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Protein

Rabankyrin-5

Gene

ANKFY1

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

Functioni

Proposed effector of Rab5. Binds to phosphatidylinositol 3-phosphate (PI3P). Involved in homotypic early endosome fusion and to a lesser extend in heterotypic fusion of chlathrin-coated vesicles with early endosomes. Involved in macropinocytosis; the function is dependent on Rab5-GTP. Required for correct endosomal localization. Involved in the internalization and trafficking of activated tyrosine kinase receptors such as PDGFRB. Regulates the subcellular localization of the retromer complex in a EHD1-dependent manner. Involved in endosome-to-Golgi transport and biosynthetic transport to late endosomes and lysosomes indicative for a regulation of retromer complex-mediated retrograde transport.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1104 – 116461FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphatidylinositol phosphate binding Source: UniProtKB
  • Rab GTPase binding Source: UniProtKB

GO - Biological processi

  • endocytosis Source: UniProtKB-KW
  • endosomal vesicle fusion Source: UniProtKB
  • endosome localization Source: UniProtKB
  • Golgi to lysosome transport Source: UniProtKB
  • positive regulation of pinocytosis Source: UniProtKB
  • retrograde transport, endosome to Golgi Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Rabankyrin-51 Publication
Short name:
Rank-51 Publication
Alternative name(s):
Ankyrin repeat and FYVE domain-containing protein 1
Ankyrin repeats hooked to a zinc finger motif
Gene namesi
Name:ANKFY1
Synonyms:ANKHZN, KIAA1255
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:20763. ANKFY1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GOC
  • early endosome Source: UniProtKB
  • endosome membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • macropinosome Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi421 – 4233NPF → APA: Disrupts interaction with EHD1. 1 Publication
Mutagenesisi424 – 4252ED → AA: Decreases interaction with EHD1. 1 Publication

Organism-specific databases

PharmGKBiPA134984226.

Polymorphism and mutation databases

BioMutaiANKFY1.
DMDMi33514905.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 11691168Rabankyrin-5PRO_0000066890Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9P2R3.
MaxQBiQ9P2R3.
PaxDbiQ9P2R3.
PRIDEiQ9P2R3.

PTM databases

iPTMnetiQ9P2R3.
PhosphoSiteiQ9P2R3.

Expressioni

Tissue specificityi

High expression in whole adult brain and intermediate expression in all other tissues and specific brain regions examined, including fetal brain.2 Publications

Gene expression databases

BgeeiQ9P2R3.
CleanExiHS_ANKFY1.
ExpressionAtlasiQ9P2R3. baseline and differential.
GenevisibleiQ9P2R3. HS.

Organism-specific databases

HPAiHPA024513.
HPA024522.

Interactioni

Subunit structurei

Interacts with RAB5A (in GTP-bound form). Interacts with RHOD (independent of GTP-loaded status). Interacts with EHD1. Interacts with VPS26A; the interaction is indepenedent of EHD1 and is indicative for an association with the cargo recognition subcomplex of the retromer complex.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EHD1Q9H4M95EBI-2513908,EBI-490691
GABARAPL2P605202EBI-2513908,EBI-720116

GO - Molecular functioni

  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119564. 33 interactions.
DIPiDIP-46068N.
IntActiQ9P2R3. 18 interactions.
STRINGi9606.ENSP00000459775.

Structurei

3D structure databases

ProteinModelPortaliQ9P2R3.
SMRiQ9P2R3. Positions 53-193, 221-1074, 1100-1163.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini68 – 13063BTBPROSITE-ProRule annotationAdd
BLAST
Repeati217 – 24731ANK 1Add
BLAST
Repeati255 – 28430ANK 2Add
BLAST
Repeati288 – 31730ANK 3Add
BLAST
Repeati322 – 36241ANK 4Add
BLAST
Repeati366 – 39631ANK 5Add
BLAST
Repeati490 – 51930ANK 6Add
BLAST
Repeati542 – 57231ANK 7Add
BLAST
Repeati588 – 61730ANK 8Add
BLAST
Repeati621 – 65030ANK 9Add
BLAST
Repeati654 – 68330ANK 10Add
BLAST
Repeati687 – 71630ANK 11Add
BLAST
Repeati724 – 75330ANK 12Add
BLAST
Repeati769 – 79830ANK 13Add
BLAST
Repeati802 – 83231ANK 14Add
BLAST
Repeati836 – 86530ANK 15Add
BLAST
Repeati870 – 89930ANK 16Add
BLAST
Repeati905 – 93430ANK 17Add
BLAST
Repeati938 – 96730ANK 18Add
BLAST
Repeati971 – 100131ANK 19Add
BLAST
Repeati1005 – 103733ANK 20Add
BLAST
Repeati1043 – 107230ANK 21Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni650 – 759110Interaction with RHOD and RAB5A1 PublicationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi421 – 4233NPF

Sequence similaritiesi

Contains 21 ANK repeats.PROSITE-ProRule annotation
Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation
Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1104 – 116461FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4591. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129770.
HOGENOMiHOG000022583.
HOVERGENiHBG050501.
InParanoidiQ9P2R3.
OMAiWSLLHKA.
OrthoDBiEOG7327MZ.
PhylomeDBiQ9P2R3.
TreeFamiTF351263.

Family and domain databases

Gene3Di1.25.40.20. 3 hits.
3.30.40.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF12796. Ank_2. 3 hits.
PF00651. BTB. 1 hit.
PF01363. FYVE. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 21 hits.
SM00225. BTB. 1 hit.
SM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 4 hits.
SSF54695. SSF54695. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 12 hits.
PS50097. BTB. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9P2R3-1) [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
MAEEEVAKLE KHLMLLRQEY VKLQKKLAET EKRCALLAAQ ANKESSSESF
60 70 80 90 100
ISRLLAIVAD LYEQEQYSDL KIKVGDRHIS AHKFVLAARS DSWSLANLSS
110 120 130 140 150
TKELDLSDAN PEVTMTMLRW IYTDELEFRE DDVFLTELMK LANRFQLQLL
160 170 180 190 200
RERCEKGVMS LVNVRNCIRF YQTAEELNAS TLMNYCAEII ASHWDDLRKE
210 220 230 240 250
DFSSMSAQLL YKMIKSKTEY PLHKAIKVER EDVVFLYLIE MDSQLPGKLN
260 270 280 290 300
EADHNGDLAL DLALSRRLES IATTLVSHKA DVDMVDKSGW SLLHKGIQRG
310 320 330 340 350
DLFAATFLIK NGAFVNAATL GAQETPLHLV ALYSSKKHSA DVMSEMAQIA
360 370 380 390 400
EALLQAGANP NMQDSKGRTP LHVSIMAGNE YVFSQLLQCK QLDLELKDHE
410 420 430 440 450
GSTALWLAVQ HITVSSDQSV NPFEDVPVVN GTSFDENSFA ARLIQRGSHT
460 470 480 490 500
DAPDTATGNC LLQRAAGAGN EAAALFLATN GAHVNHRNKW GETPLHTACR
510 520 530 540 550
HGLANLTAEL LQQGANPNLQ TEEALPLPKE AASLTSLADS VHLQTPLHMA
560 570 580 590 600
IAYNHPDVVS VILEQKANAL HATNNLQIIP DFSLKDSRDQ TVLGLALWTG
610 620 630 640 650
MHTIAAQLLG SGAAINDTMS DGQTLLHMAI QRQDSKSALF LLEHQADINV
660 670 680 690 700
RTQDGETALQ LAIRNQLPLV VDAICTRGAD MSVPDEKGNP PLWLALANNL
710 720 730 740 750
EDIASTLVRH GCDATCWGPG PGGCLQTLLH RAIDENNEPT ACFLIRSGCD
760 770 780 790 800
VNSPRQPGAN GEGEEEARDG QTPLHLAASW GLEETVQCLL EFGANVNAQD
810 820 830 840 850
AEGRTPIHVA ISSQHGVIIQ LLVSHPDIHL NVRDRQGLTP FACAMTFKNN
860 870 880 890 900
KSAEAILKRE SGAAEQVDNK GRNFLHVAVQ NSDIESVLFL ISVHANVNSR
910 920 930 940 950
VQDASKLTPL HLAVQAGSEI IVRNLLLAGA KVNELTKHRQ TALHLAAQQD
960 970 980 990 1000
LPTICSVLLE NGVDFAAVDE NGNNALHLAV MHGRLNNIRV LLTECTVDAE
1010 1020 1030 1040 1050
AFNLRGQSPL HILGQYGKEN AAAIFDLFLE CMPGYPLDKP DADGSTVLLL
1060 1070 1080 1090 1100
AYMKGNANLC RAIVRSGARL GVNNNQGVNI FNYQVATKQL LFRLLDMLSK
1110 1120 1130 1140 1150
EPPWCDGSYC YECTARFGVT TRKHHCRHCG RLLCHKCSTK EIPIIKFDLN
1160
KPVRVCNICF DVLTLGGVS
Length:1,169
Mass (Da):128,399
Last modified:August 4, 2003 - v2
Checksum:i589297CA4ACDDB56
GO
Isoform 2 (identifier: Q9P2R3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     650-650: V → VS

Show »
Length:1,170
Mass (Da):128,486
Checksum:i7972BC32D1D37137
GO
Isoform 4 (identifier: Q9P2R3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MAEE → MPTPRDCGRLRSRAGRSRAGAACSRGAPRAAREALDCRRCRDAGGK

Note: No experimental confirmation available.
Show »
Length:1,211
Mass (Da):132,821
Checksum:i810E7D2D0F90352E
GO

Sequence cautioni

The sequence AAH52308.1 differs from that shown.Intron retention.Curated
The sequence BAA86569.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481E → K in BAA90300 (PubMed:10940552).Curated
Sequence conflicti115 – 1151M → V in BAA90300 (PubMed:10940552).Curated
Sequence conflicti207 – 2071A → P in BAA90300 (PubMed:10940552).Curated
Sequence conflicti235 – 2351F → S in BAA90300 (PubMed:10940552).Curated
Sequence conflicti270 – 2701S → N in BAA90300 (PubMed:10940552).Curated
Sequence conflicti283 – 2919DMVDKSGWS → AWWPRVLE in BAA90300 (PubMed:10940552).Curated
Sequence conflicti299 – 3002RG → E in BAA90300 (PubMed:10940552).Curated
Sequence conflicti322 – 3221A → C in BAA90300 (PubMed:10940552).Curated
Sequence conflicti336 – 3372KK → RN in BAA90300 (PubMed:10940552).Curated
Sequence conflicti379 – 3791N → D in BAA90300 (PubMed:10940552).Curated
Sequence conflicti385 – 3851Q → H in BAA90300 (PubMed:10940552).Curated
Sequence conflicti645 – 6451Q → R in BAA90300 (PubMed:10940552).Curated
Sequence conflicti652 – 6543TQD → PQA in BAA90300 (PubMed:10940552).Curated
Sequence conflicti687 – 6871K → E in BAA90300 (PubMed:10940552).Curated
Sequence conflicti713 – 7131D → G in BAA90300 (PubMed:10940552).Curated
Sequence conflicti784 – 7841Missing in BAA90300 (PubMed:10940552).Curated
Sequence conflicti795 – 7951N → D in BAA90300 (PubMed:10940552).Curated
Sequence conflicti798 – 7981A → P in BAA90300 (PubMed:10940552).Curated
Sequence conflicti807 – 8071I → C in BAA90300 (PubMed:10940552).Curated
Sequence conflicti827 – 8293DIH → ISS in BAA90300 (PubMed:10940552).Curated
Sequence conflicti835 – 8351R → K in BAA90300 (PubMed:10940552).Curated
Sequence conflicti849 – 8491N → D in BAA90300 (PubMed:10940552).Curated
Sequence conflicti860 – 8601E → G in BAA90300 (PubMed:10940552).Curated
Sequence conflicti874 – 8741F → S in BAA90300 (PubMed:10940552).Curated
Sequence conflicti889 – 8891F → S in BAA90300 (PubMed:10940552).Curated
Sequence conflicti901 – 9011V → A in BAA90300 (PubMed:10940552).Curated
Sequence conflicti905 – 9051S → P in BAA90300 (PubMed:10940552).Curated
Sequence conflicti913 – 9131A → V in BAA90300 (PubMed:10940552).Curated
Sequence conflicti916 – 9161A → E in BAA90300 (PubMed:10940552).Curated
Sequence conflicti933 – 9331N → T in BAA90300 (PubMed:10940552).Curated
Sequence conflicti940 – 9401Q → K in BAA90300 (PubMed:10940552).Curated
Sequence conflicti949 – 9491Q → E in BAA90300 (PubMed:10940552).Curated
Sequence conflicti962 – 9621G → A in BAA90300 (PubMed:10940552).Curated
Sequence conflicti1120 – 11201T → A in BAA90300 (PubMed:10940552).Curated
Sequence conflicti1157 – 11571N → T in BAA90300 (PubMed:10940552).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 44MAEE → MPTPRDCGRLRSRAGRSRAG AACSRGAPRAAREALDCRRC RDAGGK in isoform 4. 1 PublicationVSP_041447
Alternative sequencei650 – 6501V → VS in isoform 2. 1 PublicationVSP_035607

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037360 mRNA. Translation: BAA90300.1.
AB033081 mRNA. Translation: BAA86569.2. Different initiation.
AK292930 mRNA. Translation: BAF85619.1.
AC087292 Genomic DNA. No translation available.
AC087742 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90448.1.
BC052308 mRNA. Translation: AAH52308.1. Sequence problems.
CCDSiCCDS42236.1. [Q9P2R3-2]
CCDS58502.1. [Q9P2R3-4]
RefSeqiNP_001244928.1. NM_001257999.1. [Q9P2R3-4]
NP_057460.3. NM_016376.3. [Q9P2R3-2]
XP_005256736.1. XM_005256679.2. [Q9P2R3-1]
UniGeneiHs.696087.

Genome annotation databases

EnsembliENST00000341657; ENSP00000343362; ENSG00000185722. [Q9P2R3-1]
ENST00000570535; ENSP00000459943; ENSG00000185722. [Q9P2R3-4]
ENST00000574367; ENSP00000459775; ENSG00000185722. [Q9P2R3-2]
GeneIDi51479.
KEGGihsa:51479.
UCSCiuc002fxn.4. human. [Q9P2R3-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037360 mRNA. Translation: BAA90300.1.
AB033081 mRNA. Translation: BAA86569.2. Different initiation.
AK292930 mRNA. Translation: BAF85619.1.
AC087292 Genomic DNA. No translation available.
AC087742 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90448.1.
BC052308 mRNA. Translation: AAH52308.1. Sequence problems.
CCDSiCCDS42236.1. [Q9P2R3-2]
CCDS58502.1. [Q9P2R3-4]
RefSeqiNP_001244928.1. NM_001257999.1. [Q9P2R3-4]
NP_057460.3. NM_016376.3. [Q9P2R3-2]
XP_005256736.1. XM_005256679.2. [Q9P2R3-1]
UniGeneiHs.696087.

3D structure databases

ProteinModelPortaliQ9P2R3.
SMRiQ9P2R3. Positions 53-193, 221-1074, 1100-1163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119564. 33 interactions.
DIPiDIP-46068N.
IntActiQ9P2R3. 18 interactions.
STRINGi9606.ENSP00000459775.

PTM databases

iPTMnetiQ9P2R3.
PhosphoSiteiQ9P2R3.

Polymorphism and mutation databases

BioMutaiANKFY1.
DMDMi33514905.

Proteomic databases

EPDiQ9P2R3.
MaxQBiQ9P2R3.
PaxDbiQ9P2R3.
PRIDEiQ9P2R3.

Protocols and materials databases

DNASUi51479.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341657; ENSP00000343362; ENSG00000185722. [Q9P2R3-1]
ENST00000570535; ENSP00000459943; ENSG00000185722. [Q9P2R3-4]
ENST00000574367; ENSP00000459775; ENSG00000185722. [Q9P2R3-2]
GeneIDi51479.
KEGGihsa:51479.
UCSCiuc002fxn.4. human. [Q9P2R3-1]

Organism-specific databases

CTDi51479.
GeneCardsiANKFY1.
H-InvDBHIX0013439.
HIX0173682.
HGNCiHGNC:20763. ANKFY1.
HPAiHPA024513.
HPA024522.
MIMi607927. gene.
neXtProtiNX_Q9P2R3.
PharmGKBiPA134984226.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4591. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129770.
HOGENOMiHOG000022583.
HOVERGENiHBG050501.
InParanoidiQ9P2R3.
OMAiWSLLHKA.
OrthoDBiEOG7327MZ.
PhylomeDBiQ9P2R3.
TreeFamiTF351263.

Miscellaneous databases

ChiTaRSiANKFY1. human.
GeneWikiiANKFY1.
GenomeRNAii51479.
PROiQ9P2R3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P2R3.
CleanExiHS_ANKFY1.
ExpressionAtlasiQ9P2R3. baseline and differential.
GenevisibleiQ9P2R3. HS.

Family and domain databases

Gene3Di1.25.40.20. 3 hits.
3.30.40.10. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF12796. Ank_2. 3 hits.
PF00651. BTB. 1 hit.
PF01363. FYVE. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 21 hits.
SM00225. BTB. 1 hit.
SM00064. FYVE. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 4 hits.
SSF54695. SSF54695. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 12 hits.
PS50097. BTB. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and chromosomal mapping of a novel human gene, ANKHZN."
    Kuriyama H., Asakawa S., Minoshima S., Maruyama H., Ishii N., Ito K., Gejyo F., Arakawa M., Shimizu N., Kuwano R.
    Gene 253:151-160(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Fetal brain.
  2. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), TISSUE SPECIFICITY.
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "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] (ISOFORM 2).
    Tissue: Trachea.
  5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] OF 1-458 (ISOFORM 1).
    Tissue: Mammary gland.
  8. Bienvenut W.V., Vousden K.H., Lukashchuk N.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11; 145-151 AND 924-931, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Lung carcinoma.
  9. "The Rab5 effector Rabankyrin-5 regulates and coordinates different endocytic mechanisms."
    Schnatwinkel C., Christoforidis S., Lindsay M.R., Uttenweiler-Joseph S., Wilm M., Parton R.G., Zerial M.
    PLoS Biol. 2:E261-E261(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RAB5A, SUBCELLULAR LOCATION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic trafficking and retromer function."
    Zhang J., Reiling C., Reinecke J.B., Prislan I., Marky L.A., Sorgen P.L., Naslavsky N., Caplan S.
    Traffic 13:745-757(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EHD1 AND VPS26A, MUTAGENESIS OF 421-ASN--PHE-423 AND 424-GLU-ASP-425.
  12. "RhoD binds the Rab5 effector Rabankyrin-5 and has a role in trafficking of the platelet-derived growth factor receptor."
    Nehru V., Voytyuk O., Lennartsson J., Aspenstroem P.
    Traffic 14:1242-1254(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ENDOSOMAL TRAFFICKING AND RECEPTOR INTERNALIZATION, INTERACTION WITH RHOD.
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiANFY1_HUMAN
AccessioniPrimary (citable) accession number: Q9P2R3
Secondary accession number(s): A8KA65, Q5RKV4, Q9ULG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: August 4, 2003
Last modified: June 8, 2016
This is version 132 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.