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Q6U7H8

- PI5L1_MOUSE

UniProt

Q6U7H8 - PI5L1_MOUSE

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Protein

Phosphatidylinositol 4-phosphate 5-kinase-like protein 1

Gene

Pip5kl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

May act as a scaffold to localize and regulate type I PI4P 5-kinases to specific compartments within the cell, where they generate PI(4,5)P2 for actin nucleation, signaling and scaffold protein recruitment and conversion to PI(3,4,5)P3.1 Publication

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.

GO - Molecular functioni

  1. 1-phosphatidylinositol-4-phosphate 5-kinase activity Source: MGI
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. phosphatidylinositol phosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-phosphate 5-kinase-like protein 1 (EC:2.7.1.68)
Short name:
PI(4)P 5-kinase-like protein 1
Short name:
PtdIns(4)P-5-kinase-like protein 1
Alternative name(s):
Phosphatidylinositol phosphate kinase homolog
Short name:
PIPKH
Gene namesi
Name:Pip5kl1
Synonyms:Pipkh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2448520. Pip5kl1.

Subcellular locationi

Cytoplasm 1 Publication. Membrane 1 Publication
Note: Localized to large cytoplasmic vesicular structures.

GO - Cellular componenti

  1. cell projection Source: MGI
  2. cytoplasm Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi155 – 1551K → R: No change. No change; when associated with A-281. 1 Publication
Mutagenesisi281 – 2811D → A: No change. No change; when associated with R-155. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395Phosphatidylinositol 4-phosphate 5-kinase-like protein 1PRO_0000285759Add
BLAST

Proteomic databases

PRIDEiQ6U7H8.

PTM databases

PhosphoSiteiQ6U7H8.

Expressioni

Tissue specificityi

Highly expressed in brain and testis, relatively to heart, spleen, lung, liver, skeletal muscle and kidney.1 Publication

Gene expression databases

BgeeiQ6U7H8.
CleanExiMM_PIP5KL1.
GenevestigatoriQ6U7H8.

Interactioni

Subunit structurei

Heterodimerizes with other type I phosphatidylinositol 4-phosphate 5-kinase.

Structurei

3D structure databases

ProteinModelPortaliQ6U7H8.
SMRiQ6U7H8. Positions 107-289.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 394358PIPKPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PIPK domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5253.
GeneTreeiENSGT00760000119184.
HOVERGENiHBG097351.
InParanoidiQ6U7H8.
KOiK13712.
OMAiPQRSWFL.
OrthoDBiEOG77DJ5R.
PhylomeDBiQ6U7H8.
TreeFamiTF354315.

Family and domain databases

Gene3Di3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProiIPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
[Graphical view]
PANTHERiPTHR23086. PTHR23086. 1 hit.
PfamiPF01504. PIP5K. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6U7H8-1) [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
MATPSLRSHE IPAHSQEAGN KSISSGSRRG LLWHLRARQS RVGLFEVGPG
60 70 80 90 100
HELHRMTRMM QEGLWAATQV SKNNPPTGPT TQKDYLEVMT QVHEEGFELG
110 120 130 140 150
TLAGPAFARL RKSIGLTEED YQATLGPGDP YLQFFSTSKS KASFFLTHDQ
160 170 180 190 200
RFFVKTQRRH EVHVLLAHLP RYVEHLQQYP HSLLARLLGV YSLRVAQGKK
210 220 230 240 250
KYFIIMQCIF YPTSRISERY DIKGCNISRW VDPAPEGSPL VLVLKDLNFQ
260 270 280 290 300
EKTMRLGAQR SWFLRQMELD TAFLREVNVL DYSLLVAIQF LHEDEKGIHH
310 320 330 340 350
SVFSTFKSIQ GVSKSKGTGD QNCRMLPDLP NALHILDGPD QRYFLGLVDM
360 370 380 390
TTVYGFRKRL EHVWKMVRYP GQSVSTVSPA HYARRLCRWA EVHTE
Length:395
Mass (Da):45,293
Last modified:July 5, 2004 - v1
Checksum:i22AA0A86324972AB
GO
Isoform 2 (identifier: Q6U7H8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MATPSLRSHE → MLFVSCASSHQ

Note: No experimental confirmation available.

Show »
Length:396
Mass (Da):45,374
Checksum:i243270F8EC48F3A9
GO
Isoform 3 (identifier: Q6U7H8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     10-10: E → EVGADQRGDKKGKGESLAITLARGLNTPPPRLCSGKIKTRPTE
     308-395: SIQGVSKSKG...LCRWAEVHTE → RTVTPAMLAMALTETTH

Note: No experimental confirmation available.

Show »
Length:366
Mass (Da):41,464
Checksum:i9BC2D0BB5AF9FE44
GO
Isoform 4 (identifier: Q6U7H8-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     201-216: KYFIIMQCIFYPTSRI → VSVADRGGSAVGAAGG
     217-395: Missing.

Note: No experimental confirmation available.

Show »
Length:216
Mass (Da):23,937
Checksum:iD3146CE96D0EEC6F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti215 – 2184RISE → VLPP in AAH28795. (PubMed:15489334)Curated
Sequence conflicti265 – 2651R → Q in AAH28795. (PubMed:15489334)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1010MATPSLRSHE → MLFVSCASSHQ in isoform 2. 1 PublicationVSP_024905
Alternative sequencei10 – 101E → EVGADQRGDKKGKGESLAIT LARGLNTPPPRLCSGKIKTR PTE in isoform 3. 1 PublicationVSP_024906
Alternative sequencei201 – 21616KYFII…PTSRI → VSVADRGGSAVGAAGG in isoform 4. 1 PublicationVSP_024907Add
BLAST
Alternative sequencei217 – 395179Missing in isoform 4. 1 PublicationVSP_024908Add
BLAST
Alternative sequencei308 – 39588SIQGV…EVHTE → RTVTPAMLAMALTETTH in isoform 3. 1 PublicationVSP_024909Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY376879 mRNA. Translation: AAQ92365.1.
AK133244 mRNA. Translation: BAE21576.1.
AK164998 mRNA. Translation: BAE37997.1.
AL928710 Genomic DNA. Translation: CAM18808.1.
BC028795 mRNA. Translation: AAH28795.1.
BC094346 mRNA. Translation: AAH94346.1.
BC117018 mRNA. Translation: AAI17019.1.
BC119037 mRNA. Translation: AAI19038.1.
CCDSiCCDS15920.1. [Q6U7H8-1]
RefSeqiNP_937834.1. NM_198191.2. [Q6U7H8-1]
UniGeneiMm.78923.

Genome annotation databases

EnsembliENSMUST00000055304; ENSMUSP00000051282; ENSMUSG00000046854. [Q6U7H8-1]
ENSMUST00000100188; ENSMUSP00000097763; ENSMUSG00000046854. [Q6U7H8-3]
GeneIDi227733.
KEGGimmu:227733.
UCSCiuc008jfv.1. mouse. [Q6U7H8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY376879 mRNA. Translation: AAQ92365.1 .
AK133244 mRNA. Translation: BAE21576.1 .
AK164998 mRNA. Translation: BAE37997.1 .
AL928710 Genomic DNA. Translation: CAM18808.1 .
BC028795 mRNA. Translation: AAH28795.1 .
BC094346 mRNA. Translation: AAH94346.1 .
BC117018 mRNA. Translation: AAI17019.1 .
BC119037 mRNA. Translation: AAI19038.1 .
CCDSi CCDS15920.1. [Q6U7H8-1 ]
RefSeqi NP_937834.1. NM_198191.2. [Q6U7H8-1 ]
UniGenei Mm.78923.

3D structure databases

ProteinModelPortali Q6U7H8.
SMRi Q6U7H8. Positions 107-289.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q6U7H8.

Proteomic databases

PRIDEi Q6U7H8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000055304 ; ENSMUSP00000051282 ; ENSMUSG00000046854 . [Q6U7H8-1 ]
ENSMUST00000100188 ; ENSMUSP00000097763 ; ENSMUSG00000046854 . [Q6U7H8-3 ]
GeneIDi 227733.
KEGGi mmu:227733.
UCSCi uc008jfv.1. mouse. [Q6U7H8-1 ]

Organism-specific databases

CTDi 138429.
MGIi MGI:2448520. Pip5kl1.

Phylogenomic databases

eggNOGi COG5253.
GeneTreei ENSGT00760000119184.
HOVERGENi HBG097351.
InParanoidi Q6U7H8.
KOi K13712.
OMAi PQRSWFL.
OrthoDBi EOG77DJ5R.
PhylomeDBi Q6U7H8.
TreeFami TF354315.

Miscellaneous databases

NextBioi 378800.
PROi Q6U7H8.
SOURCEi Search...

Gene expression databases

Bgeei Q6U7H8.
CleanExi MM_PIP5KL1.
Genevestigatori Q6U7H8.

Family and domain databases

Gene3Di 3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProi IPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
[Graphical view ]
PANTHERi PTHR23086. PTHR23086. 1 hit.
Pfami PF01504. PIP5K. 1 hit.
[Graphical view ]
PROSITEi PS51455. PIPK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a phosphoinositide phosphate kinase homolog."
    Chang J.D., Field S.J., Rameh L.E., Carpenter C.L., Cantley L.C.
    J. Biol. Chem. 279:11672-11679(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-155 AND ASP-281.
    Strain: C57BL/6.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Eye and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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] (ISOFORMS 1 AND 4).
    Strain: C57BL/6J.
    Tissue: Brain and Mammary gland.

Entry informationi

Entry nameiPI5L1_MOUSE
AccessioniPrimary (citable) accession number: Q6U7H8
Secondary accession number(s): A2ASY7
, A2ASY9, Q3TNU0, Q3V0C8, Q52KH3, Q8K345
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3