wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 460 (Zinc finger protein 272) (Zinc finger protein HZF8) (Q14592)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription intermediary factor 1-beta
Sequence:
MAAAWMAPAQESVTFEDVAVTFTQEEWGQLDVTQRALYVEVMLETCGLLVALGDSTKPETVEPIPSHLALPEEVSLQEQLAQGVPRYSYLGQAMDQDGPSEMQEYFLRPGTDPQSEKLHGKMSLEHEGLATADGICSMMIQNQVSPEDALYGFDSYGPVTDSLIHEGENSYKFEEMFNENCFLVQHEQILPRVKPYDCPECGKAFGKSKHLLQHHIIHTGEKPYKCLECGKDFNRRSHLTRHQRTHNGDKPFVCSECGRTFNRGSHLTRHQRVHSGEKPFVCNECGKAFTYRSNFVLHNKSHNEKKPFACSECGKGFYESTALIQHFIIHTGERPFKCLECGKAFNCRSHLKQHERIHTGEKPFVCSQCGKAFTHYSTYVLHERAHTGEKPFECKECGKAFSIRKDLIRHFNIHTGEKPYECLQCGKAFTRMSGLTRHQWIHTGEKPYVCIQCGKAFCRTTNLIRHFSIHTGEKPYECVECGKAFNRRSPLTRHQRIHTAEKSHEPIQSGNVSCESTDLIQHSIIHTESSPVSAVNMETPSIAAHSSSLDINGFIVEETLPL
Protein: Phospholipase D1 (PLD 1) (rPLD1) (EC 3.1.4.4) (Choline phosphatase 1) (Phosphatidylcholine-hydrolyzing phospholipase D1) (P70496)
Organism: Rattus norvegicus (Rat)
Function: Function as phospholipase selective for phosphatidylcholine (By similarity). Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic (By similarity).
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9Z280}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}. Late endosome membrane {ECO:0000250|UniProtKB:Q9Z280}; Lipid-anchor {ECO:0000250|UniProtKB:Q9Z280}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z280}.
Interaction partners:
- Ras-related protein Ral-A
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Transforming protein RhoA
- ADP-ribosylation factor 1
- Ras-related protein Ral-B
- ADP-ribosylation factor 6
- Phosphatidate cytidylyltransferase 2
- Phosphatidate cytidylyltransferase 1
- spleen exonuclease
- Cholinephosphotransferase 1
Sequence:
MSLRSEARVNTSTLQKIAADMSNLIENLDTRELHFEGEEVEYDASPGDPTAQEACIPFSSIYNTQGFKEPNIQIYLSGCPVKAQVLEVERFTSTSRMPSVNLYTIELTHGEFTWQVKRKFKHFQEFHRELLKYKAFIRIPIPTKRHTFRRQNVKEEPREMPSLPRSSENAIQEEQFFGRRKQLEDYLTKILKMPMYRNYHATTEFLDVSQLSFIHDLGPKGLEGMIMKRSGGHRIPGVNCCGHGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFRIKVGKKETETKYGLRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTDFLKDHRFGSYAAVHENILAKWYVNAKGYFEDIANAMEGATEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSSVYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGQSLGSLTAASVESMESLSLKDKHQSHKNEPVLKSVNDTDMKLKGIGKSRKFSKFSLYRQLHRRNLHNSDSISSVDSASSYFNHYRSHQNLIHGIKPHLKLFRPSSESEQGLTRHSADTGSIRSVQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPRMPWHDIGSVVHGKAARDVARHFIQRWNFTKIMKPKYRSLSYPFLLPKSQATAHELRYQVPGAVHAKAQLLRSAADWSAGIKHHEESIHAAYTHVIENSKHYIYIENQFFISCADDKVVFNKVGNAIAQRILKAHREGQRYRVYIVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGESSILEQLKPELGNKWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFAQGLRLECFRLVLGYLSDPSEDIQDPVSDKFFKEIWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPILAKEDRLRAEEELRKIRGFLVQFPFYFLSEENLLPSVGTKEAIVPMEVWT
Protein: X-linked lymphocyte-regulated protein 3B (Q6P205)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSSRKRKATDTAGRHSRMDPNLSSDDSQNPGAVAAANREVLDAGREDIISSGTERQQARKEKQDLVQEFEEPPNKVLQENRERFSRIMTSSFSAMEVKIKDVLKTHCEERQKLCQDYSLQFTNLNRKLTSDAYKLKKHAETLSNMFMEQQKFIHESLTLQKNRMKEFKSLCEKYLEKLEVLRDSRGNSIAEELRRLIATLEIKLLMLHNQQKTAAPPQSLLDVLFS
Protein: Patched domain-containing protein 3 (M0R3Q7)
Organism: Rattus norvegicus (Rat)
Function: May play a role in sperm development or sperm function. However, does not appear to have an essential role in spermatogenesis or male fertility.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:17904097}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q3KNS1}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the midpiece of the sperm tail. {ECO:0000269|PubMed:17904097}.
Interaction partners:
- Protein dispatched homolog 3
Sequence:
MISSKVAPGEEEEQQEAPAEVAPAEEELRETEGQLEAVPPDEASPSWATGPPLERLPPVGQEAPPPRRCHTDCLEAPLSSCFLRLGALVGANPWLFLLGPVLLTASLGTGLIFLPKEKENLEEQYTPIGSPAKAERRFVQSHFSTNDSYRFSASRTSSETNFASILVVSHRDSLLEPEAFAEVSRLDRAVQALKVVQENGTQILYPEVCAKYSVGCVPPNPLLFSWQQNSSLNLSELTFPIHSVADHLIHLAGFFGGNVLGYATTGNRQRLVESRAMRLLYYLKTEDPEDRERSQAWLTHFLDHFNDMKSDLALEDIEVVYFTSLSRQLEFEATSKTVIPLFHLAYILIILFAVVSCSRLDCIRNKMWVAVFGVFSVAMSVVSGFGLMLHIGVPFVIIVANSPFLILGVGVDDMFIMISAWQKTSLTESVSERLSNSYSKVAVSITITTITNVLAFYTGITSSFRSVQYFCIYTGTTLLFCYFYSITCFGAIMALDGKREVVWSRWLEKPDQKYSSFKKFCCVPFGSFPDEHGDDNHPMNLFFRDYFGPFLTTSKAKFIVVLIYIFYIISSIYGCFQVQEGLDLRNLASDDSYITPYFNVEEDYFSDYGPRVMVIVTETVNYWDKDVRQKLDKCMTQFEQNEYVDKNLTEFWLEAYMQYMNNTGNNPNDKNTFMNNIAGFLNFFPVFTYDINVSSSNEITSSRGFIQTIDVSSSSNKKRMLLKLRGIAENCEVPLMVYNQAFIYFDQYAAIIENTVRNVMIASTAMFIVSLLLIPHPVCSLWVTFAIASVIVGVTGFMAFWNVNLDSISMINLVICIGFSFDFSAHISYAFVSSNEPSVNKKSIEALYLLGYPVLQSAISTIIGVCVLAAAKAYIFRTFFKIMFLVMFFGAAHGLIFIPVFLTFF
Protein: Abscisic acid receptor PYL7 (ABI1-binding protein 7) (PYR1-like protein 7) (Regulatory components of ABA receptor 2) (Q1ECF1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor for abscisic acid (ABA) required for ABA-mediated responses such as stomatal closure and germination inhibition. Inhibits the activity of group-A protein phosphatases type 2C (PP2Cs) when activated by ABA.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9FLB1}. Nucleus {ECO:0000250|UniProtKB:O49686}. Cell membrane {ECO:0000250|UniProtKB:O49686}. Note=Localizes at the plasma membrane in the presence of a CAR protein. {ECO:0000250|UniProtKB:O80920}.
Interaction partners:
- Protein phosphatase 2C 16
- Protein phosphatase 2C 56
- Protein phosphatase 2C 37
- Protein phosphatase 2C 3
- Protein phosphatase 2C 77
- Probable protein phosphatase 2C 75
- Probable protein phosphatase 2C 24
- Probable protein phosphatase 2C 78
- Protein phosphatase 2C 7
- Serine/threonine-protein kinase SRK2D
Sequence:
MEMIGGDDTDTEMYGALVTAQSLRLRHLHHCRENQCTSVLVKYIQAPVHLVWSLVRRFDQPQKYKPFISRCTVNGDPEIGCLREVNVKSGLPATTSTERLEQLDDEEHILGINIIGGDHRLKNYSSILTVHPEMIDGRSGTMVMESFVVDVPQGNTKDDTCYFVESLIKCNLKSLACVSERLAAQDITNSIATFCNASNGYREKNHTETNL
Protein: Bacterial blight resistance protein XA26 (Q00KZ8)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
Sequence:
MALVRLPVWIFVAALLIASSSTVPCASSLGPIASKSNSSDTDLAALLAFKAQLSDPNNILAGNWTTGTPFCRWVGVSCSSHRRRRQRVTALELPNVPLQGELSSHLGNISFLFILNLTNTGLTGSVPNKIGRLRRLELLDLGHNAMSGGIPAAIGNLTRLQLLNLQFNQLYGPIPAELQGLHSLGSMNLRHNYLTGSIPDDLFNNTPLLTYLNVGNNSLSGLIPGCIGSLPILQHLNFQANNLTGAVPPAIFNMSKLSTISLISNGLTGPIPGNTSFSLPVLRWFAISKNNFFGQIPLGLAACPYLQVIAMPYNLFEGVLPPWLGRLTNLDAISLGGNNFDAGPIPTELSNLTMLTVLDLTTCNLTGNIPADIGHLGQLSWLHLAMNQLTGPIPASLGNLSSLAILLLKGNLLDGSLPSTVDSMNSLTAVDVTENNLHGDLNFLSTVSNCRKLSTLQMDLNYITGILPDYVGNLSSQLKWFTLSNNKLTGTLPATISNLTALEVIDLSHNQLRNAIPESIMTIENLQWLDLSGNSLSGFIPSNTALLRNIVKLFLESNEISGSIPKDMRNLTNLEHLLLSDNKLTSTIPPSLFHLDKIVRLDLSRNFLSGALPVDVGYLKQITIMDLSDNHFSGRIPYSIGQLQMLTHLNLSANGFYDSVPDSFGNLTGLQTLDISHNSISGTIPNYLANFTTLVSLNLSFNKLHGQIPEGGVFANITLQYLEGNSGLCGAARLGFPPCQTTSPNRNNGHMLKYLLPTIIIVVGIVACCLYVVIRKKANHQNTSAGKADLISHQLLSYHELLRATDDFSDDSMLGFGSFGKVFRGRLSNGMVVAIKVIHQHLEHAMRSFDTECRVLRMARHRNLIKILNTCSNLDFRALVLQYMPKGSLEALLHSEQGKQLGFLERLDIMLDVSMAMEYLHHEHYEVVLHCDLKPSNVLFDDDMTAHVADFGIARLLLGDDNSMISASMPGTVGYMAPEYGTLGKASRKSDVFSYGIMLLEVFTAKRPTDAMFVGELNIRQWVQQAFPAELVHVVDCQLLQDGSSSSSSNMHDFLVPVFELGLLCSADSPEQRMAMSDVVLTLNKIRKDYVKLMATTVSVVQQ
Protein: Meiotic recombination protein DMC1 homolog B (OsDMC1B) (RiLIM15B) (Q7GBF7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Recombinase that may participate in meiotic recombination, specifically in homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks (By similarity). Exhibits DNA-dependent ATPase activity when bound to single-stranded DNA (ssDNA). Mediates renaturation of homologous complementary strands as well as assimilation of single strands into homologous supercoiled duplexes leading to D-loop formation (By similarity). Binds circular single-stranded DNA (ssDNA) and circular double-stranded DNA (dsDNA) in vitro (By similarity). Catalyzes DNA homologous renaturation and DNA strand exchange. The rates of these activities are dependent on the state of ATP hydrolysis (By similarity). Forms helical filaments along ssDNA and dsDNA, and promotes strand exchange between ssDNA and dsDNA with long DNA substrates of several thousand base pairs. The presence of the replication protein A is not required for this activity. Seems to be required for homologous pairing and subsequent chromosome segregation during male meiosis (By similarity). May be not directly required for homologous pairing during male meiosis. Required for synaptonemal complex assembly and crossover formation. Functions redundantly with DMC1A.
Subcellular location: Nucleus {ECO:0000269|PubMed:26960731}.
Interaction partners:
- Os02g0562100 protein
- Os01g0164900 protein
- Os01g0164800 protein
- Os01g0660500 protein
- ATP-dependent DNA helicase
- Kinetochore protein NDC80
- Crossover junction endonuclease MUS81
- Os03g0639700 protein
- Proliferating cell nuclear antigen
- Os09g0104200 protein
Sequence:
MAPSKQYDEGGQLQLMDAERIEEEEECFESIDKLISQGINSGDVKKLQDAGIYTCNGLMMHTKKSLTGIKGLSEAKVDKICEAAEKLLSQGFMTGSDLLIKRKSVVRITTGSQALDELLGGGIETLCITEAFGEFRSGKTQLAHTLCVSTQLPIHMHGGNGKVAYIDTEGTFRPERIVPIAERFGMDANAVLDNIIYARAYTYEHQYNLLLGLAAKMAEEPFRLLIVDSVIALFRVDFSGRGELAERQQKLAQMLSRLTKIAEEFNVAVYITNQVIADPGGGMFITDPKKPAGGHVLAHAATIRLMLRKGKGEQRVCKIFDAPNLPEGEAVFQVTSGGIMDAKD
Protein: Ubiquitin-conjugating enzyme E2 J2 (EC 2.3.2.23) (Non-canonical ubiquitin-conjugating enzyme 2) (NCUBE-2) (Q6P073)
Organism: Mus musculus (Mouse)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11278356, ECO:0000269|PubMed:12082160}; Single-pass type IV membrane protein {ECO:0000269|PubMed:11278356, ECO:0000269|PubMed:12082160}.
Interaction partners:
- Adaptin ear-binding coat-associated protein 2
- Beta-1,3-galactosyltransferase 6
- Ubiquitin-conjugating enzyme E2 W
- Adaptin ear-binding coat-associated protein 1
- E3 ubiquitin-protein ligase MARCHF6
- Ubiquitin-conjugating enzyme E2 S
- Ubiquitin-conjugating enzyme E2 H
- Ubiquitin-conjugating enzyme E2 L3
- Ubiquitin-conjugating enzyme E2 G2
- Ubiquitin-conjugating enzyme E2 variant 2
Sequence:
MSNNSNKRAPTTATQRLKQDYLRIKKDPVPYICAEPLPSNILEWHYVVRGPEMTPYEGGYYHGKLIFPREFPFKPPSIYMITPNGRFKCNTRLCLSITDFHPDTWNPAWSVSTILTGLLSFMVEKGPTLGSIETSDFTKKQLAAQSLVFNLKDKVFCELFPEVVEEIKQKQKAQDELSNRPQNLPLPDVVPDGELHRGQHGIQLLNGHAPAAGPNLAGLPQANRHHGLLGGALANLFVIVGFAAFAYTVKYVLRSIAQE
Protein: DnaJ (Hsp40) homolog, subfamily B, member 1 (DnaJ homolog subfamily B member 1a) (Q6DEJ4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGKDYYRILGIEKGASDEEIKKAYRKQALRFHPDKNKSAGAEDKFKEIAEAYDVLSDAKKKDIYDRYGEDGLKGHAGSGTNGPSYTFHGDPHAMFAEFFGGRSPFDHFFASAGGPNDGMDIDDPFGAFGMGGMGGFPRSFKSRVGGPHGSREKKKDPPVVHELKVSLEEVFAGCTKKMKISRKRLNPDGCSMRNEDKILTVDIKRGWKEGTKITFPKEGDETPTNIPADIVFVVKDKIHSVFRRDGSDIIYPARISLREALCGCTINAPTLDGRTVTVSSRDVIKPGMKKRIVGEGLPLSKCPEKRGDMVLEFSVKFPDKLGPGAREALVQILPP
Protein: Endochitinase CHI (EC 3.2.1.14) (O24603)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein DMR6-LIKE OXYGENASE 1
- Glucan endo-1,3-beta-glucosidase, acidic isoform
- Germin-like protein subfamily 1 member 13
- Curculin-like
- Probable LRR receptor-like protein kinase At1g51890
- Aspartyl protease AED1
- PLC-like phosphodiesterases superfamily protein
- Subtilisin-like protease SBT3.5
- HXXXD-type acyl-transferase family protein
- Berberine bridge enzyme-like 26
Sequence:
MAKPTSRNDRFALFFITLIFLILTVSKPVASQNCGCASDFCCSKYGYCGTTDEFCGEGCQAGPCRSSGGGGDPAVSLEGTVTPDFFNSILNQRGDCPGKGFYTHDTFMAAANSYPSFGASISKREIAAFFAHVAQETGFMCYIEEIDGPAKAASGEYCDTEKPEFPCAQGKGYYGRGAIQLSWNYNYGLCGKALDENLLASPEKVAQDQVLAFKTAFWFWTTNVRTSFKSGFGATIRAVNSRECSGGDSTAKAANRIKYFQDYCGKLGVAPGDNLTC
Protein: Protein FAM221A (A4D161)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MERLTLPLGGAAAVDEYLEYRRIVGEDDGGKLFTPEEYEEYKRKVLPLRLQNRLFVSWRSPTGMDCKLVGPETLCFCTHRYKQHKTDLEAIPQQCPIDLPCQVTGCQCRAYLYVPLNGSQPIRCRCKHFADQHSAAPGFTCNTCSKCSGFHSCFTCACGQPAYAHDTVVETKQERLAQEKPVGQDIPYAAMGGLTGFSSLAEGYMRLDDSGIGVPSVEFLESPITAVDSPFLKAFQASSSSSPETLTDVGTSSQVSSLRRPEEDDMAFFERRYQERMKMEKAAKWKGKAPLPSATKPS
Protein: Rho-related protein racB (P34148)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Rac guanine nucleotide exchange factor B
- Serine/threonine-protein kinase pakC
- Uncharacterized protein
- Ras guanine nucleotide exchange factor S
- Serine/threonine-protein kinase pakB
- GTPase activating protein homolog 1
- Putative rho GDP-dissociation inhibitor 1
- Mss4-like family protein
- Cofilin-1A
- Protein pirA
Sequence:
MQSIKLVVVGDGAVGKTCLLISYTSNSFPTEYVPTVFDNYSANVMVDNKTVSLGLWDTAGQEDYDRLRPLSYPQTDVFLICFAIISQTSYTNVKSKWWPEVTHHCPNCTIILVGTKCDLREDKESLEKLREKHQQPLTFQQGEQMAKEIKAFCYMECSALTQKGLKQVFDEAIKAVIFPDRDKATNKKNSKCSIL
Protein: E3 ubiquitin-protein ligase SINA-like 7 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SINA-like 7) (Seven in absentia-like protein 7) (Q9FKD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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. It probably triggers the ubiquitin-mediated degradation of different substrates.
Interaction partners:
Sequence:
MVGAAILESPGEGIGSNSILSQKRQLSSSDAAKRDAKKRSTMLMDLEILDCPICYEAFTIPIFQCDNGHLACSSCCPKLNNKCPACTSPVGHNRCRAMESVLESILIPCPNAKLGCKKNVSYGKELTHEKECMFSHCACPALDCNYTSSYKDLYTHYRITHMEINQINTFICDIPLSVRMNISKKILIRTEHLTNHLFAVQCFREPYGVYVTVSCIAPSSPELSQYSYALSYTVDGHTVIYQSPEVKRVLKLSFQTPQENFMLIPNSLLRGDVLEMRISVKKLNKE
Protein: Serine protease SPPA, chloroplastic (EC 3.4.21.-) (Signal peptide peptidase SPPA) (Q9C9C0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine protease that may be involved in the light-dependent degradation of antenna and photosystem II in chloroplasts. May function during high light acclimation in plastids.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:11443110}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:11443110}. Note=Mostly exposed to the stroma but behaves as an intrinsic membrane protein.
Interaction partners:
- Ketose-bisphosphate aldolase class-II family protein
- Triosephosphate isomerase, chloroplastic
- Triosephosphate isomerase, cytosolic
- Xaa-Pro dipeptidase
- At1g17940
- Phosphoglycerate kinase 3, cytosolic
- Phosphoglycerate kinase 1, chloroplastic
- Phosphoglycerate kinase 2, chloroplastic
- Scarecrow-like protein 8
- Endosomal targeting BRO1-like domain-containing protein
Sequence:
MAKLLLLHAPHVIPRFSSSSSRSLVSAAALYRRPLLVNPQFSHIGPRLHSPYNRRFSARAFDDSPASSAEMEKEKQEQLLDGVSGKKDEDYPTGEMEYENRNAWEIFVVKFRMLFAYPWQRVRKGSVLTMTLRGQISDQLKSRFNSGLSLPQLSENFVKAAYDPRIAGVYLHIDPLSCGWGKVEEIRRHILNFKKSGKFIVGYISICGLKEYYLGCACNELFAPPSAYSFLYGLTVQASFLGGVFEKVGIEPQVQRIGKYKSAGDQLSRKSISEENYEMLSVLLDNIYSNWLDGVSDATGKKREDVENFINQGVYEIEKLKEAGLIKDIRYDDEVITMLKERLGVEKDKKLPTVDYKKYSGVKKWTLGLTGGRDQIAIIRAGGSISRVKGPLSTPGSAIIAEQLIEKIRSVRESKKYKAAIIRIDSPGGDALASDLMWREIKLLAETKPVIASMSDVAASGGYYMAMAANAIVAENLTLTGSIGVVTARFTLAKLYEKIGFNKETISRGKYAELLGAEERPLKPEEAELFEKSAQHAYQLFRDKAALSRSMPVDKMEEVAQGRVWTGKDAHSRGLIDAVGGLSRAIAIAKQKANIPLNKKVTLVELSRPSTSLPDILSGIGSSVIGVDRTLKGLLDELTITEGVQARMDGIMFQQLGRDSLATPIIDMLKDYLSSLR
Protein: Calcium-binding protein 39 (MO25alpha) (Protein Mo25) (Q9Y376)
Organism: Homo sapiens (Human)
Function: Component of a complex that binds and activates STK11/LKB1. In the complex, required to stabilize the interaction between CAB39/MO25 (CAB39/MO25alpha or CAB39L/MO25beta) and STK11/LKB1.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Serine/threonine-protein kinase STK11
- STE20-related kinase adapter protein beta
- STE20-related kinase adapter protein alpha
- Serine/threonine-protein kinase 25
- Serine/threonine-protein kinase 24
- Serine/threonine-protein kinase 26
- Calcium-binding protein 39-like
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- STE20/SPS1-related proline-alanine-rich protein kinase
Sequence:
MPFPFGKSHKSPADIVKNLKESMAVLEKQDISDKKAEKATEEVSKNLVAMKEILYGTNEKEPQTEAVAQLAQELYNSGLLSTLVADLQLIDFEGKKDVAQIFNNILRRQIGTRTPTVEYICTQQNILFMLLKGYESPEIALNCGIMLRECIRHEPLAKIILWSEQFYDFFRYVEMSTFDIASDAFATFKDLLTRHKLLSAEFLEQHYDRFFSEYEKLLHSENYVTKRQSLKLLGELLLDRHNFTIMTKYISKPENLKLMMNLLRDKSRNIQFEAFHVFKVFVANPNKTQPILDILLKNQAKLIEFLSKFQNDRTEDEQFNDEKTYLVKQIRDLKRPAQQEA
Protein: Mitochondrial fission process protein 1 (Mitochondrial 18 kDa protein) (MTP18) (Q9UDX5)
Organism: Homo sapiens (Human)
Function: Involved in the mitochondrial division probably by regulating membrane fission. Loss-of-function induces the release of cytochrome c, which activates the caspase cascade and leads to apoptosis.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:15155745, ECO:0000305|PubMed:15985469}; Multi-pass membrane protein {ECO:0000305|PubMed:15155745, ECO:0000305|PubMed:15985469}.
Interaction partners:
- Dynamin-1-like protein
Sequence:
MSEPQPRGAERDLYRDTWVRYLGYANEVGEAFRSLVPAAVVWLSYGVASSYVLADAIDKGKKAGEVPSPEAGRSARVTVAVVDTFVWQALASVAIPGFTINRVCAASLYVLGTATRWPLAVRKWTTTALGLLTIPIIIHPIDRSVDFLLDSSLRKLYPTVGKPSSS
Protein: Geranylgeranyl transferase type-2 subunit alpha (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit alpha) (Rab geranyl-geranyltransferase subunit alpha) (Rab GG transferase alpha) (Rab GGTase alpha) (Rab geranylgeranyltransferase subunit alpha) (Q9JHK4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit beta
- Rab proteins geranylgeranyltransferase component A 1
- Rab proteins geranylgeranyltransferase component A 2
- Ras-related protein Rab-31
- Ras-related protein Rab-22A
- Ras-related protein Rab-32
- Ras-related protein Rab-24
- Ras-related protein Rab-39A
- Geranylgeranyl transferase type-1 subunit beta
- Ras-related protein Rab-1B
Sequence:
MHGRLKVKTSEEQAEAKRLEREQKLKLYQSATQAVFQKREAGELDESVLELTSQILGANPDFATLWNCRREVLQQLETQKSPEELAALVKAELGFLESCLRVNPKSYGTWHHRCWLLSRLPEPNWARELELCARFLEADERNFHCWDYRRFVAAQAAVAPAEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQGRLPENVLLRELELVQNAFFTDPNDQSAWFYHRWLLGRAEPHDVLCCLHVSREEACLSVCFSRPLIVGSKMGTLLLTVDEAPLSVEWRTPDGRNRPSHVWLCDLPAASLNDHLPQHTFRVIWTGSDTQKECVLLKGHQECWCRDSATDEQLFRCELSVEKSTVLQSELESCKELQELEPENKWCLLTIILLMRALDPLLYEKETLEYFSTLKAVDPMRAAYLDDLRSKFLVENSVLKMEYADVRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRALPPALAALRCLEVLQASDNVLENLDGVANLPRLRELLLCNNRLQQSAALQTLASCPRLVFLNLQGNSLCQEEGIRERLAEMLPSVSSILT
Protein: Glucosylglycerate phosphorylase (GGa phosphorylase) (GGaP) (EC 2.4.1.352) (P76041)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible phosphorolysis of glucosylglycerate into alpha-D-glucose 1-phosphate (Glc1P) and D-glycerate (also called (R)-glycerate). May be a regulator of intracellular levels of glucosylglycerate, a compatible solute that primarily protects organisms facing salt stress and very specific nutritional constraints. Cannot catalyze the phosphorolysis of sucrose. Does not act on other sugars such as alpha-D-galactose 1-phosphate, alpha-D-mannose 1-phosphate or beta-D-glucose 1-phosphate; in vitro D-erythronate can substitute for D-glycerate with a much lower efficiency.
Interaction partners:
- Putative ABC transporter periplasmic-binding protein YcjN
- Inner membrane ABC transporter permease protein YcjO
- Kojibiose phosphorylase
- Inner membrane ABC transporter permease protein YcjP
- 3-dehydro-D-guloside 4-epimerase
- D-guloside 3-dehydrogenase
- Beta-phosphoglucomutase
- D-glucoside 3-dehydrogenase
- Uncharacterized HTH-type transcriptional regulator YcjW
- Mannosyl-3-phosphoglycerate phosphatase
Sequence:
MKQKITDYLDEIYGGTFTATHLQKLVTRLESAKRLITQRRKKHWDESDVVLITYADQFHSNDLKPLPTFNQFYHQWLQSIFSHVHLLPFYPWSSDDGFSVIDYHQVASEAGEWQDIQQLGECSHLMFDFVCNHMSAKSEWFKNYLQQHPGFEDFFIAVDPQTDLSAVTRPRALPLLTPFQMRDHSTRHLWTTFSDDQIDLNYRSPEVLLAMVDVLLCYLAKGAEYVRLDAVGFMWKEPGTSCIHLEKTHLIIKLLRSIIDNVAPGTVIITETNVPHKDNIAYFGAGDDEAHMVYQFSLPPLVLHAVQKQNVEALCAWAQNLTLPSSNTTWFNFLASHDGIGLNPLRGLLPESEILELVEALQQEGALVNWKNNPDGTRSPYEINVTYMDALSRRESSDEERCARFILAHAILLSFPGVPAIYIQSILGSRNDYAGVEKLGYNRAINRKKYHSKEITRELNDEATLRHAVYHELSRLITLRRSHNEFHPDNNFTIDTINSSVMRIPRSNADGNCLTGLFNVSKNIQHVNITNLHGRDLISEVDILGNEITLRPWQVMWIK
Protein: Tubulin beta chain (Tubulin beta-5 chain) (Q767L7)
Organism: Sus scrofa (Pig)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7225365}.
Interaction partners:
- Stathmin 4.
- Tubulin alpha 4a
- Microtubule-associated protein
- Tubulin alpha chain
- Tubulin alpha-1B chain
- Tubulin alpha chain
- Gap junction alpha-1 protein
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
Sequence:
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDFGEEAEEEA
Protein: 4-hydroxyproline betaine 2-epimerase (Hyp-B 2-epimerase) (EC 5.1.1.22) ((4R)-4-hydroxyproline betaine 2-epimerase) (A1B198)
Organism: Paracoccus denitrificans (strain Pd 1222)
Function: Catalyzes the 2-epimerization of trans-4-hydroxy-L-proline betaine (tHyp-B) to cis-4-hydroxy-D-proline betaine (cHyp-B). Is involved in a catabolic pathway that degrades tHyp-B to alpha-ketoglutarate. This pathway would permit the utilization of tHyp-B as a carbon and nitrogen source in the absence of osmotic stress, since tHyp-B functions as an osmolyte and is not catabolized when it is needed as osmoprotectant. Can also catalyze the racemization of L-proline betaine.
Interaction partners:
- Rieske
- Catechol 1,2-dioxygenase
- Ferredoxin
- Glutathione-independent formaldehyde dehydrogenase
- Trans-3-hydroxy-L-proline dehydratase
Sequence:
MKIAEIHVYAHDLPVKDGPYTIASSTVWSLQTTLVKIVADSGLAGWGETCPVGPTYAPSHALGARAALAEMAPGLIGANPLQPLVLRRRMDGLLCGHNYAKAAIDIAAYDLMGKHYGVRVADLLGGVAAERVPSYYATGIGQPDEIARIAAEKVAEGFPRLQIKIGGRPVEIDIETVRKVWERIRGTGTRLAVDGNRSLPSRDALRLSRECPEIPFVLEQPCNTLEEIAAIRGRVQHGIYLDESGEDLSTVIRAAGQGLCDGFGMKLTRIGGLQQMAAFRDICEARALPHSCDDAWGGDIIAAACTHIGATVQPRLNEGVWVAQPYIAQPYDEENGIRIAGGHIDLPKGPGLGITPDESLFGPPVASFS