPTLRPVISPSGPTWSIQPDLHASETHSSPPGSRSLQTGGFAWEGEVENNAYSKTTGVVPQHKYHPTAGSYQLHFALQQLEQQKLQSRQLLDQSRARHQAIFGSQTLPNSSLWTMNNGPGCRISSATTGGQKPNTLPQKVVAPPNSSTLVSKPASNHKQVLRKPASQRASKGSSAEGQLNGLQSSLNPAAFMPITNSTGSLEAPQVIFARSKPLPTQSGALATVIGQRKSKSVKSGTI
Protein: Cotranscriptional regulator ARB2A (Cotranscriptional regulator FAM172A) (Protein FAM172A) (Q3TNH5)
Organism: Mus musculus (Mouse)
Function: Plays a role in the regulation of alternative splicing, by interacting with AGO2 and CHD7. Seems to be required for stabilizing protein-protein interactions at the chromatin-spliceosome interface. May have hydrolase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:29311329}. Cytoplasm {ECO:0000269|PubMed:29311329}. Endoplasmic reticulum {ECO:0000269|PubMed:29311329}.
Interaction partners:
Sequence:
MSISLSSLIFLPIWINMAQMQQGGSNETEQTAALKDLLSRIDLDELMKKDEPPFDFPDTLEGFEYAFNEKGQLRHIKTGEPFVFNYREDLHRWNQKRYEALGEIITRYVYELLESDCNLKKISIPVDATESEPKSFIFMSEDALTNPQKLMVLIHGSGVVRAGQWARRLIINEDLDSGTQIPFIKRAMDEGYGVIVLNPNENYIEVEKQKMHKQSSSSDGTDEPAGKRERRDKVSKETKKRRDFYEKYRNPQKEKEMMQLFIRENGSPEEHAVYVWDHFIAQAAAENVFFVAHSYGGLAFVELMIQREADVKSKVTAVALTDSVHNVWHQEAGKTIREWMRENCCNWVSSSEPLDTSVESMLPDCPRVSAGTDRHELTSWKSFPSIFKFFAEASEAKSSSQKPALTRRSHRIKHEEL
Protein: Brain and acute leukemia cytoplasmic protein (Q8WXS3)
Organism: Homo sapiens (Human)
Function: May play a synaptic role at the postsynaptic lipid rafts possibly through interaction with CAMK2A.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11707601}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q920K5}. Membrane raft {ECO:0000250|UniProtKB:Q920K5}. Postsynaptic density {ECO:0000250|UniProtKB:Q920K5}. Note=In neurons, localizes to postsynaptic lipid rafts (By similarity). In myocardial and skeletal muscle cells, localizes to the cytoplasm adjacent to the inner cell membrane, polarized to one end of the myocyte (By similarity). {ECO:0000250|UniProtKB:Q8VHV1, ECO:0000250|UniProtKB:Q920K5}.
Interaction partners:
Sequence:
MGCGGSRADAIEPRYYESWTRETESTWLTYTDSDAPPSAAAPDSGPEAGGLHSGMLEDGLPSNGVPRSTAPGGIPNPEKKTNCETQCPNPQSLSSGPLTQKQNGLQTTEAKRDAKRMPAKEVTINVTDSIQQMDRSRRITKNCVN
Protein: p44 outer membrane protein, C-terminal (Q2GJE3)
Organism: Anaplasma phagocytophilum (strain HZ)
Interaction partners:
Sequence:
MYYEINQEKSLGVVPYTCVGLGGNLEGVVDEHITPKLAYRLKVGLSYQLSPEISAFAGVSTITFPRDMMPTVCTCLFGTINSFYSVDFLVVPNVSILLINNMVQTTASIQYFSAI
Protein: Transcription initiation factor TFIID subunit 11 (TAFII-40) (TAFII40) (TBP-associated factor 11) (TBP-associated factor 40 kDa) (P40) (Q04226)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the DNA-binding general transcription factor complex TFIID. Binding of TFIID to a promoter (with or without TATA element) is the initial step in pre-initiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor TFIID subunit 8
- TATA-box-binding protein
- SAGA complex/transcription factor TFIID complex subunit TAF6
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 4
- SAGA complex/transcription factor TFIID complex subunit TAF5
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 2
- SAGA complex/transcription factor TFIID complex subunit TAF9
- SAGA complex/transcription factor TFIID complex subunit TAF12
Sequence:
MTEPQGPLDTIPKVNYPPILTIANYFSTKQMIDQVISEDQDYVTWKLQNLRTGGTSINNQLNKYPKYKYQKTRINQQDPDSINKVPENLIFPQDILQQQTQNSNYEDTNTNEDENEKLAQDEQFKLLVTNLDKDQTNRFEVFHRTSLNKTQVKKLASTVANQTISENIRVFLQAVGKIYAGEIIELAMIVKNKWLTSQMCIEFDKRTKIGYKLKKYLKKLTFSIIENQQYKQDYQSDSVPEDEPDFYFDDEEVDKRETTLGNSLLQSKSLQQSDHNSQDLKLQLIEQYNKLVLQFNKLDVSIEKYNNSPLLPEHIREAWRLYRLQSDTLPNAYWRTQGEGQGSMFR
Protein: Calcium load-activated calcium channel (CLAC channel) (Q9LHL8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Nicalin
- BOS complex subunit TMEM147
- Uncharacterized protein At5g49945
- At4g24330
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL18y
- At2g29020/T9I4.10
- At5g59410
- Protein Asterix
Sequence:
MATTIPLFASFKYADSLTVVGISFCTALVCEAISWILIYRTSSYKSLKYSIDKATKKLETMKTENPSSKLSIKKSKTKKIDRVETSLKESSRDLSLFKFKSGAVVALVLFVVFGLLNSLFEGKVVAKLPFHPITIVKKMSHRGLKGDDPTDCSMAFLYLLCSISIRTNLQKFLGFSPPRGAAGAGGLFPMPDPKTN
Protein: Probable NADH dehydrogenase (Q9I4R8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU000320}.
Interaction partners:
- Na+/H+ antiporter subunit E
- Probable NADH dehydrogenase
- Na+/H+ antiporter subunit C
- K+/H+ antiporter subunit F
- Na+/H+ antiporter subunit G
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit C/D
- Formate dehydrogenase-O, major subunit
Sequence:
MSHWLILPILLPLFAGSLLLLPLAERWQRGLSLLAALALIPLSLLLIRTAASGDLSVYALGNWAAPFGIVLMLDRLAALMLLATAVLGSAALIYALRGEDRLGKHFHALFQFQLLGINGAFLTGDLFNLFVFFEILLIASYALLLHGGGAERVRSGLHYVILNLVGSAFFLIAVGTLYGLTGTLNMADMAQKIAMADAERAPLLAAAGLLLLVVFALKAALLPLYFWLPRAYATASAPVAALFAIMTKVGIYSILRVYTLVFGDAAGELANLAQAWLWPLALATLGLGAIGALAARTLQGLLAYLVVVSAGTLLAGVALGSERALAASLYYLLHSTWIAGGLFLLADLVARQRGDKAGDLVQGPALQNPRLLGGAFFIGAIAVAGLPPLSGFFGKVMLLQSVAPGSQALALWSVVLGSGLVALVALSRAGSTLFWRTGHTVLGSAELDHGRLFACILLLSAGPLLVFAAKPLLAYVQATAAQLHDLDLYRQIITRGGAA
Protein: Integral inner nuclear membrane protein ima1 (O13681)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Inner nuclear membrane protein that specifically binds to heterochromatic regions and promotes the tethering of centromeric DNA to the SUN-KASH complex. Couples centromeres to the nuclear envelope, thus contributing to their association with the microtubule organizing center attachment site and to the positioning of the nucleus at the cell center by microtubules.
Subcellular location: Nucleus inner membrane {ECO:0000269|PubMed:18692466}; Multi-pass membrane protein {ECO:0000269|PubMed:18692466}.
Interaction partners:
- Spindle pole body-associated protein sad1
- Lap-Emerin-Man domain protein 2
- Meiotically up-regulated gene 61 protein
- Uncharacterized protein C2G2.14
- ADP,ATP carrier protein
- Karyogamy meiotic segregation protein 2
Sequence:
MESSRLFTLGLGNSDDGLKSTFGDKTVTCFYCNKKKEKIRDGTSTWTCSICEATNHIDEKGDILDYRPPTPTQDKGVGPFYAIRDFPSSSSFQSPFCEKCQMNQLIVNRMLADYLPDSSHPDYQAYEKALPEYKKSIEEKFPIVCSECYDSVQDQLDANDYEAKNQVLGYWLQKSKEQLNAKVPHHYPKASFVLWLLRGFGFSFFYLQSIVWHLYHSMIISLLPDGIRNLFLKAISYFLLDGSSSKIFYFNWLGFFVVFWNPYWYKMMDNPSWELFGRDQYIQCQALYLIIRLTCLYLLSCYESEILNLSSDTNLESDFLLRQIHAAFFFVTICFTWISISCLKPSPPPEVHLTGEILKPRKKRQESTSSVHRIGKESSDRKDGISGQNKLQQFATISILNNTNATSHLGNQSVRERAPEESPMTFLQKKMAALPTSSPVRPMLKPTLQLQNSPLSKLVPQEVGNKVNDSIHTTSNQPSKFSLNPSISLKGDNVIEKNLPFSVSTLKSTAKKDTGKAGDGQNREIQNEPVSLESHFSKSLALQNDPTEVIQVKNVLHRNRRNAKLLIAFTILFLVGLICGWRLNRFTMFIYYLCILVLATYYVMKHNFYPLRKVA
Protein: Pimeloyl-[acyl-carrier protein] methyl ester esterase (EC 3.1.1.85) (Biotin synthesis protein BioH) (Carboxylesterase BioH) (Q9K197)
Organism: Neisseria meningitidis serogroup B (strain ATCC BAA-335 / MC58)
Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01260}.
Interaction partners:
- Putative 8-amino-7-oxononanoate synthase
- Enoyl-[acyl-carrier-protein] reductase FabI
- Biotin synthesis protein BioG
- Biotin synthesis protein BioC
- ATP-dependent dethiobiotin synthetase BioD
- Bifunctional enzyme BirA/CoaX synthetase
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- Octanoyltransferase
- Malonyl-[acyl-carrier protein] O-methyltransferase
Sequence:
MRRQRERKSMPDAVKKVYLIHGWGANRHMFDDLMPRLPATWPVSAVDLPGHGDAPFVRPFDIAAAADGIAAQIDAPADILGWSLGGLVALYLAARHPDKVRSLCLTASFARLTADEDYPEGLAAPALGKMVGAFRSDYAKHIKQFLQLQLLHTPDADGIIGRILPDLARCGTPQALQEALDAAERADARHLLDKIDVPVLLVFGGKDAITPPRMGEYLHRRLKGSRLVVMEKAAHAPFLSHAEAFAALYRDFVEGGLR
Protein: ESCRT-II subunit protein (Q5AK78)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Vacuolar protein-sorting-associated protein 36
- Vacuolar-sorting protein SNF8
- ESCRT-III subunit protein
- Vacuolar protein sorting-associated protein 28
- Vacuolar-sorting protein SNF7
- ESCRT-III subunit protein
- Ubiquitin-binding ESCRT-I subunit protein
- Vacuolar protein sorting-associated protein 27
- Uncharacterized protein
- ESCRT-III subunit protein
Sequence:
MSDPILQFEFPKIYSFPPFYTQQPNTTVLNQQLDSWVSIILHYCEYYRITSLSIEGIPKHSQLEVPLSSLSSIFINKTINRQVNSDFQKLIVKHLIHNKKAEFINPKKPELGVYIYWRSLVDWGDLLYQYVDDTGQKGTVLTIYELTKSEETTVPQDLHNLDETFLVKIIKDYLIKQGKAQLLIDENNEIGGVKIV
Protein: Iminosuccinate reductase (EC 1.4.1.-) (A1B8Z0)
Organism: Paracoccus denitrificans (strain Pd 1222)
Function: Imine reductase that catalyzes the NADH-dependent reduction of iminosuccinate to L-aspartate. Is essential for the growth of P.denitrificans in the presence of glycolate and glyoxylate since it functions in glyoxylate assimilation via the beta-hydroxyaspartate cycle (BHAC). Thereby BhcD regenerates the amino group donor for the first step of the BHAC.
Interaction partners:
- 3-hydroxy-D-aspartate aldolase
- beta-hydroxyaspartate dehydratase
- Bifunctional protein PutA
- Arginase
- Delta
- Ornithine cyclodeaminase
- Proline racemase
- ornithine decarboxylase
- Arginase/agmatinase/formiminoglutamase
- Pyrroline-5-carboxylate reductase
Sequence:
MLVVAEKEIAGLMTPEAAFEAIEAVFASMARRKAYNFPVVREAIGHEDALYGFKGGFDASALVLGLKAGGYWPNNQKHNLINHQSTVFLFDPDTGRVSAAVGGNLLTALRTAAASAVSIKYLAPKGAKVLGMIGAGHQSAFQMRAAANVHRFEKVIGWNPHPEMLSRLADTAAELGLPFEAVELDRLGAEADVIVSITSSFSPLLMNEHVKGPTHIAAMGTDTKGKQELDPALVARARIFTDEVAQSVSIGECQHAIAAGLIREDQVGELGAVVAGDDPGRGDAEVTIFDGTGVGLQDLAVAQAVVELAKHKGVAQEVEI