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Protein

Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1

Gene

INPP5D

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

Functioni

Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Acts as a negative regulator of B-cell antigen receptor signaling. Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Acts as a negative regulator of myeloid cell proliferation/survival and chemotaxis, mast cell degranulation, immune cells homeostasis, integrin alpha-IIb/beta-3 signaling in platelets and JNK signaling in B-cells. Regulates proliferation of osteoclast precursors, macrophage programming, phagocytosis and activation and is required for endotoxin tolerance. Involved in the control of cell-cell junctions, CD32a signaling in neutrophils and modulation of EGF-induced phospholipase C activity. Key regulator of neutrophil migration, by governing the formation of the leading edge and polarization required for chemotaxis. Modulates FCGR3/CD16-mediated cytotoxicity in NK cells. Mediates the activin/TGF-beta-induced apoptosis through its Smad-dependent expression. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6.2 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 3,4-diphosphate + phosphate.2 Publications

Enzyme regulationi

Activated upon translocation to the sites of synthesis of PtdIns(3,4,5)P3 in the membrane.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Apoptosis, Immunity

Enzyme and pathway databases

BioCyciMetaCyc:HS09849-MONOMER.
ZFISH:HS09849-MONOMER.
BRENDAi3.1.3.86. 2681.
ReactomeiR-HSA-1660499. Synthesis of PIPs at the plasma membrane.
R-HSA-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-HSA-202424. Downstream TCR signaling.
R-HSA-210990. PECAM1 interactions.
R-HSA-912526. Interleukin receptor SHC signaling.
SignaLinkiQ92835.
SIGNORiQ92835.

Chemistry databases

SwissLipidsiSLP:000000951.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC:3.1.3.86)
Alternative name(s):
Inositol polyphosphate-5-phosphatase of 145 kDa
Short name:
SIP-145
SH2 domain-containing inositol 5'-phosphatase 1
Short name:
SH2 domain-containing inositol phosphatase 1
Short name:
SHIP-1
p150Ship
Short name:
hp51CN
Gene namesi
Name:INPP5D
Synonyms:SHIP, SHIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6079. INPP5D.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cell membrane By similarity; Peripheral membrane protein By similarity
  • Membrane raft By similarity
  • Cytoplasmcytoskeleton By similarity
  • Membrane 1 Publication; Peripheral membrane protein 1 Publication

  • Note: Translocates to the plasma membrane when activated, translocation is probably due to different mechanisms depending on the stimulus and cell type. Translocates from the cytoplasm to membrane ruffles in a FCGR3/CD16-dependent manner. Colocalizes with FC-gamma-RIIB receptor (FCGR2B) or FCGR3/CD16 at membrane ruffles. Tyrosine phosphorylation may also participate in membrane localization.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

DisGeNETi3635.
OpenTargetsiENSG00000168918.
ENSG00000281614.
PharmGKBiPA29887.

Chemistry databases

ChEMBLiCHEMBL1781870.

Polymorphism and mutation databases

BioMutaiINPP5D.
DMDMi158564077.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003028661 – 1189Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1Add BLAST1189

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei243PhosphoserineBy similarity1
Modified residuei915PhosphotyrosineCombined sources1
Modified residuei934PhosphoserineBy similarity1
Modified residuei944PhosphotyrosineBy similarity1
Modified residuei960PhosphoserineCombined sources1
Modified residuei963PhosphothreonineCombined sources1
Modified residuei971PhosphoserineCombined sources1
Modified residuei1022PhosphotyrosineBy similarity1

Post-translational modificationi

Tyrosine phosphorylated by the members of the SRC family after exposure to a diverse array of extracellular stimuli such as cytokines, growth factors, antibodies, chemokines, integrin ligands and hypertonic and oxidative stress. Phosphorylated upon IgG receptor FCGR2B-binding.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ92835.
MaxQBiQ92835.
PaxDbiQ92835.
PeptideAtlasiQ92835.
PRIDEiQ92835.

PTM databases

DEPODiQ92835.
iPTMnetiQ92835.
PhosphoSitePlusiQ92835.

Expressioni

Tissue specificityi

Specifically expressed in immune and hematopoietic cells. Expressed in bone marrow and blood cells. Levels vary considerably within this compartment. Present in at least 74% of immature CD34+ cells, whereas within the more mature population of CD33+ cells, it is present in only 10% of cells. Present in the majority of T-cells, while it is present in a minority of B-cells (at protein level).4 Publications

Gene expression databases

BgeeiENSG00000168918.
CleanExiHS_INPP5D.
ExpressionAtlasiQ92835. baseline and differential.
GenevisibleiQ92835. HS.

Organism-specific databases

HPAiCAB016300.
HPA070455.

Interactioni

Subunit structurei

Interacts with tyrosine phosphorylated forms of SHC1, DOK1, DOK3, PTPN11/SHP-2, SLAMF1/CD150. Interacts with PTPN11 in response to IL-3. Interacts with receptors EPOR, MS4A2/FCER1B and FCER1G, FCGR2A, FCGR2B and FCGR3. Interacts with GRB2 and PLCG1. Interacts with tyrosine kinases SRC and TEC. Interacts with FCGR2A, leading to regulate gene expression during the phagocytic process. Interacts with c-Met/MET (By similarity). Interacts with MILR1 (tyrosine-phosphorylated). Can weakly interact (via NPXY motif 2) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
CD244Q9BZW86EBI-1380477,EBI-1580565
FCGR2BP319943EBI-1380477,EBI-724784
KHDRBS3O755253EBI-1380477,EBI-722504
KRT31Q153233EBI-1380477,EBI-948001
KRT40Q6A1623EBI-1380477,EBI-10171697
KRTAP10-7P604093EBI-1380477,EBI-10172290
KRTAP10-9P604113EBI-1380477,EBI-10172052
NOTCH2NLQ7Z3S93EBI-1380477,EBI-945833
SH3KBP1Q96B976EBI-1380477,EBI-346595

Protein-protein interaction databases

BioGridi109847. 40 interactors.
IntActiQ92835. 26 interactors.
MINTiMINT-123561.
STRINGi9606.ENSP00000352575.

Structurei

Secondary structure

11189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi12 – 22Combined sources11
Beta strandi27 – 32Combined sources6
Beta strandi39 – 45Combined sources7
Beta strandi50 – 57Combined sources8
Beta strandi63 – 65Combined sources3
Beta strandi70 – 72Combined sources3
Beta strandi76 – 78Combined sources3
Helixi79 – 85Combined sources7
Beta strandi88 – 95Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YSXNMR-A1-112[»]
ProteinModelPortaliQ92835.
SMRiQ92835.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92835.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 101SH2PROSITE-ProRule annotationAdd BLAST97

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1016 – 1030Interaction with DAB2By similarityAdd BLAST15

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi124 – 129SH3-binding 16
Motifi912 – 915NPXY motif 14
Motifi969 – 974SH3-binding 26
Motifi1019 – 1022NPXY motif 24
Motifi1040 – 1051SH3-binding 3Add BLAST12

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi920 – 1148Pro-richAdd BLAST229

Domaini

The SH2 domain interacts with tyrosine phosphorylated forms of proteins such as SHC1 or PTPN11/SHP-2. It competes with that of GRB2 for binding to phosphorylated SHC1 to inhibit the Ras pathway. It is also required for tyrosine phosphorylation (By similarity).By similarity
The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain.By similarity

Sequence similaritiesi

Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain, SH3-binding

Phylogenomic databases

eggNOGiKOG0565. Eukaryota.
COG5411. LUCA.
GeneTreeiENSGT00760000119075.
HOVERGENiHBG106726.
InParanoidiQ92835.
KOiK03084.
OMAiLTKPEMF.
OrthoDBiEOG091G00P6.
PhylomeDBiQ92835.
TreeFamiTF323475.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR000980. SH2.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00128. IPPc. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEiPS50001. SH2. 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: Q92835-1) [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
MVPCWNHGNI TRSKAEELLS RTGKDGSFLV RASESISRAY ALCVLYRNCV
60 70 80 90 100
YTYRILPNED DKFTVQASEG VSMRFFTKLD QLIEFYKKEN MGLVTHLQYP
110 120 130 140 150
VPLEEEDTGD DPEEDTVESV VSPPELPPRN IPLTASSCEA KEVPFSNENP
160 170 180 190 200
RATETSRPSL SETLFQRLQS MDTSGLPEEH LKAIQDYLST QLAQDSEFVK
210 220 230 240 250
TGSSSLPHLK KLTTLLCKEL YGEVIRTLPS LESLQRLFDQ QLSPGLRPRP
260 270 280 290 300
QVPGEANPIN MVSKLSQLTS LLSSIEDKVK ALLHEGPESP HRPSLIPPVT
310 320 330 340 350
FEVKAESLGI PQKMQLKVDV ESGKLIIKKS KDGSEDKFYS HKKILQLIKS
360 370 380 390 400
QKFLNKLVIL VETEKEKILR KEYVFADSKK REGFCQLLQQ MKNKHSEQPE
410 420 430 440 450
PDMITIFIGT WNMGNAPPPK KITSWFLSKG QGKTRDDSAD YIPHDIYVIG
460 470 480 490 500
TQEDPLSEKE WLEILKHSLQ EITSVTFKTV AIHTLWNIRI VVLAKPEHEN
510 520 530 540 550
RISHICTDNV KTGIANTLGN KGAVGVSFMF NGTSLGFVNS HLTSGSEKKL
560 570 580 590 600
RRNQNYMNIL RFLALGDKKL SPFNITHRFT HLFWFGDLNY RVDLPTWEAE
610 620 630 640 650
TIIQKIKQQQ YADLLSHDQL LTERREQKVF LHFEEEEITF APTYRFERLT
660 670 680 690 700
RDKYAYTKQK ATGMKYNLPS WCDRVLWKSY PLVHVVCQSY GSTSDIMTSD
710 720 730 740 750
HSPVFATFEA GVTSQFVSKN GPGTVDSQGQ IEFLRCYATL KTKSQTKFYL
760 770 780 790 800
EFHSSCLESF VKSQEGENEE GSEGELVVKF GETLPKLKPI ISDPEYLLDQ
810 820 830 840 850
HILISIKSSD SDESYGEGCI ALRLEATETQ LPIYTPLTHH GELTGHFQGE
860 870 880 890 900
IKLQTSQGKT REKLYDFVKT ERDESSGPKT LKSLTSHDPM KQWEVTSRAP
910 920 930 940 950
PCSGSSITEI INPNYMGVGP FGPPMPLHVK QTLSPDQQPT AWSYDQPPKD
960 970 980 990 1000
SPLGPCRGES PPTPPGQPPI SPKKFLPSTA NRGLPPRTQE SRPSDLGKNA
1010 1020 1030 1040 1050
GDTLPQEDLP LTKPEMFENP LYGSLSSFPK PAPRKDQESP KMPRKEPPPC
1060 1070 1080 1090 1100
PEPGILSPSI VLTKAQEADR GEGPGKQVPA PRLRSFTCSS SAEGRAAGGD
1110 1120 1130 1140 1150
KSQGKPKTPV SSQAPVPAKR PIKPSRSEIN QQTPPTPTPR PPLPVKSPAV
1160 1170 1180
LHLQHSKGRD YRDNTELPHH GKHRPEEGPP GPLGRTAMQ
Length:1,189
Mass (Da):133,292
Last modified:September 11, 2007 - v2
Checksum:i7958E91A64A4B68B
GO
Isoform 2 (identifier: Q92835-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     117-117: Missing.

Show »
Length:1,188
Mass (Da):133,193
Checksum:i335673E161C5FFAD
GO
Isoform 3 (identifier: Q92835-3) [UniParc]FASTAAdd to basket
Also known as: SIP-110

The sequence of this isoform differs from the canonical sequence as follows:
     1-212: Missing.
     213-222: TTLLCKELYG → MFTLSPAPR

Show »
Length:976
Mass (Da):109,294
Checksum:i2B90E6DD584DD048
GO

Sequence cautioni

The sequence AAC50454 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25 – 26DG → GT in AAB49680 (PubMed:9058707).Curated2
Sequence conflicti1029P → H in AAB49680 (PubMed:9058707).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034979685V → E in one patient with acute myeloid leukemya; somatic mutation. 1 Publication1
Natural variantiVAR_0593581169H → Y.2 PublicationsCorresponds to variant rs9247dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0279771 – 212Missing in isoform 3. 1 PublicationAdd BLAST212
Alternative sequenceiVSP_027978117Missing in isoform 2. 3 Publications1
Alternative sequenceiVSP_027979213 – 222TTLLCKELYG → MFTLSPAPR in isoform 3. 1 Publication10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98429 mRNA. Translation: CAA67071.1.
U57650 mRNA. Translation: AAB53573.1.
U50040 mRNA. Translation: AAC50453.1.
U50041 mRNA. Translation: AAC50454.1. Different initiation.
U84400 mRNA. Translation: AAB49680.1.
U53470 mRNA. Translation: AAD00081.1.
BC062985 mRNA. Translation: AAH62985.1.
BC099920 mRNA. Translation: AAH99920.1.
BC113580 mRNA. Translation: AAI13581.1.
BC113582 mRNA. Translation: AAI13583.1.
CCDSiCCDS74672.1. [Q92835-1]
CCDS77543.1. [Q92835-2]
PIRiJC4889.
RefSeqiNP_001017915.1. NM_001017915.2. [Q92835-1]
NP_005532.2. NM_005541.4. [Q92835-2]
UniGeneiHs.262886.
Hs.601911.

Genome annotation databases

EnsembliENST00000359570; ENSP00000352575; ENSG00000168918. [Q92835-2]
ENST00000445964; ENSP00000405338; ENSG00000168918. [Q92835-1]
ENST00000629761; ENSP00000486669; ENSG00000281614. [Q92835-2]
ENST00000630854; ENSP00000487191; ENSG00000281614. [Q92835-1]
GeneIDi3635.
KEGGihsa:3635.
UCSCiuc032ovq.2. human. [Q92835-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98429 mRNA. Translation: CAA67071.1.
U57650 mRNA. Translation: AAB53573.1.
U50040 mRNA. Translation: AAC50453.1.
U50041 mRNA. Translation: AAC50454.1. Different initiation.
U84400 mRNA. Translation: AAB49680.1.
U53470 mRNA. Translation: AAD00081.1.
BC062985 mRNA. Translation: AAH62985.1.
BC099920 mRNA. Translation: AAH99920.1.
BC113580 mRNA. Translation: AAI13581.1.
BC113582 mRNA. Translation: AAI13583.1.
CCDSiCCDS74672.1. [Q92835-1]
CCDS77543.1. [Q92835-2]
PIRiJC4889.
RefSeqiNP_001017915.1. NM_001017915.2. [Q92835-1]
NP_005532.2. NM_005541.4. [Q92835-2]
UniGeneiHs.262886.
Hs.601911.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YSXNMR-A1-112[»]
ProteinModelPortaliQ92835.
SMRiQ92835.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109847. 40 interactors.
IntActiQ92835. 26 interactors.
MINTiMINT-123561.
STRINGi9606.ENSP00000352575.

Chemistry databases

ChEMBLiCHEMBL1781870.
SwissLipidsiSLP:000000951.

PTM databases

DEPODiQ92835.
iPTMnetiQ92835.
PhosphoSitePlusiQ92835.

Polymorphism and mutation databases

BioMutaiINPP5D.
DMDMi158564077.

Proteomic databases

EPDiQ92835.
MaxQBiQ92835.
PaxDbiQ92835.
PeptideAtlasiQ92835.
PRIDEiQ92835.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359570; ENSP00000352575; ENSG00000168918. [Q92835-2]
ENST00000445964; ENSP00000405338; ENSG00000168918. [Q92835-1]
ENST00000629761; ENSP00000486669; ENSG00000281614. [Q92835-2]
ENST00000630854; ENSP00000487191; ENSG00000281614. [Q92835-1]
GeneIDi3635.
KEGGihsa:3635.
UCSCiuc032ovq.2. human. [Q92835-1]

Organism-specific databases

CTDi3635.
DisGeNETi3635.
GeneCardsiINPP5D.
H-InvDBHIX0057065.
HGNCiHGNC:6079. INPP5D.
HPAiCAB016300.
HPA070455.
MIMi601582. gene.
neXtProtiNX_Q92835.
OpenTargetsiENSG00000168918.
ENSG00000281614.
PharmGKBiPA29887.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0565. Eukaryota.
COG5411. LUCA.
GeneTreeiENSGT00760000119075.
HOVERGENiHBG106726.
InParanoidiQ92835.
KOiK03084.
OMAiLTKPEMF.
OrthoDBiEOG091G00P6.
PhylomeDBiQ92835.
TreeFamiTF323475.

Enzyme and pathway databases

BioCyciMetaCyc:HS09849-MONOMER.
ZFISH:HS09849-MONOMER.
BRENDAi3.1.3.86. 2681.
ReactomeiR-HSA-1660499. Synthesis of PIPs at the plasma membrane.
R-HSA-1855204. Synthesis of IP3 and IP4 in the cytosol.
R-HSA-202424. Downstream TCR signaling.
R-HSA-210990. PECAM1 interactions.
R-HSA-912526. Interleukin receptor SHC signaling.
SignaLinkiQ92835.
SIGNORiQ92835.

Miscellaneous databases

ChiTaRSiINPP5D. human.
EvolutionaryTraceiQ92835.
GeneWikiiINPP5D.
GenomeRNAii3635.
PROiQ92835.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000168918.
CleanExiHS_INPP5D.
ExpressionAtlasiQ92835. baseline and differential.
GenevisibleiQ92835. HS.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
IPR000980. SH2.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
SMARTiSM00128. IPPc. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSHIP1_HUMAN
AccessioniPrimary (citable) accession number: Q92835
Secondary accession number(s): O00145
, Q13544, Q13545, Q6P5A4, Q92656, Q9UE80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: November 2, 2016
This is version 138 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

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.