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Q15735

- PI5PA_HUMAN

UniProt

Q15735 - PI5PA_HUMAN

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Protein

Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A

Gene
INPP5J, PIB5PA, PIPP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles By similarity.

Catalytic activityi

D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate.
1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.

GO - Molecular functioni

  1. inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity Source: UniProtKB-EC
  2. inositol-1,4,5-trisphosphate 5-phosphatase activity Source: UniProtKB-EC
  3. inositol-polyphosphate 5-phosphatase activity Source: UniProtKB-EC
  4. phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity Source: Ensembl

GO - Biological processi

  1. inositol phosphate metabolic process Source: Reactome
  2. negative regulation of microtubule polymerization Source: Ensembl
  3. negative regulation of neuron projection development Source: Ensembl
  4. negative regulation of peptidyl-serine phosphorylation Source: Ensembl
  5. phosphatidylinositol biosynthetic process Source: Reactome
  6. phosphatidylinositol dephosphorylation Source: InterPro
  7. phospholipid metabolic process Source: Reactome
  8. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:HS11950-MONOMER.
ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (EC:3.1.3.56)
Alternative name(s):
Inositol polyphosphate 5-phosphatase J
Gene namesi
Name:INPP5J
Synonyms:PIB5PA, PIPP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:8956. INPP5J.

Subcellular locationi

Cytoplasm By similarity
Note: Predominantly localized to membrane ruffles By similarity.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Reactome
  3. dendritic shaft Source: Ensembl
  4. growth cone Source: Ensembl
  5. plasma membrane Source: Ensembl
  6. ruffle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164720918.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10061006Phosphatidylinositol 4,5-bisphosphate 5-phosphatase APRO_0000209738Add
BLAST

Proteomic databases

MaxQBiQ15735.
PaxDbiQ15735.
PRIDEiQ15735.

PTM databases

PhosphoSiteiQ15735.

Expressioni

Gene expression databases

ArrayExpressiQ15735.
BgeeiQ15735.
CleanExiHS_INPP5J.
GenevestigatoriQ15735.

Organism-specific databases

HPAiHPA034539.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000384534.

Structurei

3D structure databases

ProteinModelPortaliQ15735.
SMRiQ15735. Positions 423-728.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni425 – 728304Catalytic Reviewed predictionAdd
BLAST
Regioni729 – 840112Required for ruffle localization By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi102 – 1076RSXSXX motif 1
Motifi345 – 3506SH3-binding Reviewed prediction
Motifi350 – 3556RSXSXX motif 2
Motifi874 – 8796RSXSXX motif 3
Motifi885 – 8906RSXSXX motif 4
Motifi911 – 9166RSXSXX motif 5

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 371250Pro-richAdd
BLAST
Compositional biasi840 – 93798Ser-richAdd
BLAST

Domaini

The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute binding sites for the 14-3-3 protein.

Sequence similaritiesi

Keywords - Domaini

Repeat, SH3-binding

Phylogenomic databases

eggNOGiCOG5411.
HOGENOMiHOG000046051.
HOVERGENiHBG082135.
InParanoidiQ15735.
KOiK01106.
OMAiNIYQVTF.
OrthoDBiEOG789CB4.
PhylomeDBiQ15735.
TreeFamiTF317034.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTiSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15735-1) [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

MEGQSSRGSR RPGTRAGLGS LPMPQGVAQT GAPSKVDSSF QLPAKKNAAL     50
GPSEPRLALA PVGPRAAMSA SSEGPRLALA SPRPILAPLC TPEGQKTATA 100
HRSSSLAPTS VGQLVMSASA GPKPPPATTG SVLAPTSLGL VMPASAGPRS 150
PPVTLGPNLA PTSRDQKQEP PASVGPKPTL AASGLSLALA SEEQPPELPS 200
TPSPVPSPVL SPTQEQALAP ASTASGAASV GQTSARKRDA PAPRPLPASE 250
GHLQPPAQTS GPTGSPPCIQ TSPDPRLSPS FRARPEALHS SPEDPVLPRP 300
PQTLPLDVGQ GPSEPGTHSP GLLSPTFRPG APSGQTVPPP LPKPPRSPSR 350
SPSHSPNRSP CVPPAPDMAL PRLGTQSTGP GRCLSPNLQA QEAPAPVTTS 400
SSTSTLSSSP WSAQPTWKSD PGFRITVVTW NVGTAMPPDD VTSLLHLGGG 450
DDSDGADMIA IGLQEVNSML NKRLKDALFT DQWSELFMDA LGPFNFVLVS 500
SVRMQGVILL LFAKYYHLPF LRDVQTDCTR TGLGGYWGNK GGVSVRLAAF 550
GHMLCFLNCH LPAHMDKAEQ RKDNFQTILS LQQFQGPGAQ GILDHDLVFW 600
FGDLNFRIES YDLHFVKFAI DSDQLHQLWE KDQLNMAKNT WPILKGFQEG 650
PLNFAPTFKF DVGTNKYDTS AKKRKPAWTD RILWKVKAPG GGPSPSGRKS 700
HRLQVTQHSY RSHMEYTVSD HKPVAAQFLL QFAFRDDMPL VRLEVADEWV 750
RPEQAVVRYR METVFARSSW DWIGLYRVGF RHCKDYVAYV WAKHEDVDGN 800
TYQVTFSEES LPKGHGDFIL GYYSHNHSIL IGITEPFQIS LPSSELASSS 850
TDSSGTSSEG EDDSTLELLA PKSRSPSPGK SKRHRSRSPG LARFPGLALR 900
PSSRERRGAS RSPSPQSRRL SRVAPDRSSN GSSRGSSEEG PSGLPGPWAF 950
PPAVPRSLGL LPALRLETVD PGGGGSWGPD REALAPNSLS PSPQGHRGLE 1000
EGGLGP 1006
Length:1,006
Mass (Da):107,197
Last modified:October 17, 2006 - v3
Checksum:iADB6382AA33E15AC
GO
Isoform 2 (identifier: Q15735-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-367: Missing.

Show »
Length:639
Mass (Da):70,464
Checksum:i3ED5CD8BBB3398D0
GO
Isoform 3 (identifier: Q15735-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     56-423: Missing.

Note: No experimental confirmation available.

Show »
Length:638
Mass (Da):70,239
Checksum:i3F8ECF77ECC71C26
GO

Sequence cautioni

The sequence AAD15618.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti333 – 3331S → I.
Corresponds to variant rs12485025 [ dbSNP | Ensembl ].
VAR_028107

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 367367Missing in isoform 2. VSP_007296Add
BLAST
Alternative sequencei56 – 423368Missing in isoform 3. VSP_021017Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti610 – 6123SYD → ARG1 Publication
Sequence conflicti662 – 6621V → A in BAC86611. 1 Publication
Sequence conflicti791 – 7911W → R in AAI09289. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK092859 mRNA. Translation: BAG52616.1.
AK095944 mRNA. Translation: BAC04657.1.
AK126610 mRNA. Translation: BAC86611.1.
AC005005 Genomic DNA. Translation: AAD15618.1. Sequence problems.
CH471095 Genomic DNA. Translation: EAW59936.1.
BC109288 mRNA. Translation: AAI09289.1.
U45975 mRNA. Translation: AAB03216.1.
CCDSiCCDS46687.1. [Q15735-3]
CCDS63453.1. [Q15735-1]
CCDS63455.1. [Q15735-2]
RefSeqiNP_001002837.1. NM_001002837.2. [Q15735-3]
NP_001271214.1. NM_001284285.1. [Q15735-1]
NP_001271217.1. NM_001284288.1. [Q15735-2]
NP_001271218.1. NM_001284289.1. [Q15735-2]
UniGeneiHs.517549.

Genome annotation databases

EnsembliENST00000331075; ENSP00000333262; ENSG00000185133. [Q15735-1]
ENST00000400294; ENSP00000383150; ENSG00000185133. [Q15735-2]
ENST00000404390; ENSP00000384534; ENSG00000185133. [Q15735-3]
ENST00000405300; ENSP00000384596; ENSG00000185133. [Q15735-2]
GeneIDi27124.
KEGGihsa:27124.
UCSCiuc003ajs.4. human. [Q15735-1]
uc003ajt.4. human. [Q15735-3]

Polymorphism databases

DMDMi116242713.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK092859 mRNA. Translation: BAG52616.1 .
AK095944 mRNA. Translation: BAC04657.1 .
AK126610 mRNA. Translation: BAC86611.1 .
AC005005 Genomic DNA. Translation: AAD15618.1 . Sequence problems.
CH471095 Genomic DNA. Translation: EAW59936.1 .
BC109288 mRNA. Translation: AAI09289.1 .
U45975 mRNA. Translation: AAB03216.1 .
CCDSi CCDS46687.1. [Q15735-3 ]
CCDS63453.1. [Q15735-1 ]
CCDS63455.1. [Q15735-2 ]
RefSeqi NP_001002837.1. NM_001002837.2. [Q15735-3 ]
NP_001271214.1. NM_001284285.1. [Q15735-1 ]
NP_001271217.1. NM_001284288.1. [Q15735-2 ]
NP_001271218.1. NM_001284289.1. [Q15735-2 ]
UniGenei Hs.517549.

3D structure databases

ProteinModelPortali Q15735.
SMRi Q15735. Positions 423-728.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000384534.

PTM databases

PhosphoSitei Q15735.

Polymorphism databases

DMDMi 116242713.

Proteomic databases

MaxQBi Q15735.
PaxDbi Q15735.
PRIDEi Q15735.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331075 ; ENSP00000333262 ; ENSG00000185133 . [Q15735-1 ]
ENST00000400294 ; ENSP00000383150 ; ENSG00000185133 . [Q15735-2 ]
ENST00000404390 ; ENSP00000384534 ; ENSG00000185133 . [Q15735-3 ]
ENST00000405300 ; ENSP00000384596 ; ENSG00000185133 . [Q15735-2 ]
GeneIDi 27124.
KEGGi hsa:27124.
UCSCi uc003ajs.4. human. [Q15735-1 ]
uc003ajt.4. human. [Q15735-3 ]

Organism-specific databases

CTDi 27124.
GeneCardsi GC22P031518.
HGNCi HGNC:8956. INPP5J.
HPAi HPA034539.
MIMi 606481. gene.
neXtProti NX_Q15735.
PharmGKBi PA164720918.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5411.
HOGENOMi HOG000046051.
HOVERGENi HBG082135.
InParanoidi Q15735.
KOi K01106.
OMAi NIYQVTF.
OrthoDBi EOG789CB4.
PhylomeDBi Q15735.
TreeFami TF317034.

Enzyme and pathway databases

BioCyci MetaCyc:HS11950-MONOMER.
Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.
REACT_150312. Synthesis of IP3 and IP4 in the cytosol.
REACT_150352. Synthesis of IP2, IP, and Ins in the cytosol.

Miscellaneous databases

GeneWikii PIB5PA.
GenomeRNAii 27124.
NextBioi 49824.
PROi Q15735.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15735.
Bgeei Q15735.
CleanExi HS_INPP5J.
Genevestigatori Q15735.

Family and domain databases

Gene3Di 3.60.10.10. 1 hit.
InterProi IPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view ]
Pfami PF03372. Exo_endo_phos. 1 hit.
[Graphical view ]
SMARTi SM00128. IPPc. 1 hit.
[Graphical view ]
SUPFAMi SSF56219. SSF56219. 1 hit.
ProtoNeti Search...

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 AND 3).
    Tissue: Cerebellum, Heart and Spleen.
  2. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 2).
  5. Nussbaum R.L.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 610-1006.
    Tissue: Brain.

Entry informationi

Entry nameiPI5PA_HUMAN
AccessioniPrimary (citable) accession number: Q15735
Secondary accession number(s): B3KS54
, Q32M61, Q6ZTH6, Q8N902, Q9UDT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: October 17, 2006
Last modified: September 3, 2014
This is version 126 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi