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Q5T4F4 - ZFY27_HUMAN

UniProt

Q5T4F4 - ZFY27_HUMAN

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Protein

Protrudin

Gene

ZFYVE27

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

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri344 – 41067FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. neuron projection development Source: UniProtKB
  2. neurotrophin TRK receptor signaling pathway Source: UniProtKB
  3. protein localization to plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protrudin
Alternative name(s):
Zinc finger FYVE domain-containing protein 27
Gene namesi
Name:ZFYVE27
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:26559. ZFYVE27.

Subcellular locationi

Recycling endosome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein. Cell projection › growth cone membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein
Note: Localizes at both dendrites and axons.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6666CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei67 – 8721HelicalSequence AnalysisAdd
BLAST
Topological domaini88 – 881ExtracellularSequence Analysis
Transmembranei89 – 10921HelicalSequence AnalysisAdd
BLAST
Topological domaini110 – 18778CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei188 – 20821HelicalSequence AnalysisAdd
BLAST
Topological domaini209 – 411203ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. dendrite Source: UniProtKB
  3. endoplasmic reticulum Source: UniProtKB
  4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  5. growth cone membrane Source: UniProtKB
  6. integral component of membrane Source: UniProtKB-KW
  7. recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Endoplasmic reticulum, Endosome, Membrane

Pathology & Biotechi

Involvement in diseasei

Spastic paraplegia 33, autosomal dominant1 Publication

The disease is caused by mutations affecting the gene represented in this entry. According to PubMed:18606302, the properties of the variant Val-191 and its frequency in some populations raise doubts on the implication of that gene in the disease.

Disease descriptionA 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.

See also OMIM:610244
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti191 – 1911G → V in SPG33; aberrant subcellular localization and altered interaction with SPAST. 2 Publications
Corresponds to variant rs35077384 [ dbSNP | Ensembl ].		VAR_027269

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi13 – 131L → A: Alters interaction with RAB11A; when associated with A-49. 1 Publication
Mutagenesisi49 – 491I → A: Alters interaction with RAB11A; when associated with A-13. 1 Publication
Mutagenesisi289 – 2891D → A: Loss of interaction with VAPA and loss of function in cell projections formation. 1 Publication

Keywords - Diseasei

Disease mutation, Hereditary spastic paraplegia, Neurodegeneration

Organism-specific databases

MIMi610244. phenotype.
PharmGKBiPA134863310.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411ProtrudinPRO_0000245601Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi209 – 2091N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Phosphorylated. Phosphorylation is induced by NGF through the MAPK/ERK pathway and modulates interaction with RAB11A.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ5T4F4.
PaxDbiQ5T4F4.
PRIDEiQ5T4F4.

PTM databases

PhosphoSiteiQ5T4F4.

Expressioni

Gene expression databases

BgeeiQ5T4F4.
ExpressionAtlasiQ5T4F4. baseline and differential.
GenevestigatoriQ5T4F4.

Organism-specific databases

HPAiHPA037523.

Interactioni

Subunit structurei

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).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FKBP8Q143184EBI-3892947,EBI-724839
RAB11AP624914EBI-3892947,EBI-745098
VAPAQ9P0L05EBI-3892947,EBI-1059156
VAPBO952922EBI-3892947,EBI-1188298

Protein-protein interaction databases

BioGridi125623. 1 interaction.
IntActiQ5T4F4. 7 interactions.

Structurei

Secondary structure

1
411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi351 – 3533Combined sources
Beta strandi359 – 3613Combined sources
Beta strandi367 – 3693Combined sources
Turni375 – 3773Combined sources
Beta strandi380 – 3823Combined sources
Turni385 – 3873Combined sources
Beta strandi399 – 4013Combined sources
Helixi403 – 4108Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4UNMR-A341-411[»]
ProteinModelPortaliQ5T4F4.
SMRiQ5T4F4. Positions 341-411.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5T4F4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni51 – 6414Necessary for interaction with RAB11A and function in neurite outgrowthAdd
BLAST
Regioni286 – 2927Necessary for interaction with VAPA and function in cell projections formation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi246 – 2494Poly-Pro

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri344 – 41067FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiNOG28771.
GeneTreeiENSGT00390000013298.
HOVERGENiHBG054907.
InParanoidiQ5T4F4.
OMAiSYKRLEI.
OrthoDBiEOG7VTDNG.
PhylomeDBiQ5T4F4.
TreeFamiTF331044.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5T4F4-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MQTSEREGSG PELSPSVMPE APLESPPFPT KSPAFDLFNL VLSYKRLEIY 
        60         70         80         90        100
LEPLKDAGDG VRYLLRWQMP LCSLLTCLGL NVLFLTLNEG AWYSVGALMI 
       110        120        130        140        150
SVPALLGYLQ EVCRARLPDS ELMRRKYHSV RQEDLQRGRL SRPEAVAEVK 
       160        170        180        190        200
SFLIQLEAFL SRLCCTCEAA YRVLHWENPV VSSQFYGALL GTVCMLYLLP 
       210        220        230        240        250
LCWVLTLLNS TLFLGNVEFF RVVSEYRASL QQRMNPKQEE HAFESPPPPD 
       260        270        280        290        300
VGGKDGLMDS TPALTPTEDL TPGSVEEAEE AEPDEEFKDA IEETHLVVLE 
       310        320        330        340        350
DDEGAPCPAE DELALQDNGF LSKNEVLRSK VSRLTERLRK RYPTNNFGNC 
       360        370        380        390        400
TGCSATFSVL KKRRSCSNCG NSFCSRCCSF KVPKSSMGAT APEAQRETVF 
       410 
VCASCNQTLS K
Length:411
Mass (Da):45,843
Last modified:December 21, 2004 - v1
Checksum:i5B86C64A398033D2
GO
Isoform 2 (identifier: Q5T4F4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     294-300: Missing.

Show »
Length:404
Mass (Da):45,052
Checksum:i0FA0436DAE7716D7
GO
Isoform 3 (identifier: Q5T4F4-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     268-268: E → ESLSSQ

Show »
Length:416
Mass (Da):46,346
Checksum:iBF488D2456C6B924
GO
Isoform 4 (identifier: Q5T4F4-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:285
Mass (Da):31,744
Checksum:i977E99E1E5857BDD
GO
Isoform 5 (identifier: Q5T4F4-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     66-152: RWQMPLCSLL...PEAVAEVKSF → S
     294-300: Missing.

Show »
Length:318
Mass (Da):35,205
Checksum:i1E3E1DF487779DEB
GO
Isoform 6 (identifier: Q5T4F4-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     67-184: Missing.
     294-300: Missing.

Note: No experimental confirmation available.

Show »
Length:286
Mass (Da):31,612
Checksum:iC4F817D0A286151B
GO
Isoform 7 (identifier: Q5T4F4-7) [UniParc]FASTAAdd to Basket

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.

Show »
Length:311
Mass (Da):34,681
Checksum:i3035EAF2EF4EEA53
GO
Isoform 8 (identifier: Q5T4F4-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-89: Missing.
     294-300: Missing.

Note: No experimental confirmation available.

Show »
Length:372
Mass (Da):41,417
Checksum:i0D235A6E1A98B2E2
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501Y → N in AAH30621. (PubMed:15489334)Curated
Sequence conflicti218 – 2181E → G in BAC11260. (PubMed:14702039)Curated
Sequence conflicti222 – 2221V → F in BAH13112. (PubMed:14702039)Curated
Sequence conflicti340 – 3401K → R in BAH13112. (PubMed:14702039)Curated
Sequence conflicti387 – 3871M → A in BAH13112. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821V → I.
Corresponds to variant rs17108378 [ dbSNP | Ensembl ].		VAR_027002
Natural varianti138 – 1381G → V.3 Publications
Corresponds to variant rs10882993 [ dbSNP | Ensembl ].		VAR_027003
Natural varianti191 – 1911G → V in SPG33; aberrant subcellular localization and altered interaction with SPAST. 2 Publications
Corresponds to variant rs35077384 [ dbSNP | Ensembl ].		VAR_027269

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9898Missing in isoform 7. 1 PublicationVSP_045265Add
BLAST
Alternative sequencei1 – 6868Missing in isoform 4. 1 PublicationVSP_019751Add
BLAST
Alternative sequencei58 – 8932Missing in isoform 8. 1 PublicationVSP_046051Add
BLAST
Alternative sequencei66 – 15287RWQMP…EVKSF → S in isoform 5. 1 PublicationVSP_019752Add
BLAST
Alternative sequencei67 – 184118Missing in isoform 6. 1 PublicationVSP_045266Add
BLAST
Alternative sequencei268 – 2681E → ESLSSQ in isoform 3, isoform 4 and isoform 7. 2 PublicationsVSP_019753
Alternative sequencei294 – 3007Missing in isoform 2, isoform 4, isoform 5, isoform 6, isoform 7 and isoform 8. 1 PublicationVSP_019754
Alternative sequencei349 – 3568NCTGCSAT → VTGAGSS in isoform 4. 1 PublicationVSP_019755
Alternative sequencei357 – 41155Missing in isoform 4. 1 PublicationVSP_019756Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31263.1. [Q5T4F4-1]
CCDS31264.1. [Q5T4F4-2]
CCDS53562.1. [Q5T4F4-8]
CCDS53563.1. [Q5T4F4-5]
CCDS53564.1. [Q5T4F4-6]
CCDS53565.1. [Q5T4F4-7]
RefSeqiNP_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]
UniGeneiHs.744075.

Genome annotation databases

EnsembliENST00000337540; ENSP00000337993; ENSG00000155256. [Q5T4F4-8]
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]
GeneIDi118813.
KEGGihsa:118813.
UCSCiuc001kol.2. human. [Q5T4F4-1]
uc001kom.2. human. [Q5T4F4-2]
uc001koq.3. human. [Q5T4F4-5]
uc021pwq.1. human. [Q5T4F4-3]

Polymorphism databases

DMDMi74744927.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31263.1. [Q5T4F4-1]
CCDS31264.1. [Q5T4F4-2]
CCDS53562.1. [Q5T4F4-8]
CCDS53563.1. [Q5T4F4-5]
CCDS53564.1. [Q5T4F4-6]
CCDS53565.1. [Q5T4F4-7]
RefSeqiNP_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]
UniGeneiHs.744075.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4UNMR-A341-411[»]
ProteinModelPortaliQ5T4F4.
SMRiQ5T4F4. Positions 341-411.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125623. 1 interaction.
IntActiQ5T4F4. 7 interactions.

PTM databases

PhosphoSiteiQ5T4F4.

Polymorphism databases

DMDMi74744927.

Proteomic databases

MaxQBiQ5T4F4.
PaxDbiQ5T4F4.
PRIDEiQ5T4F4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337540; ENSP00000337993; ENSG00000155256. [Q5T4F4-8]
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]
GeneIDi118813.
KEGGihsa:118813.
UCSCiuc001kol.2. human. [Q5T4F4-1]
uc001kom.2. human. [Q5T4F4-2]
uc001koq.3. human. [Q5T4F4-5]
uc021pwq.1. human. [Q5T4F4-3]

Organism-specific databases

CTDi118813.
GeneCardsiGC10P099486.
HGNCiHGNC:26559. ZFYVE27.
HPAiHPA037523.
MIMi610243. gene.
610244. phenotype.
neXtProtiNX_Q5T4F4.
PharmGKBiPA134863310.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG28771.
GeneTreeiENSGT00390000013298.
HOVERGENiHBG054907.
InParanoidiQ5T4F4.
OMAiSYKRLEI.
OrthoDBiEOG7VTDNG.
PhylomeDBiQ5T4F4.
TreeFamiTF331044.

Miscellaneous databases

ChiTaRSiZFYVE27. human.
EvolutionaryTraceiQ5T4F4.
GenomeRNAii118813.
NextBioi35535086.
PROiQ5T4F4.
SOURCEiSearch...

Gene expression databases

BgeeiQ5T4F4.
ExpressionAtlasiQ5T4F4. baseline and differential.
GenevestigatoriQ5T4F4.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiZFY27_HUMAN
AccessioniPrimary (citable) accession number: Q5T4F4
Secondary accession number(s): B7Z3S0
, B7Z404, B7Z626, G8JLC3, G8JLF0, J3KP98, Q5T4F1, Q5T4F2, Q5T4F3, Q8N1K0, Q8N6D6, Q8NCA0, Q8NDE4, Q96M08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: December 21, 2004
Last modified: February 4, 2015
This is version 110 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.