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Q9Y5X3

- SNX5_HUMAN

UniProt

Q9Y5X3 - SNX5_HUMAN

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Protein
Sorting nexin-5
Gene
SNX5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in several stages of intracellular trafficking. Plays a role in macropinocytosis. Plays a role in the internalization of EGFR after EGF stimulation.2 Publications

GO - Molecular functioni

  1. phosphatidylinositol binding Source: UniProtKB

GO - Biological processi

  1. intracellular protein transport Source: RefGenome
  2. pinocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Sorting nexin-5
Gene namesi
Name:SNX5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:14969. SNX5.

Subcellular locationi

Early endosome membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cell projectionphagocytic cup. Cell projectionruffle
Note: Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2). Detected on macropinosomes. Targeted to membrane ruffles in response to EGFR stimulation.5 Publications

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  2. early endosome membrane Source: UniProtKB-SubCell
  3. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  4. extrinsic component of endosome membrane Source: UniProtKB
  5. macropinocytic cup Source: UniProtKB
  6. phagocytic cup Source: UniProtKB-SubCell
  7. ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37945.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 404403Sorting nexin-5
PRO_0000213844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei275 – 2751N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y5X3.
PaxDbiQ9Y5X3.
PRIDEiQ9Y5X3.

PTM databases

PhosphoSiteiQ9Y5X3.

Expressioni

Gene expression databases

ArrayExpressiQ9Y5X3.
BgeeiQ9Y5X3.
CleanExiHS_SNX5.
GenevestigatoriQ9Y5X3.

Organism-specific databases

HPAiCAB020679.

Interactioni

Subunit structurei

Interacts with SNX1; this promotes location at the endosome membrane.1 Publication

Protein-protein interaction databases

BioGridi118022. 23 interactions.
IntActiQ9Y5X3. 17 interactions.
MINTiMINT-2823978.
STRINGi9606.ENSP00000366988.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SYSX-ray2.40C257-265[»]
ProteinModelPortaliQ9Y5X3.
SMRiQ9Y5X3. Positions 20-174.

Miscellaneous databases

EvolutionaryTraceiQ9Y5X3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 172148PX
Add
BLAST
Domaini202 – 404203BAR
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 467Phosphatidylinositol bisphosphate binding By similarity
Regioni99 – 1057Phosphatidylinositol bisphosphate binding By similarity
Regioni113 – 1164Phosphatidylinositol bisphosphate binding By similarity

Domaini

The PX domain mediates interaction with membranes enriched in phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 4,5-bisphosphate By similarity.

Sequence similaritiesi

Belongs to the sorting nexin family.
Contains 1 BAR domain.

Phylogenomic databases

eggNOGiNOG255198.
HOVERGENiHBG000716.
InParanoidiQ9Y5X3.
KOiK17920.
OMAiIKDSCAK.
OrthoDBiEOG7X0VH4.
PhylomeDBiQ9Y5X3.
TreeFamiTF313698.

Family and domain databases

Gene3Di3.30.1520.10. 1 hit.
InterProiIPR001683. Phox.
IPR028654. SNX5.
IPR014637. SNX5/SNX6/SNX32.
IPR015404. Vps5_C.
[Graphical view]
PANTHERiPTHR10555:SF6. PTHR10555:SF6. 1 hit.
PfamiPF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view]
PIRSFiPIRSF036924. Snx5_Snx6. 1 hit.
SMARTiSM00312. PX. 1 hit.
[Graphical view]
SUPFAMiSSF64268. SSF64268. 1 hit.
PROSITEiPS50195. PX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y5X3-1 [UniParc]FASTAAdd to Basket

« Hide

MAAVPELLQQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH    50
TKTTLPTFQS PEFSVTRQHE DFVWLHDTLI ETTDYAGLII PPAPTKPDFD 100
GPREKMQKLG EGEGSMTKEE FAKMKQELEA EYLAVFKKTV SSHEVFLQRL 150
SSHPVLSKDR NFHVFLEYDQ DLSVRRKNTK EMFGGFFKSV VKSADEVLFT 200
GVKEVDDFFE QEKNFLINYY NRIKDSCVKA DKMTRSHKNV ADDYIHTAAC 250
LHSLALEEPT VIKKYLLKVA ELFEKLRKVE GRVSSDEDLK LTELLRYYML 300
NIEAAKDLLY RRTKALIDYE NSNKALDKAR LKSKDVKLAE AHQQECCQKF 350
EQLSESAKEE LINFKRKRVA AFRKNLIEMS ELEIKHARNN VSLLQSCIDL 400
FKNN 404
Length:404
Mass (Da):46,816
Last modified:November 1, 1999 - v1
Checksum:i87A85620AF827EC6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti279 – 2791V → L1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF121855 mRNA. Translation: AAD27828.1.
AK001793 mRNA. Translation: BAA91914.1.
AL121585 Genomic DNA. Translation: CAC00471.1.
BC000100 mRNA. No translation available.
CH471133 Genomic DNA. Translation: EAX10264.1.
CH471133 Genomic DNA. Translation: EAX10265.1.
CH471133 Genomic DNA. Translation: EAX10266.1.
CH471133 Genomic DNA. Translation: EAX10268.1.
BC093623 mRNA. Translation: AAH93623.1.
BC093980 mRNA. Translation: AAH93980.1.
BC143274 mRNA. Translation: AAI43275.1.
CCDSiCCDS13130.1.
RefSeqiNP_055241.1. NM_014426.3.
NP_689413.1. NM_152227.2.
UniGeneiHs.316890.

Genome annotation databases

EnsembliENST00000377759; ENSP00000366988; ENSG00000089006.
ENST00000377768; ENSP00000366998; ENSG00000089006.
GeneIDi27131.
KEGGihsa:27131.
UCSCiuc002wqc.3. human.

Polymorphism databases

DMDMi10720289.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF121855 mRNA. Translation: AAD27828.1 .
AK001793 mRNA. Translation: BAA91914.1 .
AL121585 Genomic DNA. Translation: CAC00471.1 .
BC000100 mRNA. No translation available.
CH471133 Genomic DNA. Translation: EAX10264.1 .
CH471133 Genomic DNA. Translation: EAX10265.1 .
CH471133 Genomic DNA. Translation: EAX10266.1 .
CH471133 Genomic DNA. Translation: EAX10268.1 .
BC093623 mRNA. Translation: AAH93623.1 .
BC093980 mRNA. Translation: AAH93980.1 .
BC143274 mRNA. Translation: AAI43275.1 .
CCDSi CCDS13130.1.
RefSeqi NP_055241.1. NM_014426.3.
NP_689413.1. NM_152227.2.
UniGenei Hs.316890.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SYS X-ray 2.40 C 257-265 [» ]
ProteinModelPortali Q9Y5X3.
SMRi Q9Y5X3. Positions 20-174.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118022. 23 interactions.
IntActi Q9Y5X3. 17 interactions.
MINTi MINT-2823978.
STRINGi 9606.ENSP00000366988.

PTM databases

PhosphoSitei Q9Y5X3.

Polymorphism databases

DMDMi 10720289.

Proteomic databases

MaxQBi Q9Y5X3.
PaxDbi Q9Y5X3.
PRIDEi Q9Y5X3.

Protocols and materials databases

DNASUi 27131.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000377759 ; ENSP00000366988 ; ENSG00000089006 .
ENST00000377768 ; ENSP00000366998 ; ENSG00000089006 .
GeneIDi 27131.
KEGGi hsa:27131.
UCSCi uc002wqc.3. human.

Organism-specific databases

CTDi 27131.
GeneCardsi GC20M017870.
HGNCi HGNC:14969. SNX5.
HPAi CAB020679.
MIMi 605937. gene.
neXtProti NX_Q9Y5X3.
PharmGKBi PA37945.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG255198.
HOVERGENi HBG000716.
InParanoidi Q9Y5X3.
KOi K17920.
OMAi IKDSCAK.
OrthoDBi EOG7X0VH4.
PhylomeDBi Q9Y5X3.
TreeFami TF313698.

Enzyme and pathway databases

Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.

Miscellaneous databases

ChiTaRSi SNX5. human.
EvolutionaryTracei Q9Y5X3.
GeneWikii SNX5.
GenomeRNAii 27131.
NextBioi 49854.
PROi Q9Y5X3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y5X3.
Bgeei Q9Y5X3.
CleanExi HS_SNX5.
Genevestigatori Q9Y5X3.

Family and domain databases

Gene3Di 3.30.1520.10. 1 hit.
InterProi IPR001683. Phox.
IPR028654. SNX5.
IPR014637. SNX5/SNX6/SNX32.
IPR015404. Vps5_C.
[Graphical view ]
PANTHERi PTHR10555:SF6. PTHR10555:SF6. 1 hit.
Pfami PF00787. PX. 1 hit.
PF09325. Vps5. 1 hit.
[Graphical view ]
PIRSFi PIRSF036924. Snx5_Snx6. 1 hit.
SMARTi SM00312. PX. 1 hit.
[Graphical view ]
SUPFAMi SSF64268. SSF64268. 1 hit.
PROSITEi PS50195. PX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A large family of endosome-localized proteins related to sorting nexin 1."
    Teasdale R.D., Loci D., Houghton F., Karlsson L., Gleeson P.A.
    Biochem. J. 358:7-16(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovarian carcinoma.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Placenta.
  6. "Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation."
    Merino-Trigo A., Kerr M.C., Houghton F., Lindberg A., Mitchell C., Teasdale R.D., Gleeson P.A.
    J. Cell Sci. 117:6413-6424(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHATIDYLINOSITOL 3,4-BISPHOSPHATE BINDING.
  7. "Visualisation of macropinosome maturation by the recruitment of sorting nexins."
    Kerr M.C., Lindsay M.R., Luetterforst R., Hamilton N., Simpson F., Parton R.G., Gleeson P.A., Teasdale R.D.
    J. Cell Sci. 119:3967-3980(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SNX1, SUBCELLULAR LOCATION.
  8. "A role for SNX5 in the regulation of macropinocytosis."
    Lim J.P., Wang J.T., Kerr M.C., Teasdale R.D., Gleeson P.A.
    BMC Cell Biol. 9:58-58(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-275, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The SNX-PX-BAR family in macropinocytosis: the regulation of macropinosome formation by SNX-PX-BAR proteins."
    Wang J.T., Kerr M.C., Karunaratne S., Jeanes A., Yap A.S., Teasdale R.D.
    PLoS ONE 5:E13763-E13763(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 257-265 IN COMPLEX WITH HLA CLASS I HISTOCOMPATIBILITY COMPLEX.

Entry informationi

Entry nameiSNX5_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5X3
Secondary accession number(s): B7ZKN3
, D3DW26, Q52LC4, Q9BWP0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

The selectivity for particular phosphatidylinositol lipids is under debate. According to one report (PubMed:19553671), the rat protein binds exclusively to phosphatidylinositol 4,5-bisphosphate, while the human protein has been reported (1 Publication) to bind to phosphatidylinositol 3,4-bisphosphate and also to phosphatidylinositol 3-phosphate.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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