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Protein

Glycerophosphoinositol inositolphosphodiesterase GDPD2

Gene

GDPD2

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

Functioni

Has glycerophosphoinositol inositolphosphodiesterase activity and specifically hydrolyzes glycerophosphoinositol, with no activity for other substrates such as glycerophosphoinositol 4-phosphate, glycerophosphocholine, glycerophosphoethanolamine, and glycerophosphoserine. Accelerates the program of osteoblast differentiation and growth. May play a role in remodeling of the actin cytoskeleton (By similarity).By similarity

Catalytic activityi

1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O = glycerol + 1D-myo-inositol 1-phosphate.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi256 – 2561Divalent metal cationSequence Analysis
Metal bindingi258 – 2581Divalent metal cationSequence Analysis
Metal bindingi271 – 2711Divalent metal cationSequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glycerophosphoinositol inositolphosphodiesterase GDPD2 (EC:3.1.4.43)
Alternative name(s):
Glycerophosphodiester phosphodiesterase 3
Glycerophosphodiester phosphodiesterase domain-containing protein 2
Osteoblast differentiation promoting factor
Gene namesi
Name:GDPD2
Synonyms:GDE3, OBDPF
ORF Names:UNQ1935/PRO4418
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:25974. GDPD2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3838CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei39 – 5921HelicalSequence AnalysisAdd
BLAST
Topological domaini60 – 8526ExtracellularSequence AnalysisAdd
BLAST
Transmembranei86 – 10621HelicalSequence AnalysisAdd
BLAST
Topological domaini107 – 12115CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence AnalysisAdd
BLAST
Topological domaini143 – 15412ExtracellularSequence AnalysisAdd
BLAST
Transmembranei155 – 17521HelicalSequence AnalysisAdd
BLAST
Topological domaini176 – 18813CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei189 – 20921HelicalSequence AnalysisAdd
BLAST
Topological domaini210 – 490281ExtracellularSequence AnalysisAdd
BLAST
Transmembranei491 – 51121HelicalSequence AnalysisAdd
BLAST
Topological domaini512 – 53928CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134907263.

Polymorphism and mutation databases

BioMutaiGDPD2.
DMDMi74752794.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 539539Glycerophosphoinositol inositolphosphodiesterase GDPD2PRO_0000251934Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi442 – 4421N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9HCC8.
PRIDEiQ9HCC8.

PTM databases

PhosphoSiteiQ9HCC8.

Expressioni

Gene expression databases

BgeeiQ9HCC8.
CleanExiHS_GDPD2.
GenevisibleiQ9HCC8. HS.

Organism-specific databases

HPAiHPA045026.

Interactioni

Protein-protein interaction databases

BioGridi120207. 4 interactions.
IntActiQ9HCC8. 41 interactions.
MINTiMINT-1426959.
STRINGi9606.ENSP00000414019.

Structurei

3D structure databases

ProteinModelPortaliQ9HCC8.
SMRiQ9HCC8. Positions 226-377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini224 – 479256GP-PDEAdd
BLAST

Sequence similaritiesi

Contains 1 GP-PDE domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0584.
GeneTreeiENSGT00510000046457.
HOGENOMiHOG000232101.
HOVERGENiHBG081551.
InParanoidiQ9HCC8.
KOiK01124.
OMAiIKALHQD.
OrthoDBiEOG7F511B.
PhylomeDBiQ9HCC8.
TreeFamiTF313692.

Family and domain databases

Gene3Di3.20.20.190. 1 hit.
InterProiIPR004129. GlyceroP-diester-Pdiesterase.
IPR030395. GP_PDE_dom.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
[Graphical view]
PANTHERiPTHR23344. PTHR23344. 1 hit.
PfamiPF03009. GDPD. 1 hit.
[Graphical view]
SUPFAMiSSF51695. SSF51695. 1 hit.
PROSITEiPS51704. GP_PDE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9HCC8-1) [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
MAESPGCCSV WARCLHCLYS CHWRKCPRER MQTSKCDCIW FGLLFLTFLL
60 70 80 90 100
SLSWLYIGLV LLNDLHNFNE FLFRRWGHWM DWSLAFLLVI SLLVTYASLL
110 120 130 140 150
LVLALLLRLC RQPLHLHSLH KVLLLLIMLL VAAGLVGLDI QWQQEWHSLR
160 170 180 190 200
VSLQATAPFL HIGAAAGIAL LAWPVADTFY RIHRRGPKIL LLLLFFGVVL
210 220 230 240 250
VIYLAPLCIS SPCIMEPRDL PPKPGLVGHR GAPMLAPENT LMSLRKTAEC
260 270 280 290 300
GATVFETDVM VSSDGVPFLM HDEHLSRTTN VASVFPTRIT AHSSDFSWTE
310 320 330 340 350
LKRLNAGSWF LERRPFWGAK PLAGPDQKEA ESQTVPALEE LLEEAAALNL
360 370 380 390 400
SIMFDLRRPP QNHTYYDTFV IQTLETVLNA RVPQAMVFWL PDEDRANVQR
410 420 430 440 450
RAPGMRQIYG RQGGNRTERP QFLNLPYQDL PLLDIKALHK DNVSVNLFVV
460 470 480 490 500
NKPWLFSLLW CAGVDSVTTN DCQLLQQMRY PIWLITPQTY LIIWVITNCV
510 520 530
STMLLLWTFL LQRRFVKKRG KTGLETAVLL TRINNFMME
Length:539
Mass (Da):61,729
Last modified:March 1, 2001 - v1
Checksum:i8271C3A74766D540
GO
Isoform 2 (identifier: Q9HCC8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.

Note: No experimental confirmation available.
Show »
Length:460
Mass (Da):52,186
Checksum:i16081E6BAB94B16A
GO
Isoform 3 (identifier: Q9HCC8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     436-436: K → KDRFLLPAQAGLKLLASSNLPASASQSAGITGLSHCPPQPPGYKHELSHLAM

Note: No experimental confirmation available.
Show »
Length:590
Mass (Da):66,991
Checksum:i1DC750F7411D9FDA
GO

Sequence cautioni

The sequence BAA91014.1 differs from that shown. Reason: Frameshift at position 397. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti418 – 4181E → G in BAA91014 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7979Missing in isoform 2. 1 PublicationVSP_042622Add
BLAST
Alternative sequencei436 – 4361K → KDRFLLPAQAGLKLLASSNL PASASQSAGITGLSHCPPQP PGYKHELSHLAM in isoform 3. 1 PublicationVSP_042623

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB048363 mRNA. Translation: BAB13350.1.
AY358986 mRNA. Translation: AAQ89345.1.
AK000214 mRNA. Translation: BAA91014.1. Frameshift.
AK299255 mRNA. Translation: BAG61286.1.
AK301025 mRNA. Translation: BAG62641.1.
AK316035 mRNA. Translation: BAH14406.1.
AL139398 Genomic DNA. Translation: CAI41020.1.
BC032009 mRNA. Translation: AAH32009.1.
CCDSiCCDS14402.1. [Q9HCC8-1]
CCDS55437.1. [Q9HCC8-3]
CCDS55438.1. [Q9HCC8-2]
RefSeqiNP_001164662.1. NM_001171191.1. [Q9HCC8-2]
NP_001164663.1. NM_001171192.1. [Q9HCC8-3]
NP_001164664.1. NM_001171193.1. [Q9HCC8-2]
NP_060181.2. NM_017711.3. [Q9HCC8-1]
UniGeneiHs.438712.

Genome annotation databases

EnsembliENST00000374382; ENSP00000363503; ENSG00000130055. [Q9HCC8-1]
ENST00000453994; ENSP00000414019; ENSG00000130055. [Q9HCC8-3]
ENST00000536730; ENSP00000445982; ENSG00000130055. [Q9HCC8-2]
ENST00000538649; ENSP00000444601; ENSG00000130055. [Q9HCC8-2]
GeneIDi54857.
KEGGihsa:54857.
UCSCiuc004dyh.3. human. [Q9HCC8-1]
uc011mpk.2. human. [Q9HCC8-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB048363 mRNA. Translation: BAB13350.1.
AY358986 mRNA. Translation: AAQ89345.1.
AK000214 mRNA. Translation: BAA91014.1. Frameshift.
AK299255 mRNA. Translation: BAG61286.1.
AK301025 mRNA. Translation: BAG62641.1.
AK316035 mRNA. Translation: BAH14406.1.
AL139398 Genomic DNA. Translation: CAI41020.1.
BC032009 mRNA. Translation: AAH32009.1.
CCDSiCCDS14402.1. [Q9HCC8-1]
CCDS55437.1. [Q9HCC8-3]
CCDS55438.1. [Q9HCC8-2]
RefSeqiNP_001164662.1. NM_001171191.1. [Q9HCC8-2]
NP_001164663.1. NM_001171192.1. [Q9HCC8-3]
NP_001164664.1. NM_001171193.1. [Q9HCC8-2]
NP_060181.2. NM_017711.3. [Q9HCC8-1]
UniGeneiHs.438712.

3D structure databases

ProteinModelPortaliQ9HCC8.
SMRiQ9HCC8. Positions 226-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120207. 4 interactions.
IntActiQ9HCC8. 41 interactions.
MINTiMINT-1426959.
STRINGi9606.ENSP00000414019.

PTM databases

PhosphoSiteiQ9HCC8.

Polymorphism and mutation databases

BioMutaiGDPD2.
DMDMi74752794.

Proteomic databases

PaxDbiQ9HCC8.
PRIDEiQ9HCC8.

Protocols and materials databases

DNASUi54857.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374382; ENSP00000363503; ENSG00000130055. [Q9HCC8-1]
ENST00000453994; ENSP00000414019; ENSG00000130055. [Q9HCC8-3]
ENST00000536730; ENSP00000445982; ENSG00000130055. [Q9HCC8-2]
ENST00000538649; ENSP00000444601; ENSG00000130055. [Q9HCC8-2]
GeneIDi54857.
KEGGihsa:54857.
UCSCiuc004dyh.3. human. [Q9HCC8-1]
uc011mpk.2. human. [Q9HCC8-3]

Organism-specific databases

CTDi54857.
GeneCardsiGC0XP069642.
HGNCiHGNC:25974. GDPD2.
HPAiHPA045026.
neXtProtiNX_Q9HCC8.
PharmGKBiPA134907263.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0584.
GeneTreeiENSGT00510000046457.
HOGENOMiHOG000232101.
HOVERGENiHBG081551.
InParanoidiQ9HCC8.
KOiK01124.
OMAiIKALHQD.
OrthoDBiEOG7F511B.
PhylomeDBiQ9HCC8.
TreeFamiTF313692.

Miscellaneous databases

GenomeRNAii54857.
NextBioi57728.
PROiQ9HCC8.

Gene expression databases

BgeeiQ9HCC8.
CleanExiHS_GDPD2.
GenevisibleiQ9HCC8. HS.

Family and domain databases

Gene3Di3.20.20.190. 1 hit.
InterProiIPR004129. GlyceroP-diester-Pdiesterase.
IPR030395. GP_PDE_dom.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
[Graphical view]
PANTHERiPTHR23344. PTHR23344. 1 hit.
PfamiPF03009. GDPD. 1 hit.
[Graphical view]
SUPFAMiSSF51695. SSF51695. 1 hit.
PROSITEiPS51704. GP_PDE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Novel membrane protein containing glycerophosphodiester phosphodiesterase motif is transiently expressed during osteoblast differentiation."
    Yanaka N., Imai Y., Kawai E., Akatsuka H., Wakimoto K., Nogusa Y., Kato N., Chiba H., Kotani E., Omori K., Sakurai N.
    J. Biol. Chem. 278:43595-43602(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "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 1; 2 AND 3).
    Tissue: Caudate nucleus, Colon mucosa and Spleen.
  4. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORM 1).
    Tissue: Skin.

Entry informationi

Entry nameiGDPD2_HUMAN
AccessioniPrimary (citable) accession number: Q9HCC8
Secondary accession number(s): B4DRH4, B4DVC9, Q9NXJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2001
Last modified: June 24, 2015
This is version 118 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 catalytic domain of GDPD2 is oriented extracellularly; Glycerophosphoinositol is hydrolyzed in the medium of cells overexpressing Gdpd2, whereas intracellular levels of glycerophosphoinositol is not affected.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. 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.