wanglab/gogpt-training-data huggingface dataset:
Protein: Glucan endo-1,3-beta-D-glucosidase 1 (Endo-1,3-beta-glucanase 1) (EC 3.2.1.39) (Laminarinase) (RmLam81A) (A0A023I7E1)
Organism: Rhizomucor miehei
Function: Cleaves internal linkages in 1,3-beta-glucan.
Subcellular location: Secreted, cell wall {ECO:0000250|UniProtKB:P53753}.
Interaction partners:
Sequence:
MRFQVIVAAATITMITSYIPGVASQSTSDGDDLFVPVSNFDPKSIFPEIKHPFEPMYANTENGKIVPTNSWISNLFYPSADNLAPTTPDPYTLRLLDGYGGNPGLTIRQPSAKVLGSYPPTNDVPYTDAGYMINSVVVDLRLTSSEWSDVVPDRQVTDWDHLSANLRLSTPQDSNSYIDFPIVRGMAYITANYNNLTPQFLSQHAIISVEADEKKSDDNTSTFSGRKFKITMNDDPTSTFIIYSLGDKPLELRKQDNSNLVASKPYTGVIRVAKLPAPEFETLLDASRAVWPTGGDISARSDDNNGASYTIKWKTNSNEAPLLTYAYAHHLTSIDDSNVKRTDMTLQSATKGPMTALVGNEWTLRETELSPVEWLPLQAAPNPTTINEIMTEINKDIASNYTQETAKEDNYFSGKGLQKFAMLALILNKSDQTQLRNPELAQIALDKLKAAFLPYLQNEQADPFRYDTLYKGIVAKAGLPTSMGGTDDLSAEFGHSYYSDHHYHQGYFVVTAAIIHHLDPTWNADRLKAWTEALIRDVNNANDGDEYFAAFRNWDWFAGHSWAGGIKPDGALDGRDQESVPESVNFYWGAKLWGLATGNTPLTKLASLQLAVTKRTTYEYFWMLDGNKNRPENIVRNKVIGIYFEQKTDYTTYFGRFLEYIHGIQQLPMTPELMEYIRTPEFVSQEWDEKLGAIAPTVQSPWAGVLYLNYAIINPAEAYPALRKVQMDDGQTRSYSLYLTATRPHFFRRSLLAALARHGSTRRPSLPSSGDDDKHEDGFLLRFRRLNPFNLKHRIY
Protein: AT0ZI1 protein (ATOZI1 protein) (Monopolar spindle protein (DUF1138)) (Stress-induced protein OZI1) (Q38842)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DUF724 domain-containing protein 6
- Blue-light photoreceptor PHR2
Sequence:
MSRATYIIGALAGSAVVAYVCDKVISDDKLFGGTTPGTITNKEWGAATEERLQAWPRVAGPPVVMNPISRQNFIVKSRPE
Protein: Eukaryotic translation initiation factor 4C (Q5XJR0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPKNKGKGGKNRRRGKNENESEKRELVFKEDGQEYAQVIKMLGNGRLEAMCFDGVKRLCHIRGKLRKKVWINTSDIILVGLRDYQDVKADVILKYNADEARSLKAYGELPEHAKINETDTFGPGDDDEILFDDIGENDDDIDDI
Protein: Iron transport multicopper oxidase fio1 (EC 1.-.-.-) (Q09920)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Could be an iron transport multicopper oxidase, which is required for Fe(2+) high affinity uptake. May be required to oxidize Fe(2+) and release it from the transporter. Essential component of copper-dependent iron transport.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}.
Interaction partners:
- Plasma membrane iron permease
- Ferric reductase transmembrane component 1
- Copper-transporting ATPase ccc2
- Iron-sensing transcriptional repressor
- Siderophore iron transporter 1
- Ferric/cupric reductase transmembrane component 2
- Copper transport protein ctr5
- L-ornithine N
- Vacuolar heme ABC transmembrane exporter abc3
- Manganese transporter pdt1
Sequence:
MNKFFSFPILGLLLTCVRFVVAKERLFEWNVTDVYDVDPDGSGNSRWVIGVNNKWPIDPLVVDYGDQVIIKMTNSLANNRTTSLHSHGLFQKFTPYMDGVPQSTQCEIPPGATFYYNYTALQNGTYWVHSHDMSQYPDGLRTPFIINALEEPYDYDEEYIISMTDWYYTPFNILVPDEFKTWKNPTGAEPVPDTGLFNDTANATFAMEPGKTYRLRFINIGAFNNYDVMIEDHNMTIIEVDGEYTEPQEVSSIHLTVAQRYSVLVTAKNSTDRNYAITAYMDESLFDTIPDNYNPNVTAWLSYNSDASYDLGPDIDEIDSYDDAELNPLYSWDVTESNHSINIWFDFFTLGDGANYAEINDSSYVFPKVPSIMIANSTNVDGYNLEPVTYGPYTNAYIFEYGDVVDVIIDNHDTGKHPFHLHGHTFQVLERGEENAGLYSDQESHTYYDNPMRRDTVEIEPGSFIVIRFIADNPGAWVIHCHIEWHMESGLLATFIEAPEMIPSISSPDFVKEQCMLDGVPTIGNGAGNYKNISDLSGAPSPPGEMPAGWTSKAIGTMAACVISACIGMGSIIFYGASIHPVPTEELDENDDLQEAALENAAMFLDTDKAVEKVVEGKDEIK
Protein: Small ribosomal subunit protein eS1z (40S ribosomal protein S3a-1) (Q9CAV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122}.
Interaction partners:
- Small ribosomal subunit protein eS6z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein uS2z
- Small ribosomal subunit protein eS6y
- Probable elongation factor 1-gamma 2
- Small ribosomal subunit protein eS24y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein eL8z
- Large ribosomal subunit protein uL2y
Sequence:
MAVGKNKRISKGRKGGKKKAVDPFSKKDWYDVKAPSIFTHRNVGKTLVSRTQGTKIASEGLKHRVFEVSLADLQGDEDNAYRKIRLRAEDVQGRNVLCQFWGMDFTTDKLRSLVKKWQTLIEAHVDVKTTDSYTLRLFCIAFTKRRANQVKRTCYAQSSQIRQIRRKMRDIMVREASSCDLKDLVAKFIPEAIGREIEKATQGIYPLQNVFIRKVKILKAPKFDLGKLMDVHGDYSAEDVGVKVDRPADEMAVEEPTEIIGA
Protein: Cathepsin B (EC 3.4.22.1) (Cathepsin B1) [Cleaved into: Cathepsin B light chain; Cathepsin B heavy chain] (P10605)
Organism: Mus musculus (Mouse)
Function: Thiol protease which is believed to participate in intracellular degradation and turnover of proteins (By similarity). Cleaves matrix extracellular phosphoglycoprotein MEPE (By similarity). Involved in the solubilization of cross-linked TG/thyroglobulin in the thyroid follicle lumen. Has also been implicated in tumor invasion and metastasis (By similarity).
Subcellular location: Lysosome {ECO:0000269|PubMed:12782676}. Melanosome {ECO:0000250|UniProtKB:P07858}. Secreted, extracellular space {ECO:0000269|PubMed:12782676}. Apical cell membrane {ECO:0000269|PubMed:12782676}; Peripheral membrane protein {ECO:0000269|PubMed:12782676}; Extracellular side {ECO:0000269|PubMed:12782676}. Note=Localizes to the lumen of thyroid follicles and to the apical membrane of thyroid epithelial cells. {ECO:0000269|PubMed:12782676}.
Interaction partners:
- Cathepsin D
- NACHT, LRR and PYD domains-containing protein 3
- Procathepsin L
- H-2 class II histocompatibility antigen gamma chain
- Cathepsin S
- Caspase-1
- Apoptosis regulator Bcl-2
- Annexin A2
- Cystatin-A
- Bcl-2-like protein 1
Sequence:
MWWSLILLSCLLALTSAHDKPSFHPLSDDLINYINKQNTTWQAGRNFYNVDISYLKKLCGTVLGGPKLPGRVAFGEDIDLPETFDAREQWSNCPTIGQIRDQGSCGSCWAFGAVEAISDRTCIHTNGRVNVEVSAEDLLTCCGIQCGDGCNGGYPSGAWSFWTKKGLVSGGVYNSHVGCLPYTIPPCEHHVNGSRPPCTGEGDTPRCNKSCEAGYSPSYKEDKHFGYTSYSVSNSVKEIMAEIYKNGPVEGAFTVFSDFLTYKSGVYKHEAGDMMGGHAIRILGWGVENGVPYWLAANSWNLDWGDNGFFKILRGENHCGIESEIVAGIPRTDQYWGRF
Protein: G-protein coupled receptor 151 (G-protein coupled receptor PGR7) (GPCR-2037) (Galanin receptor 4) (Galanin-receptor-like protein) (GalRL) (Q8TDV0)
Organism: Homo sapiens (Human)
Function: Proton-sensing G-protein coupled receptor.
Subcellular location: Cell membrane {ECO:0000305|PubMed:31119277}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Galanin peptides
Sequence:
MLAAAFADSNSSSMNVSFAHLHFAGGYLPSDSQDWRTIIPALLVAVCLVGFVGNLCVIGILLHNAWKGKPSMIHSLILNLSLADLSLLLFSAPIRATAYSKSVWDLGWFVCKSSDWFIHTCMAAKSLTIVVVAKVCFMYASDPAKQVSIHNYTIWSVLVAIWTVASLLPLPEWFFSTIRHHEGVEMCLVDVPAVAEEFMSMFGKLYPLLAFGLPLFFASFYFWRAYDQCKKRGTKTQNLRNQIRSKQVTVMLLSIAIISALLWLPEWVAWLWVWHLKAAGPAPPQGFIALSQVLMFSISSANPLIFLVMSEEFREGLKGVWKWMITKKPPTVSESQETPAGNSEGLPDKVPSPESPASIPEKEKPSSPSSGKGKTEKAEIPILPDVEQFWHERDTVPSVQDNDPIPWEHEDQETGEGVK
Protein: Dynactin subunit 3 (Dynactin light chain p24) (Q9Z0Y1)
Organism: Mus musculus (Mouse)
Function: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). Together with dynein may be involved in spindle assembly and cytokinesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O75935}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O75935}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:O75935}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O75935}. Cleavage furrow {ECO:0000250|UniProtKB:O75935}. Midbody {ECO:0000250|UniProtKB:O75935}. Note=Localizes to punctate cytoplasmic structures and to the centrosome during interphase, and to kinetochores and to spindle poles throughout mitosis. Colocalizes with dynein to the cleavage furrow and to midbody of dividing cells. {ECO:0000250|UniProtKB:O75935}.
Interaction partners:
- Dynactin subunit 2
- Dynactin subunit 6
- Dynactin subunit 1
- Dynactin subunit 4
- Dynactin subunit 5
- Actin-related protein 10
- Alpha-centractin
- Beta-centractin
- Cytoplasmic dynein 1 intermediate chain 2
- Cytoplasmic dynein 1 heavy chain 1
Sequence:
MAALTDVQRLQSRVEELERWVYGPGGTRGSRKVADGLVKVQVALGNIASKRERVKILYKKIEDLIKYLDPEYIDRIAIPEASKLQFILAEEQFILSQVALLEQVNALVPVLDSASIKAVPEHAARLQRLAQIHIQQQDQCVAITEESKALLEGYNKTTMLLSKQFVQWDELLCQLEAAKQVKPAEE
Protein: Cytochrome P450 3A (EC 1.14.14.-) (X5L1L5)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406, ECO:0000256|RuleBase:RU368049}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Microsome membrane {ECO:0000256|ARBA:ARBA00004174, ECO:0000256|RuleBase:RU368049}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004174}.
Interaction partners:
Sequence:
MDLIPSFSTETWLLLAISLVLLYLYGTYTHGIFRKLGIPGPTPLPFVGTALGYRNGFYVFDMKCFSKYGRMWGFYDGRQPVLAITDPDMIKTVLVKECYSVFTNRRTLGPVGFMKSAISLSEDEEWKRIRTLLSPTFTTGKLKEMFSIIGQYGDVLVNNLRKEAEKGKAINLKDVFGAYSMDVITSTSFGVNIDSLNHPQDPFVENTKKLLKFDFLDPFFFSILLFPFLTPVFEILNIWLFPKKVTDFFRKSVERMKESRLKDKQKHRVDFLQLMINSQNSKEMDTHKALSDLELVAQSIIFIFAGYETTSTSLSFLMYELATHPDVQQKLQEEIDATFPNKALPTYDALVQMEYLDMVLNETLRLYPIAGRLERVCKKDVEISGVFIPKGTVVMVPTFTLHRDQSLWPEPEEFRPERFSRKNKDSINPYTYLPFGTGPRNCIGMRFAIMNMKLALVRVLQNFSFKPCKETQIPLKLNAQGIIQPEKPIVLKVEPRDGSVNGA
Protein: 5-methyltetrahydrofolate-homocysteine methyltransferase reductase (H0Y9D5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XVRAGARLVEVALCRFVPGWRGVGLGDSEYTYFCNGGKIIDKRLQELGARHFYDTGHADDCVGLELVVEPWIAGLWPALRKHFRSSRGQEEISGALPVASPASSRTDLVKSELLHIESQVELLRFDDSGRKDSEVLKQNAVNSNQSNVVIEDFESSLTRS
Protein: Regulatory solute carrier protein family 1 member 1 (Regulatory subunit of SGLT1) (Transporter regulator RS1) (mRS1) (Q9ER99)
Organism: Mus musculus (Mouse)
Function: Mediates transcriptional and post-transcriptional regulation of SLC5A1. Inhibits a dynamin and PKC-dependent exocytotic pathway of SLC5A1. Also involved in transcriptional regulation of SLC22A2. Exhibits glucose-dependent, short-term inhibition of SLC5A1 and SLC22A2 by inhibiting the release of vesicles from the trans-Golgi network (By similarity). Regulates the expression of SLC5A1 in a tissue-specific manner and is specifically involved in its regulation in the small intestine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15601832}. Nucleus {ECO:0000269|PubMed:15601832}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Note=Localizes at the inner side of the plasma membrane.
Interaction partners:
- Protein DDI1 homolog 1
Sequence:
MSSLPTSDGFDHPAPSGQSPEVGSPTSLARSVSASVCAIKPGDPNSIESLAMEATKASAEFQTNSKKTDPPPLQVLPDLASSAEQSLAMPFHKSSKEAVVAGNLEKSVEKGTQGLRVYLHTRQDASLTLTTTGMREPQIFAEEKSWHPENQTPSPVNGLQQHRETGSVQREAGQQSVPQDQGCLCDAEDLELHEEVVSLEALRKGELQRHAHLPSAEKGLPASGLCSCPCSEALMEVDTAEQSLVAMCSSTGRQDAVIKSPSVAHLASDNPTMEVETLQSNPSCEPVEHSILTRELQLPEDNVDMSTMDNKDDNSSSLLSGHGQPSVESAEEFCSSVTVALKELHELLVISCKPASEESPEHVTCQSEIGAESQPSVSDLSGRRVQSVHLTPSDQYSQGSCHQATSESGKTEIVGTAPCAAVEDEASTSFEGLGDGLSPDREDVRRSTESARKSCSVAITSAKLSEQLPCTSGVEIAPELAASEGAHSQPSEHVHNPGPDRPETSSVCPGAGLPRSGLDQPPTQSLSTPSVLPPFIFPAADVDRILGAGFTLQEALGALHRVGGNADLALLVLLAKNIVVPT
Protein: Serine/threonine-protein phosphatase 1 regulatory subunit GAC1 (P28006)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulates the activity of glycogen synthase. It is most probably a regulatory subunit for protein phosphatase type 1.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-2
- Glycogen [starch] synthase isoform 2
- Protein phosphatase 1 regulatory subunit SDS22
- Protein REG2
- GLC7-interacting protein 2
- GLC7-interacting protein 1
- Resistance to glucose repression protein 1
- GSY2-interacting protein PIG2
- Glycogenin-1
- Serine/threonine-protein phosphatase 1 regulatory subunit PIG1
Sequence:
MVIQTATTLSPAKARPSFPHNDLIKSMSDSLISRPTHPPIRKLKSSLKISHPEPISRSKSEIFCTSPEKNVRFAIELTTVKRFDKNAEPSSISNENSPTLSPVDSNTAADDVQLFNNEDCWFNDSSLVTNLLKNEKKFRYMNSLNNMFKLDLYDSEDEDDIDEHINSQAEYGYTYNSLSTRGKTSENKSATSSLATQATNICDWKLHCTDLVPFKIAPPLFTKTLSASDLQGQLTKYLNGQNVKLHSLTQLGDDSSKITGLVYVKNLSFEKYLEIKFTFNSWRDIHYVTANFNRTINSNVDEFKFTIDLNSLKYILLIKRIITMEKNTSSCPLNIELCCRYDVNNETYYDNNNGKNYHLFMTTFKKGGETKEKIPVVVEPASQTDAAMSPKEMKARFVSSNPTLSRFLPQSRKFSEDTDYYNTSPLKHLYHNDTTSWVKPKRLNVVLDKLENATPPPPSSALANDTARTGKITKDKNNVLAPPTASNSIDLPILGSQHQSLYSGSSSYSSSSSSISSSLSFASSNNSSTNSSSASCSFPLTELDNFDYANLYEPNDTFTTANLFNHSLNSLMPEISTPSFFGGFRNENTINNNDSKNLVTSLEDSYEDKQSVITDTTMDENNKTSTINNSTDTLIKPSKENGTVKENKSSANSTSAPSSSQNRASTILNDHSNGKSDLKYVNYQSLLDSHCFYNHPSSPNLQSTSFSSAAPFSGISQASDIFDYENEDSDSNQIAGEIDNNSFPPHFYLDEDDKSACLSDDALIDHHRNTNPFINTFSSSPPILSQEVDRWRL
Protein: 2,4-diaminopentanoate dehydrogenase (DAPDH) (EC 1.4.1.12) (E3PY99)
Organism: Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF) (Clostridium sticklandii)
Function: Involved in the ornithine fermentation pathway. Catalyzes the oxidative deamination of (2R,4S)-2,4-diaminopentanoate (DAP) to yield 2-amino-4-ketopentanoate (AKP).
Interaction partners:
- D-ornithine 4,5-aminomutase subunit beta
- D-ornithine 4,5-aminomutase subunit alpha
- 2-amino-4-ketopentanoate thiolase alpha subunit
- 2-amino-4-ketopentanoate thiolase beta subunit
- Lysine 5,6-aminomutase beta subunit
- Putative component of D-ornithine aminomutase
- Lysine 5,6-aminomutase alpha subunit
- Ornithine racemase
- Proline racemase
- D-proline reductase subunit gamma
Sequence:
MEKVKVIIMGLGAMGGGMADMLLKKQGVEIVGVVGRGKMLGTSMYDHISTPRGDREDVIVGAMEDVITEKAADVVLLCTDSFTRKAFDKIKFIVEKKINVISSAEEMAYPMAQEPELAKEIDRLAKENGVSVLGTGINPGLIMDLLVILMTGCCEEVHSILSRRVNSLSPFGPAVMEEQGIGITVEEFNKGVQEGTLAGHVGFHESIGMIADAIGWKLSAPITQSMEPIVTDVDRKSPYGFAKAGNVAGCAMKGFGYVDGELKIEMDHPQQIEPEQVGVQTGDYVIINGVPNINMVNSPEVPGGIGTIAMCVNMIPQIINARPGLHTMIDLPVPRAIMGDFRDLISEEAKIVK
Protein: Mitochondrial import inner membrane translocase subunit Tim13 (P62075)
Organism: Mus musculus (Mouse)
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit Tim8 A
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit Tim8 B
- Putative mitochondrial import inner membrane translocase subunit Tim8 A-B
- Mitochondrial import inner membrane translocase subunit Tim10 B
- Mitochondrial import inner membrane translocase subunit Tim23
- Mitochondrial import inner membrane translocase subunit TIM50
- Small nuclear ribonucleoprotein Sm D2
- Mitochondrial import receptor subunit TOM22 homolog
Sequence:
MDSGFGSDFGGTGGGKLDPGAIMEQVKVQIAVANAQELLQRMTDKCFRKCIGKPGGSLDNSEQKCIAMCMDRYMDAWNTVSRAYNSRLQRERANM
Protein: Evasin P1134 (A0A0K8RAI0)
Organism: Ixodes ricinus (Common tick) (Acarus ricinus)
Function: Salivary chemokine-binding protein which binds to host chemokine CXCL1.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MEVKTFAFLQIAVFIALGIQIFAAVTAAADANEEVFTVEYCGMNCTQKSDGTWTECSGKNKDCRCYHESDAREGLCLSTEYTDFSQFETPSNSDLEAATPRPRKTLYPVRNPHGPKTRGLGYDKRILRDRVKFLI
Protein: Minor fimbrium subunit Mfa5 (B2RHG5)
Organism: Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Function: Accessory subunit of the minor fimbriae. These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in invasion of periodontal tissues and are recognized as major virulence factors. Fimbrium subunits from different strains have highly divergent sequences, and this correlates with pathogenicity (Probable).
Subcellular location: Fimbrium {ECO:0000269|PubMed:19589838, ECO:0000269|PubMed:24118823, ECO:0000269|PubMed:26001707, ECO:0000269|PubMed:26437277}.
Interaction partners:
Sequence:
MMKRYTIILAVFLLFCTVFTFQIKARPYERFADVEKPWIQKHSMDSKLVPANKGNLIQAEIVYQSVSEHSDLVISPVNEIRPANRFPSHRKSFFAENLRASPPVVPVAVDKYAVPVANPMDPENPNAWDVTLKITTKAVTVPVDVVMVIDQSSSMGGQNIARLKSAIASGQRFVKKMLPKGMATEGVRIALVSYDHEPHRLSDFTKDTAFLCQKIRALTPIWGTHTQGGLKMARNIMATSTAVDKHIILMSDGLATEQYPVKNVTTADFIGETGNANDPIDLVIQGAINFPTNYVSNNPSTPLTPNYPTHSSKVGRRNLPESKFDYSNLSARITFDGVAGALVYEPRFPHPYYYYFPCNAAINEAQFAKNSGYTIHTIGYDLGDFALANNSLKLTATDENHFFTATPANLAAAFDNIAQTINIGIQRGEVTDFVAPGFIVKNLTQSGDVTHLLNVSNGTVHYDVSTKKLTWTTGTILSSSEATITYRIYADLDYIQNNDIPVNTTSAIGPDLGGFDTNTEAKLTYTNSNGESNQQLIFPRPTVKLGYGVIKRHYVLVNKDGQPIQANGTVVSSLSEAHVLQSQDFFLPSGGGHIVPKWIKLDKTTEALQYYSVPPTNTVITTADGKRYRFVEVPGSTPNPGQIGISWKKPAGNAYFAYKLLNYWMGGTTDQQSEWDVTSNWTGAQVPLTGEDVEFATTENFGSPAVADLHVPTTNPKIIGNLINNSDKDLVVTTNSQLTINGVVEDNNPNVGTIVVKSSKDNPTGTLLFANPGYNQNVGGTVEFYNQGYDCADCGMYRRSWQYFGIPVNESGFPINDVGGNETVNQWVEPFNGDKWRPAPYAPDTKLQKFKGYQITNDVQAQPTGVYSFKGTLCVCDAFLNLTRTSGVNYSGANLIGNSYTGAIDIKQGIVFPPEVEQTVYLFNTGTRDQWRKLNGSTVSGFRAGQYLSVPKNTAGQDNLPDRIPSMHSFLVKMQNGASCTLQILYDKLLKNTTVNNGNGTQITWRSGNSGSANMPSLVMDVLGNESADRLWIFTDGGLSFGFDNGWDGRKLTEKGLSQLYAMSDIGNDKFQVAGVPELNNLLIGFDADKDGQYTLEFALSDHFAKGGVFLEDLSRGVTRRIVDGGSYSFDAKRGDSGARFRLSYDEEWVESAEVSVLVGTVGKRILITNNCEHACQANVYTTDGKLLIRLDVKPGSKSMTEPLIDGAYVVSLQSPATSSNVRKVVVN
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q380W0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MIQPNNIEQVLVLTLSMLTMQKAMAENEAENAIASLCHEAKYLHKVAEDFKSLLSTTDSDVSQAEKLTQIWQLKAAEATQLKEQNAYAALVLHGRLKIDKTKQARVNYKQTLSGVREGILQRISYLQGRTQAYTSFKVSKSTRDATTTKCKAKTTWAKHGDAQCDPTTLSNSPLERKTISAMAATKVKAATEAEIDIEMGNYDLELELSTALNSDSNNKCQTTTTQGTLEAITMVAKATAPHYGGKLLPTRKTDRPKQNCDAEEEKPPSKLPTADKLAALLCKAREAVPPPKIALESTTTETLFGDSDFLYIAAQLLTTEIPAGTQPEGTEADQIKQLIKSTYGDATTFGSRYTTGLYDKQTKYKKETQDSKGTLDSIATGTDLALVSSYFKGIALRLTAVQAGQEKQKNKTGQTDETCEKKGTGAECKDGCKLTGVVDNKKCVVDPDFVKKEVEGVKAENDGKTNTNTTGSNSVIIKKAPLVLAFFLR
Protein: Polygalacturonase inhibitor 2 (Polygalacturonase-inhibiting protein 2) (PGIP-2) (Q9M5J8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inhibitor of fungal polygalacturonase. It is an important factor for plant resistance to phytopathogenic fungi.
Subcellular location: Secreted, cell wall {ECO:0000250|UniProtKB:P58822}. Membrane; Peripheral membrane protein.
Interaction partners:
- EP1-like glycoprotein 3 lectin family protein)
Sequence:
MDKTMTLFLLLSTLLLTTSLAKDLCHKDDKTTLLKIKKSLNNPYHLASWDPKTDCCSWYCLECGDATVNHRVTSLIIQDGEISGQIPPEVGDLPYLTSLIFRKLTNLTGHIQPTIAKLKNLTFLRLSWTNLTGPVPEFLSQLKNLEYIDLSFNDLSGSIPSSLSSLRKLEYLELSRNKLTGPIPESFGTFSGKVPSLFLSHNQLSGTIPKSLGNPDFYRIDLSRNKLQGDASILFGAKKTTWIVDISRNMFQFDLSKVKLAKTLNNLDMNHNGITGSIPAEWSKAYFQLLNVSYNRLCGRIPKGEYIQRFDSYSFFHNKCLCGAPLPSCK
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-3 (EC 3.1.4.11) (Phosphoinositide phospholipase C-delta-3) (Phospholipase C-delta-3) (PLC-delta-3) (Q8K2J0)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow. Regulates neurite outgrowth through the inhibition of RhoA/Rho kinase signaling.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q8N3E9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8N3E9}. Cytoplasm {ECO:0000250|UniProtKB:Q8N3E9}. Cleavage furrow {ECO:0000250|UniProtKB:Q8N3E9}. Note=Localizes at the cleavage furrow during cytokinesis. {ECO:0000250|UniProtKB:Q8N3E9}.
Interaction partners:
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Protein kinase C alpha type
- Inositol polyphosphate-5-phosphatase A.
- Protein kinase C gamma type
- Protein kinase C beta type
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- Inositol polyphosphate multikinase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase delta-4
Sequence:
MLCGGWKRSRRSPEESRVSAQVAAPLAFPPSPASSDSSTKRPGLRALKKMGLTEDEDVQAMLRGSRLLKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAASKHIFFVQHIEAVREGHQSEGLRRFGGAFAPACCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLAKLRARLDAMSQRERLDHWIHSYLHRADSDQDSKMSFKEIKSLLRMVNVDMNDMYAYRLFKECDHSNNERLEGAEIEAFLRRLLKRPELEEIFRRYSGEDRVLSASELLEFLEDQGEDGATLACAQQLIQTYELNETAKQHELMTLDGFMMYLLSPEGAALNVAHTCVFQDMGQPLAHYFISSSHNTYLTDSQIGGTSSTEAYIRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVIQAVRDHAFTSSPYPVILSLENHCGLEQQAVMARHLRSILGDMLVTQALDSQNPEELPSPEQLKGRILVKGKKLPAARSEDGRILSDREEEEEEEEEAEEALEAAEQRSRAKQISPELSALAVYCCATRLRTLDPSPGPPQSCTVGSLSERKARKFTREAGTSFVRHNTQQLTRVYPLGLRMNSANYNPQEMWNSGCQLVALNFQTPGYEMDLNTGRFLINGQCGYVLKPAYLRQLNTTFDPECPGPPRTTLAIQVLTAQQLPKLNAEKPSSIVDPLVRVEIHGVPEDCAQKETDYVLNNGFNPCWEQTLQFRLRAPELVLVRFVVEDYDTTSPNDFVGQSTLPLSSLKQGYRHIHLLSKDGASLAPATLFVHIRIQNS
Protein: Protein hinderin (Q86T90)
Organism: Homo sapiens (Human)
Function: Competes with SMC1 for binding to SMC3. May affect the availability of SMC3 to engage in the formation of multimeric protein complexes.
Interaction partners:
- ADAMTS-like protein 3
- Mirror-image polydactyly gene 1 protein
- Astrotactin-2
- Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2
- Tyrosine-protein kinase FRK
- Biogenesis of lysosome-related organelles complex 1 subunit 6
- WD repeat-containing and planar cell polarity effector protein fritz homolog
- Importin subunit alpha-6
- Tubulin polyglutamylase complex subunit 2
- Coiled-coil domain-containing protein 14
Sequence:
MADVAGPSRPSAAAFWSRDFSDEEQSVVYVPGISAEGNVRSRHKLMSPKADVKLKTSRVTDASISMESLKGTGDSVDEQNSCRGEIKSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSIARPQTYYQTKQRPKSAVQDSASESLIAFRNNSLKPVTLHHPKDDLDKIPSETTTCNCESPGRKPAVPTEKMPQEELHMKECPHLKPTPSQCCGHRLAADRVHDSHPTNMTPQHPKTHPESCSYCRLSWASLVHGGGALQPIETLKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLHQSRLDYNCLLKSNCDGWLLGTSSSIKKHQDPPNSGENRKERKTVGFHSHMKDDAQWSCQKKDTCRPQRGTVTGVRKDASTSPMPTGSLKDFVTTASPSLQHTTSRYETSLLDLVQSLSPNSAPKPQRYPSREAGAWNHGTFRLSPLKSTRKKMGMHRTPEELEENQILEDIFFI
Protein: Chaperone protein ClpB4, mitochondrial (ATP-dependent Clp protease ATP-binding subunit ClpB homolog 4) (Casein lytic proteinase B4) (Q8VYJ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Molecular chaperone that does not seem to be involved in heat stress response or tolerance.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17144892}.
Interaction partners:
- Heat shock 70 kDa protein 8
- 17.8 kDa class I heat shock protein
- CLP protease regulatory subunit CLPX1
- Heat shock 70 kDa protein 5
- Heat shock 70 kDa protein 4
- Heat stress transcription factor A-4c
- Heat shock 70 kDa protein 10, mitochondrial
- At1g56300
- Heat shock protein 90-3
- Chaperone protein dnaJ GFA2, mitochondrial
Sequence:
MALRRLSKSVSSAIKAQYTLSRPSPLLRSRSLSSSPHYTSIGRPTNSFIGKINNSSITHATTTHGQLFPLSSPRRFCTTTAQVNQNEFTEMAWEGLINAFDAARESKQQIVESEHLMKALLEQKDGMARKIFTKAGIDNSSVLQATDLFISKQPTVSDASGQRLGSSLSVILENAKRHKKDMLDSYVSVEHFLLAYYSDTRFGQEFFRDMKLDIQVLKDAIKDVRGDQRVTDRNPESKYQALEKYGNDLTEMARRGKLDPVIGRDDEIRRCIQILCRRTKNNPVIIGEPGVGKTAIAEGLAQRIVRGDVPEPLMNRKLISLDMGSLLAGAKFRGDFEERLKAVMKEVSASNGQTILFIDEIHTVVGAGAMDGAMDASNLLKPMLGRGELRCIGATTLTEYRKYIEKDPALERRFQQVLCVQPSVEDTISILRGLRERYELHHGVTISDSALVSAAVLADRYITERFLPDKAIDLVDEAGAKLKMEITSKPTELDGIDRAVIKLEMEKLSLKNDTDKASKERLQKIENDLSTLKQKQKELNVQWEKEKSLMTKIRSFKEEIDRVNLEIESAEREYDLNRAAELKYGTLLSLQRQLEEAEKNLTNFRQFGQSLLREVVTDLDIAEIVSKWTGIPLSNLQQSEREKLVMLEEVLHHRVIGQDMAVKSVADAIRRSRAGLSDPNRPIASFMFMGPTGVGKTELAKALAGYLFNTENAIVRVDMSEYMEKHSVSRLVGAPPGYVGYEEGGQLTEVVRRRPYSVVLFDEIEKAHPDVFNILLQLLDDGRITDSQGRTVSFKNCVVIMTSNIGSHHILETLRNNEDSKEAVYEIMKRQVVELARQNFRPEFMNRIDEYIVFQPLDSNEISKIVELQMRRVKNSLEQKKIKLQYTKEAVDLLAQLGFDPNYGARPVKRVIQQMVENEIAVGILKGDFAEEDTVLVDVDHLASDNKLVIKKLESNASAEEMAA