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Q5T4F4 (ZFY27_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protrudin
Alternative name(s):
Zinc finger FYVE domain-containing protein 27
Gene names
Name:ZFYVE27
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length411 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as an upstream inhibitor of RAB11, regulating directional protein transport to the forming neurites. Involved in nerve growth factor-induced neurite formation. May have a more general role in cell projections formation. Ref.5 Ref.7

Subunit structure

Interacts with SPAST. Interacts with RAB11A (GDP-bound form); regulates RAB11A. Interacts with FKBP8; may negatively regulate ZFYVE27 phosphorylation. Interacts with VAPA (via MSP domain); may regulate ZFYVE27 retention in the endoplasmic reticulum and its function in cell projections formation. Interacts with VAPB (via MSP domain). Ref.5 Ref.6 Ref.7 Ref.9

Subcellular location

Recycling endosome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell projectiongrowth cone membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note: Localizes at both dendrites and axons By similarity. Ref.7 Ref.9

Post-translational modification

Phosphorylated. Phosphorylation is induced by NGF through the MAPK/ERK pathway and modulates interaction with RAB11A. Ref.5

Involvement in disease

Spastic paraplegia 33, autosomal dominant (SPG33) [MIM:610244]: A form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body.
Note: The disease is caused by mutations affecting the gene represented in this entry. According to Ref.10, the properties of the variant Val-191 and its frequency in some populations raise doubts on the implication of that gene in the disease. Ref.9 Ref.10

Sequence similarities

Contains 1 FYVE-type zinc finger.

Sequence caution

The sequence CAD38913.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Endoplasmic reticulum
Endosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Hereditary spastic paraplegia
Neurodegeneration
   DomainTransmembrane
Transmembrane helix
Zinc-finger
   LigandMetal-binding
Zinc
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection development

Inferred from direct assay Ref.5. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentaxon

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay Ref.7. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

growth cone membrane

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

recycling endosome membrane

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.5Ref.6Ref.7. Source: IntAct

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5T4F4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q5T4F4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     294-300: Missing.
Isoform 3 (identifier: Q5T4F4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     268-268: E → ESLSSQ
Isoform 4 (identifier: Q5T4F4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.
     268-268: E → ESLSSQ
     294-300: Missing.
     349-356: NCTGCSAT → VTGAGSS
     357-411: Missing.
Isoform 5 (identifier: Q5T4F4-5)

The sequence of this isoform differs from the canonical sequence as follows:
     66-152: RWQMPLCSLL...PEAVAEVKSF → S
     294-300: Missing.
Isoform 6 (identifier: Q5T4F4-6)

The sequence of this isoform differs from the canonical sequence as follows:
     67-184: Missing.
     294-300: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: Q5T4F4-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: Missing.
     268-268: E → ESLSSQ
     294-300: Missing.
Note: No experimental confirmation available.
Isoform 8 (identifier: Q5T4F4-8)

The sequence of this isoform differs from the canonical sequence as follows:
     58-89: Missing.
     294-300: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 411411Protrudin
PRO_0000245601

Regions

Topological domain1 – 6666Cytoplasmic Potential
Transmembrane67 – 8721Helical; Potential
Topological domain881Extracellular Potential
Transmembrane89 – 10921Helical; Potential
Topological domain110 – 18778Cytoplasmic Potential
Transmembrane188 – 20821Helical; Potential
Topological domain209 – 411203Extracellular Potential
Zinc finger344 – 41067FYVE-type
Region51 – 6414Necessary for interaction with RAB11A and function in neurite outgrowth
Region286 – 2927Necessary for interaction with VAPA and function in cell projections formation
Compositional bias246 – 2494Poly-Pro

Amino acid modifications

Glycosylation2091N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 9898Missing in isoform 7.
VSP_045265
Alternative sequence1 – 6868Missing in isoform 4.
VSP_019751
Alternative sequence58 – 8932Missing in isoform 8.
VSP_046051
Alternative sequence66 – 15287RWQMP…EVKSF → S in isoform 5.
VSP_019752
Alternative sequence67 – 184118Missing in isoform 6.
VSP_045266
Alternative sequence2681E → ESLSSQ in isoform 3, isoform 4 and isoform 7.
VSP_019753
Alternative sequence294 – 3007Missing in isoform 2, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8.
VSP_019754
Alternative sequence349 – 3568NCTGCSAT → VTGAGSS in isoform 4.
VSP_019755
Alternative sequence357 – 41155Missing in isoform 4.
VSP_019756
Natural variant821V → I.
Corresponds to variant rs17108378 [ dbSNP | Ensembl ].
VAR_027002
Natural variant1381G → V. Ref.1 Ref.3 Ref.4
Corresponds to variant rs10882993 [ dbSNP | Ensembl ].
VAR_027003
Natural variant1911G → V in SPG33; aberrant subcellular localization and altered interaction with SPAST. Ref.9 Ref.10
Corresponds to variant rs35077384 [ dbSNP | Ensembl ].
VAR_027269

Experimental info

Mutagenesis131L → A: Alters interaction with RAB11A; when associated with A-49. Ref.5
Mutagenesis491I → A: Alters interaction with RAB11A; when associated with A-13. Ref.5
Mutagenesis2891D → A: Loss of interaction with VAPA and loss of function in cell projections formation. Ref.7
Sequence conflict501Y → N in AAH30621. Ref.3
Sequence conflict2181E → G in BAC11260. Ref.1
Sequence conflict2221V → F in BAH13112. Ref.1
Sequence conflict3401K → R in BAH13112. Ref.1
Sequence conflict3871M → A in BAH13112. Ref.1

Secondary structure

................. 411
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 5B86C64A398033D2

FASTA41145,843
        10         20         30         40         50         60 
MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY LEPLKDAGDG 

        70         80         90        100        110        120 
VRYLLRWQMP LCSLLTCLGL NVLFLTLNEG AWYSVGALMI SVPALLGYLQ EVCRARLPDS 

       130        140        150        160        170        180 
ELMRRKYHSV RQEDLQRGRL SRPEAVAEVK SFLIQLEAFL SRLCCTCEAA YRVLHWENPV 

       190        200        210        220        230        240 
VSSQFYGALL GTVCMLYLLP LCWVLTLLNS TLFLGNVEFF RVVSEYRASL QQRMNPKQEE 

       250        260        270        280        290        300 
HAFESPPPPD VGGKDGLMDS TPALTPTEDL TPGSVEEAEE AEPDEEFKDA IEETHLVVLE 

       310        320        330        340        350        360 
DDEGAPCPAE DELALQDNGF LSKNEVLRSK VSRLTERLRK RYPTNNFGNC TGCSATFSVL 

       370        380        390        400        410 
KKRRSCSNCG NSFCSRCCSF KVPKSSMGAT APEAQRETVF VCASCNQTLS K 

« Hide

Isoform 2 [UniParc].

Checksum: 0FA0436DAE7716D7
Show »

FASTA40445,052
Isoform 3 [UniParc].

Checksum: BF488D2456C6B924
Show »

FASTA41646,346
Isoform 4 [UniParc].

Checksum: 977E99E1E5857BDD
Show »

FASTA28531,744
Isoform 5 [UniParc].

Checksum: 1E3E1DF487779DEB
Show »

FASTA31835,205
Isoform 6 [UniParc].

Checksum: C4F817D0A286151B
Show »

FASTA28631,612
Isoform 7 [UniParc].

Checksum: 3035EAF2EF4EEA53
Show »

FASTA31134,681
Isoform 8 [UniParc].

Checksum: 0D235A6E1A98B2E2
Show »

FASTA37241,417

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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] (ISOFORMS 2; 4; 5; 6; 7 AND 8), VARIANT VAL-138.
Tissue: Brain, Testis, Thalamus and Thymus.
[2]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORM 1), VARIANT VAL-138.
Tissue: Brain.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-411 (ISOFORM 3), VARIANT VAL-138.
Tissue: Brain.
[5]"Protrudin induces neurite formation by directional membrane trafficking."
Shirane M., Nakayama K.I.
Science 314:818-821(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FKBP8 AND RAB11A, PHOSPHORYLATION, MUTAGENESIS OF LEU-13 AND ILE-49.
[6]"Regulation of apoptosis and neurite extension by FKBP38 is required for neural tube formation in the mouse."
Shirane M., Ogawa M., Motoyama J., Nakayama K.I.
Genes Cells 13:635-651(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FKBP8.
[7]"Promotion of neurite extension by protrudin requires its interaction with vesicle-associated membrane protein-associated protein."
Saita S., Shirane M., Natume T., Iemura S., Nakayama K.I.
J. Biol. Chem. 284:13766-13777(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VAPA AND VAPB, MUTAGENESIS OF ASP-289, SUBCELLULAR LOCATION.
[8]"Solution structure of the FYVE domain from human FYVE domain containing 27 isoform B protein."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 341-411.
[9]"ZFYVE27 (SPG33), a novel spastin-binding protein, is mutated in hereditary spastic paraplegia."
Mannan A.U., Krawen P., Sauter S.M., Boehm J., Chronowska A., Paulus W., Neesen J., Engel W.
Am. J. Hum. Genet. 79:351-357(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPG33 VAL-191, CHARACTERIZATION OF VARIANT SPG33 VAL-191, SUBCELLULAR LOCATION, INTERACTION WITH SPAST.
[10]"The role of ZFYVE27/protrudin in hereditary spastic paraplegia."
Martignoni M., Riano E., Rugarli E.I.
Am. J. Hum. Genet. 83:127-130(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT SPG33 VAL-191.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK057481 mRNA. Translation: BAB71506.1.
AK097945 mRNA. Translation: BAC05200.1.
AK074876 mRNA. Translation: BAC11260.1.
AK296295 mRNA. Translation: BAH12306.1.
AK296588 mRNA. Translation: BAH12390.1.
AK299735 mRNA. Translation: BAH13112.1.
AL358938 Genomic DNA. Translation: CAI14270.1.
AL358938 Genomic DNA. Translation: CAI14271.1.
AL358938 Genomic DNA. Translation: CAI14272.1.
BC030621 mRNA. Translation: AAH30621.2.
AL834235 mRNA. Translation: CAD38913.2. Different initiation.
CCDSCCDS31262.1. [Q5T4F4-3]
CCDS31263.1. [Q5T4F4-1]
CCDS31264.1. [Q5T4F4-2]
CCDS53562.1. [Q5T4F4-8]
CCDS53563.1. [Q5T4F4-5]
CCDS53564.1. [Q5T4F4-6]
CCDS53565.1. [Q5T4F4-7]
RefSeqNP_001002261.1. NM_001002261.3. [Q5T4F4-3]
NP_001002262.1. NM_001002262.3. [Q5T4F4-2]
NP_001167590.1. NM_001174119.1. [Q5T4F4-8]
NP_001167591.1. NM_001174120.1. [Q5T4F4-5]
NP_001167592.1. NM_001174121.1. [Q5T4F4-7]
NP_001167593.1. NM_001174122.1. [Q5T4F4-6]
NP_653189.3. NM_144588.6. [Q5T4F4-1]
XP_005269559.1. XM_005269502.1. [Q5T4F4-3]
XP_005269560.1. XM_005269503.1. [Q5T4F4-3]
XP_005269561.1. XM_005269504.1. [Q5T4F4-1]
XP_005269563.1. XM_005269506.1. [Q5T4F4-2]
UniGeneHs.744075.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4UNMR-A341-411[»]
ProteinModelPortalQ5T4F4.
SMRQ5T4F4. Positions 341-411.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125623. 2 interactions.
IntActQ5T4F4. 7 interactions.

PTM databases

PhosphoSiteQ5T4F4.

Polymorphism databases

DMDM74744927.

Proteomic databases

MaxQBQ5T4F4.
PaxDbQ5T4F4.
PRIDEQ5T4F4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337540; ENSP00000337993; ENSG00000155256. [Q5T4F4-8]
ENST00000356257; ENSP00000348593; ENSG00000155256. [Q5T4F4-3]
ENST00000357540; ENSP00000350148; ENSG00000155256. [Q5T4F4-5]
ENST00000359980; ENSP00000353069; ENSG00000155256. [Q5T4F4-2]
ENST00000370610; ENSP00000359642; ENSG00000155256. [Q5T4F4-7]
ENST00000370613; ENSP00000359646; ENSG00000155256. [Q5T4F4-6]
ENST00000393677; ENSP00000377282; ENSG00000155256. [Q5T4F4-1]
GeneID118813.
KEGGhsa:118813.
UCSCuc001kol.2. human. [Q5T4F4-1]
uc001kom.2. human. [Q5T4F4-2]
uc001koq.3. human. [Q5T4F4-5]
uc021pwq.1. human. [Q5T4F4-3]

Organism-specific databases

CTD118813.
GeneCardsGC10P099486.
HGNCHGNC:26559. ZFYVE27.
HPAHPA037523.
MIM610243. gene.
610244. phenotype.
neXtProtNX_Q5T4F4.
PharmGKBPA134863310.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG28771.
HOVERGENHBG054907.
OMASYKRLEI.
OrthoDBEOG7VTDNG.
PhylomeDBQ5T4F4.
TreeFamTF331044.

Gene expression databases

ArrayExpressQ5T4F4.
BgeeQ5T4F4.
GenevestigatorQ5T4F4.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF01363. FYVE. 1 hit.
[Graphical view]
SMARTSM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZFYVE27. human.
EvolutionaryTraceQ5T4F4.
GenomeRNAi118813.
NextBio35535086.
PROQ5T4F4.
SOURCESearch...

Entry information

Entry nameZFY27_HUMAN
AccessionPrimary (citable) accession number: Q5T4F4
Secondary accession number(s): B7Z3S0 expand/collapse secondary AC list , B7Z404, B7Z626, G8JLC3, G8JLF0, J3KP98, Q5T4F1, Q5T4F2, Q5T4F3, Q8N1K0, Q8N6D6, Q8NCA0, Q8NDE4, Q96M08
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: December 21, 2004
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM