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Q5VWQ8

- DAB2P_HUMAN

UniProt

Q5VWQ8 - DAB2P_HUMAN

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Protein

Disabled homolog 2-interacting protein

Gene

DAB2IP

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

Functioni

Functions as a scaffold protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Involved in several processes such as innate immune response, inflammation and cell growth inhibition, apoptosis, cell survival, angiogenesis, cell migration and maturation. Plays also a role in cell cycle checkpoint control; reduces G1 phase cyclin levels resulting in G0/G1 cell cycle arrest. Mediates signal transduction by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF), interferon (IFN) or lipopolysaccharide (LPS). Modulates the balance between phosphatidylinositol 3-kinase (PI3K)-AKT-mediated cell survival and apoptosis stimulated kinase (MAP3K5)-JNK signaling pathways; sequesters both AKT1 and MAP3K5 and counterbalances the activity of each kinase by modulating their phosphorylation status in response to proinflammatory stimuli. Acts as a regulator of the endoplasmic reticulum (ER) unfolded protein response (UPR) pathway; specifically involved in transduction of the ER stress-response to the JNK cascade through ERN1. Mediates TNF-alpha-induced apoptosis activation by facilitating dissociation of inhibitor 14-3-3 from MAP3K5; recruits the PP2A phosphatase complex which dephosphorylates MAP3K5 on 'Ser-966', leading to the dissociation of 13-3-3 proteins and activation of the MAP3K5-JNK signaling pathway in endothelial cells. Mediates also TNF/TRAF2-induced MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling. Acts a negative regulator in the IFN-gamma-mediated JAK-STAT signaling cascade by inhibiting smooth muscle cell (VSMCs) proliferation and intimal expansion, and thus, prevents graft arteriosclerosis (GA). Acts as a GTPase-activating protein (GAP) for the ADP ribosylation factor 6 (ARF6) and Ras. Promotes hydrolysis of the ARF6-bound GTP and thus, negatively regulates phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent TLR4-TIRAP-MyD88 and NF-kappa-B signaling pathways in endothelial cells in response to lipopolysaccharides (LPS). Binds specifically to phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 3-phosphate (PtdIns3P). In response to vascular endothelial growth factor (VEGFA), acts as a negative regulator of the VEGFR2-PI3K-mediated angiogenic signaling pathway by inhibiting endothelial cell migration and tube formation. In the developing brain, promotes both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex in a glial-dependent locomotion process. Probable downstream effector of the Reelin signaling pathway; promotes Purkinje cell (PC) dendrites development and formation of cerebellar synapses. Functions also as a tumor suppressor protein in prostate cancer progression; prevents cell proliferation and epithelial-to-mesenchymal transition (EMT) through activation of the glycogen synthase kinase-3 beta (GSK3B)-induced beta-catenin and inhibition of PI3K-AKT and Ras-MAPK survival downstream signaling cascades, respectively.10 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei172 – 1732Breakpoint for translocation to form KMT2A/MLL1-DAB2IP

GO - Molecular functioni

  1. 14-3-3 protein binding Source: BHF-UCL
  2. death receptor binding Source: BHF-UCL
  3. identical protein binding Source: IntAct
  4. kinase binding Source: UniProtKB
  5. mitogen-activated protein kinase kinase binding Source: UniProtKB
  6. mitogen-activated protein kinase kinase kinase binding Source: BHF-UCL
  7. phosphatidylinositol 3-kinase binding Source: UniProtKB
  8. phosphatidylinositol 3-kinase regulatory subunit binding Source: UniProtKB
  9. phosphatidylinositol-3-phosphate binding Source: UniProtKB
  10. phosphatidylinositol-4-phosphate binding Source: UniProtKB
  11. protein complex binding Source: UniProtKB
  12. protein homodimerization activity Source: BHF-UCL
  13. protein kinase binding Source: BHF-UCL
  14. protein phosphatase 2A binding Source: BHF-UCL
  15. Ras GTPase activator activity Source: BHF-UCL
  16. SH3 domain binding Source: UniProtKB
  17. signaling adaptor activity Source: BHF-UCL
  18. vascular endothelial growth factor receptor 2 binding Source: UniProtKB

GO - Biological processi

  1. activation of JUN kinase activity Source: BHF-UCL
  2. activation of MAPKKK activity Source: UniProtKB
  3. angiogenesis Source: UniProtKB-KW
  4. cell cycle Source: UniProtKB-KW
  5. cell motility involved in cerebral cortex radial glia guided migration Source: UniProtKB
  6. cellular protein catabolic process Source: UniProtKB
  7. cellular response to epidermal growth factor stimulus Source: BHF-UCL
  8. cellular response to interleukin-1 Source: UniProtKB
  9. cellular response to lipopolysaccharide Source: UniProtKB
  10. cellular response to tumor necrosis factor Source: UniProtKB
  11. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  12. endothelial cell apoptotic process Source: BHF-UCL
  13. extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  14. I-kappaB phosphorylation Source: UniProtKB
  15. inflammatory response Source: UniProtKB-KW
  16. innate immune response Source: UniProtKB-KW
  17. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: BHF-UCL
  18. layer formation in cerebral cortex Source: UniProtKB
  19. negative regulation of angiogenesis Source: UniProtKB
  20. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
  21. negative regulation of catenin import into nucleus Source: BHF-UCL
  22. negative regulation of cell growth Source: Ensembl
  23. negative regulation of cell proliferation Source: UniProtKB
  24. negative regulation of cyclin catabolic process Source: UniProtKB
  25. negative regulation of endothelial cell migration Source: UniProtKB
  26. negative regulation of epidermal growth factor receptor signaling pathway Source: BHF-UCL
  27. negative regulation of epithelial cell migration Source: UniProtKB
  28. negative regulation of epithelial cell proliferation Source: BHF-UCL
  29. negative regulation of epithelial to mesenchymal transition Source: UniProtKB
  30. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  31. negative regulation of fibroblast proliferation Source: BHF-UCL
  32. negative regulation of G0 to G1 transition Source: UniProtKB
  33. negative regulation of GTPase activity Source: UniProtKB
  34. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  35. negative regulation of MAP kinase activity Source: BHF-UCL
  36. negative regulation of NF-kappaB transcription factor activity Source: BHF-UCL
  37. negative regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  38. negative regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  39. negative regulation of protein phosphorylation Source: UniProtKB
  40. negative regulation of protein serine/threonine kinase activity Source: UniProtKB
  41. negative regulation of Ras GTPase activity Source: BHF-UCL
  42. negative regulation of Ras protein signal transduction Source: BHF-UCL
  43. negative regulation of toll-like receptor 4 signaling pathway Source: UniProtKB
  44. negative regulation of transcription, DNA-templated Source: UniProtKB
  45. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  46. negative regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
  47. negative regulation of vascular endothelial growth factor signaling pathway Source: UniProtKB
  48. neuron projection morphogenesis Source: UniProtKB
  49. positive regulation of apoptotic process Source: UniProtKB
  50. positive regulation of apoptotic signaling pathway Source: UniProtKB
  51. positive regulation of cell cycle arrest Source: UniProtKB
  52. positive regulation of dendrite development Source: UniProtKB
  53. positive regulation of JNK cascade Source: UniProtKB
  54. positive regulation of JUN kinase activity Source: BHF-UCL
  55. positive regulation of MAPK cascade Source: UniProtKB
  56. positive regulation of neuron migration Source: UniProtKB
  57. positive regulation of neuron projection development Source: UniProtKB
  58. positive regulation of proteasomal protein catabolic process Source: UniProtKB
  59. positive regulation of protein catabolic process Source: UniProtKB
  60. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  61. positive regulation of Ras GTPase activity Source: RefGenome
  62. positive regulation of synapse maturation Source: UniProtKB
  63. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  64. regulation of ARF GTPase activity Source: UniProtKB
  65. regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  66. regulation of p38MAPK cascade Source: UniProtKB
  67. regulation of protein complex assembly Source: UniProtKB
  68. response to unfolded protein Source: UniProtKB-KW
  69. transformed cell apoptotic process Source: BHF-UCL
  70. tube formation Source: UniProtKB
  71. vascular endothelial growth factor receptor-2 signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, GTPase activation

Keywords - Biological processi

Angiogenesis, Apoptosis, Cell cycle, Growth regulation, Immunity, Inflammatory response, Innate immunity, Stress response, Unfolded protein response

Names & Taxonomyi

Protein namesi
Recommended name:
Disabled homolog 2-interacting protein
Short name:
DAB2 interaction protein
Short name:
DAB2-interacting protein
Alternative name(s):
ASK-interacting protein 1
Short name:
AIP-1
DOC-2/DAB-2 interactive protein
Gene namesi
Name:DAB2IP
Synonyms:AF9Q34, AIP1, KIAA1743
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:17294. DAB2IP.

Subcellular locationi

Cytoplasm. Cell membrane Curated; Peripheral membrane protein Curated. Membrane. Cell projectiondendrite By similarity
Note: Localized in soma and dendrites of Purkinje cells as well as in scattered cell bodies in the molecular layer of the cerebellum By similarity. Colocalizes with TIRAP at the plasma membrane. Colocalizes with ARF6 at the plasma membrane and endocytic vesicles. Translocates from the plasma membrane to the cytoplasm in response to TNF-alpha. Phosphatidylinositol 4-phosphate (PtdIns4P) binding is essential for plasma membrane localization.By similarity

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. cerebellar mossy fiber Source: UniProtKB
  3. climbing fiber Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. endocytic vesicle Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProt
  7. intrinsic component of the cytoplasmic side of the plasma membrane Source: RefGenome
  8. neuronal cell body Source: UniProtKB
  9. neuronal cell body membrane Source: UniProtKB
  10. parallel fiber Source: UniProtKB
  11. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving DAB2IP is found in a patient with acute myeloid leukemia (AML). Translocation t(9;11)(q34;q23) with KMT2A/MLL1. May give rise to a KMT2A/MLL1-DAB2IP fusion protein lacking the PH domain.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi228 – 2303KKK → AAA: Reduces interaction with KDR/VEGFR2. Does not inhibit interaction with MAP3K5. 2 Publications
Mutagenesisi281 – 2844KKKK → AAAA: Significantly reduces interaction with MAP3K5. Does not reduce interaction with KDR/VEGFR2. 2 Publications
Mutagenesisi413 – 4131R → L: Does not inhibit interaction with MAP3K5. Does not reduce GSK3B-induced beta-catenin transcription activity, TNF-alpha-induced apoptosis, ARF6-mediated TLR4-TIRAP-MyD88 signaling inhibition, Ras and NF-kappa-B activities and tumor development. Does not suppress tumor development; when associated with A-728. 4 Publications
Mutagenesisi728 – 7281S → A: Inhibits phosphorylation and TNF-alpha-induced MAP3K5 dephosphorylation. Reduces interaction with 14-3-3 proteins, AKT1, a regulatory p85 subunit, MAP3K5, RIPK1, TRAF2 and TNF-alpha-induced MAP3K5-JNK signaling and apoptosis. Reduces RAS activity. Does not reduce GSK3B-induced beta catenin-mediated transcription activity. Does not reduce NF-kappa-B activity, cell invasion, epithelial-to-mesenchymal transition (EMT) and tumor development. Does not suppress tumor development; when associated with R-413. 4 Publications
Mutagenesisi920 – 92910PPPPPPPPPP → AAAAAAAAAA: Reduces interaction with a regulatory p85 subunit of the PI3K complex. Inhibits MAP3K5 active form increase, AKT1 active form decrease, PI3K-p85 complex activity inhibition and TNF-induced apoptosis. 1 Publication
Mutagenesisi935 – 9351T → A: Does not reduce interaction with 14-3-3 proteins. 1 Publication

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA27133.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11891189Disabled homolog 2-interacting proteinPRO_0000252407Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei728 – 7281Phosphoserine; by MAP3K5 and RIPK12 Publications
Modified residuei978 – 9781Phosphoserine1 Publication

Post-translational modificationi

In response to TNF-alpha-induction, phosphorylated at Ser-728; phosphorylation leads to a conformational change, and thus, increases its association with 14-3-3 proteins, MAP3K5, RIPK1 and TRAF2 in endothelial cells; also stimulates regulatory p85 subunit sequestring and PI3K-p85 complex activity inhibition.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ5VWQ8.
PaxDbiQ5VWQ8.
PRIDEiQ5VWQ8.

PTM databases

PhosphoSiteiQ5VWQ8.

Expressioni

Tissue specificityi

Expressed in endothelial and vascular smooth muscle cells (VSMCs). Expressed in prostate epithelial but poorly in prostate cancer cells. Poorly expressed in medulloblastoma cells compared to cerebellar precursor proliferating progenitor cells (at protein level). Low expression in prostate. Down-regulated in prostate cancer.4 Publications

Inductioni

Down-regulated in prostate cancer and medulloblastoma.2 Publications

Gene expression databases

BgeeiQ5VWQ8.
CleanExiHS_DAB2IP.
ExpressionAtlasiQ5VWQ8. baseline and differential.
GenevestigatoriQ5VWQ8.

Organism-specific databases

HPAiHPA036977.

Interactioni

Subunit structurei

On plasma membrane, exists in an inactive form complexed with TNFR1; in response to TNF-alpha, dissociates from TNFR1 complex, tranlocates to cytoplasm and forms part of an intracellular signaling complex comprising TRADD, RALBP1, TRAF2 and MAP3K5. Interacts with DAB1. Interacts (via NPXY motif) with DAB2 (via PID domain). Interacts (via PH domain) with ERN1 By similarity. Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF-alpha; this complex formation promotes MAP3K5-JNK activation and subsequent apoptosis. Interacts (via N-terminal domain) with JAK2; the interaction occurs in a IFNG/IFN-gamma-dependent manner and inhibits JAK2 autophosphorylation activity. Interacts (via C2 domain) with GSK3B; the interaction stimulates GSK3B kinase activation. Interacts (via C2 domain) with PPP2CA. Interacts (via proline-rich motif) with a regulatory p85 subunit (via SH3 domain) of the PI3K complex; the interaction inhibits the PI3K-AKT complex activity in a TNF-alpha-dependent manner in prostate cancer (PCa) cells. Interacts with AKT1; the interaction is increased in a TNF-alpha-induced manner. Interacts (via C2 domain and active form preferentially) with KDR/VEGFR2 (tyrosine-phosphorylated active form preferentially); the interaction occurs at the late phase of VEGFA response and inhibits KDR/VEGFR2 activity. Interacts (via N-terminus C2 domain) with MAP3K5 ('Ser-966' dephosphorylated form preferentially); the interaction occurs in a TNF-alpha-induced manner. Interacts (via Ras-GAP domain) with the catalytic subunit of protein phosphatase PP2A; the interaction occurs in resting endothelial cells, is further enhanced by TNF-alpha stimulation and is required to bridge PP2A to MAP3K5. Interacts (via C-terminus PER domain) with TRAF2 (via zinc fingers); the interaction occurs in a TNF-alpha-dependent manner. Interacts with 14-3-3 proteins; the interaction occurs in a TNF-alpha-dependent manner. Interacts (via Ras-GAP domain) with RIPK1 (via kinase domain); the interaction occurs in a TNF-alpha-dependent manner.By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2871881,EBI-2871881
AXIN1O151692EBI-9543020,EBI-710484
GSK3BP498412EBI-9543020,EBI-373586
MAP3K5Q996832EBI-2871881,EBI-476263

Protein-protein interaction databases

BioGridi127478. 20 interactions.
DIPiDIP-41721N.
IntActiQ5VWQ8. 5 interactions.
MINTiMINT-268247.
STRINGi9606.ENSP00000259371.

Structurei

3D structure databases

ProteinModelPortaliQ5VWQ8.
SMRiQ5VWQ8. Positions 329-662.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini101 – 202102PHPROSITE-ProRule annotationAdd
BLAST
Domaini200 – 29596C2Add
BLAST
Domaini371 – 563193Ras-GAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni646 – 943298Necessary for interaction with AKT1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1026 – 1159134Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 5245Arg-richAdd
BLAST
Compositional biasi112 – 1176Poly-Ala
Compositional biasi867 – 8704Poly-Ala
Compositional biasi903 – 94846Pro-richAdd
BLAST

Domaini

The C2 and Ras-GAP domains constitutively bind to MAP3K5 and facilitate the release of 14-3-3 proteins from MAP3K5. The PH and Ras-GAP domains, but not the NPXY motif, are crucial for its cell membrane localization and neuronal migration function. The PH domain is necessary but not sufficient to activate the JNK signaling pathway through ERN1 By similarity. Exists in a closed inactive form by an intramolecular interaction between the N- and the C-terminal domains. The proline-rich motif is critical both for PI3K-AKT activity inhibition and MAP3K5 activation. The PH and C2 domains are necessary for the binding to phosphatidylinositol phosphate. The Ras-GAP domain is necessary for its tumor-suppressive function.By similarity

Sequence similaritiesi

Contains 1 C2 domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 Ras-GAP domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG245428.
GeneTreeiENSGT00760000119092.
HOVERGENiHBG006492.
InParanoidiQ5VWQ8.
OMAiEKGGQPT.
OrthoDBiEOG74XS5P.
PhylomeDBiQ5VWQ8.
TreeFamiTF105303.

Family and domain databases

Gene3Di1.10.506.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR021887. DUF3498.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001936. RasGAP.
IPR023152. RasGAP_CS.
IPR008936. Rho_GTPase_activation_prot.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF12004. DUF3498. 1 hit.
PF00616. RasGAP. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
[Graphical view]
SUPFAMiSSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 1 hit.
PROSITEiPS50003. PH_DOMAIN. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5VWQ8-1) [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
MSAGGSARKS TGRSSYYYRL LRRPRLQRQR SRSRSRTRPA RESPQERPGS
60 70 80 90 100
RRSLPGSLSE KSPSMEPSAA TPFRVTGFLS RRLKGSIKRT KSQPKLDRNH
110 120 130 140 150
SFRHILPGFR SAAAAAADNE RSHLMPRLKE SRSHESLLSP SSAVEALDLS
160 170 180 190 200
MEEEVVIKPV HSSILGQDYC FEVTTSSGSK CFSCRSAAER DKWMENLRRA
210 220 230 240 250
VHPNKDNSRR VEHILKLWVI EAKDLPAKKK YLCELCLDDV LYARTTGKLK
260 270 280 290 300
TDNVFWGEHF EFHNLPPLRT VTVHLYRETD KKKKKERNSY LGLVSLPAAS
310 320 330 340 350
VAGRQFVEKW YPVVTPNPKG GKGPGPMIRI KARYQTITIL PMEMYKEFAE
360 370 380 390 400
HITNHYLGLC AALEPILSAK TKEEMASALV HILQSTGKVK DFLTDLMMSE
410 420 430 440 450
VDRCGDNEHL IFRENTLATK AIEEYLKLVG QKYLQDALGE FIKALYESDE
460 470 480 490 500
NCEVDPSKCS AADLPEHQGN LKMCCELAFC KIINSYCVFP RELKEVFASW
510 520 530 540 550
RQECSSRGRP DISERLISAS LFLRFLCPAI MSPSLFNLLQ EYPDDRTART
560 570 580 590 600
LTLIAKVTQN LANFAKFGSK EEYMSFMNQF LEHEWTNMQR FLLEISNPET
610 620 630 640 650
LSNTAGFEGY IDLGRELSSL HSLLWEAVSQ LEQSIVSKLG PLPRILRDVH
660 670 680 690 700
TALSTPGSGQ LPGTNDLAST PGSGSSSISA GLQKMVIEND LSGLIDFTRL
710 720 730 740 750
PSPTPENKDL FFVTRSSGVQ PSPARSSSYS EANEPDLQMA NGGKSLSMVD
760 770 780 790 800
LQDARTLDGE AGSPAGPDVL PTDGQAAAAQ LVAGWPARAT PVNLAGLATV
810 820 830 840 850
RRAGQTPTTP GTSEGAPGRP QLLAPLSFQN PVYQMAAGLP LSPRGLGDSG
860 870 880 890 900
SEGHSSLSSH SNSEELAAAA KLGSFSTAAE ELARRPGELA RRQMSLTEKG
910 920 930 940 950
GQPTVPRQNS AGPQRRIDQP PPPPPPPPPA PRGRTPPNLL STLQYPRPSS
960 970 980 990 1000
GTLASASPDW VGPSTRLRQQ SSSSKGDSPE LKPRAVHKQG PSPVSPNALD
1010 1020 1030 1040 1050
RTAAWLLTMN AQLLEDEGLG PDPPHRDRLR SKDELSQAEK DLAVLQDKLR
1060 1070 1080 1090 1100
ISTKKLEEYE TLFKCQEETT QKLVLEYQAR LEEGEERLRR QQEDKDIQMK
1110 1120 1130 1140 1150
GIISRLMSVE EELKKDHAEM QAAVDSKQKI IDAQEKRIAS LDAANARLMS
1160 1170 1180
ALTQLKERYS MQARNGISPT NPTKLQITEN GEFRNSSNC

Note: Gene prediction based on EST data.

Length:1,189
Mass (Da):131,625
Last modified:October 17, 2006 - v2
Checksum:i7494FF05AACF3320
GO
Isoform 2 (identifier: Q5VWQ8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-124: Missing.

Show »
Length:1,065
Mass (Da):117,651
Checksum:i4787F41F02108AA3
GO
Isoform 3 (identifier: Q5VWQ8-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-193: Missing.
     1158-1189: RYSMQARNGISPTNPTKLQITENGEFRNSSNC → SMH

Show »
Length:967
Mass (Da):106,764
Checksum:iE69CEB1FB00A2219
GO
Isoform 4 (identifier: Q5VWQ8-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-124: Missing.
     1158-1189: RYSMQARNGISPTNPTKLQITENGEFRNSSNC → SMH

Show »
Length:1,036
Mass (Da):114,410
Checksum:i1B07D8D3B9DEA76A
GO
Isoform 5 (identifier: Q5VWQ8-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-41: SAGGSARKSTGRSSYYYRLLRRPRLQRQRSRSRSRTRPAR → EPDSLLDQDDSY
     1158-1189: RYSMQARNGISPTNPTKLQITENGEFRNSSNC → SMH

Note: Gene prediction based on EST data.

Show »
Length:1,132
Mass (Da):125,041
Checksum:i85C487CD98660B19
GO

Sequence cautioni

The sequence CAH72155.3 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti482 – 4821I → T in AAM00371. (PubMed:11944990)Curated
Sequence conflicti921 – 9211P → S in AAM00371. (PubMed:11944990)Curated
Sequence conflicti1091 – 10922QQ → HE in AAM00371. (PubMed:11944990)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591S → F.
Corresponds to variant rs7027492 [ dbSNP | Ensembl ].
VAR_056858

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 193193Missing in isoform 3. 1 PublicationVSP_020952Add
BLAST
Alternative sequencei1 – 124124Missing in isoform 2 and isoform 4. 3 PublicationsVSP_020953Add
BLAST
Alternative sequencei2 – 4140SAGGS…TRPAR → EPDSLLDQDDSY in isoform 5. CuratedVSP_047361Add
BLAST
Alternative sequencei1158 – 118932RYSMQ…NSSNC → SMH in isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_020954Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF367051 mRNA. Translation: AAM00371.1.
AY032952 mRNA. Translation: AAK50336.1.
AB051530 mRNA. Translation: BAB21834.2.
AL357936 Genomic DNA. No translation available.
AL365274 Genomic DNA. Translation: CAH72155.3. Sequence problems.
AL365274 Genomic DNA. Translation: CAQ10385.1.
AL365274 Genomic DNA. Translation: CAH72158.1.
CH471090 Genomic DNA. Translation: EAW87503.1.
CH471090 Genomic DNA. Translation: EAW87504.1.
BC146762 mRNA. Translation: AAI46763.1.
CCDSiCCDS6832.1. [Q5VWQ8-2]
CCDS6833.2. [Q5VWQ8-5]
RefSeqiNP_115941.2. NM_032552.3. [Q5VWQ8-5]
NP_619723.1. NM_138709.2. [Q5VWQ8-2]
XP_005251776.1. XM_005251719.2. [Q5VWQ8-1]
UniGeneiHs.522378.

Genome annotation databases

EnsembliENST00000259371; ENSP00000259371; ENSG00000136848. [Q5VWQ8-5]
ENST00000309989; ENSP00000310827; ENSG00000136848. [Q5VWQ8-2]
ENST00000408936; ENSP00000386183; ENSG00000136848. [Q5VWQ8-1]
GeneIDi153090.
KEGGihsa:153090.
UCSCiuc004bln.3. human.
uc004blo.3. human. [Q5VWQ8-1]

Polymorphism databases

DMDMi116247768.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF367051 mRNA. Translation: AAM00371.1 .
AY032952 mRNA. Translation: AAK50336.1 .
AB051530 mRNA. Translation: BAB21834.2 .
AL357936 Genomic DNA. No translation available.
AL365274 Genomic DNA. Translation: CAH72155.3 . Sequence problems.
AL365274 Genomic DNA. Translation: CAQ10385.1 .
AL365274 Genomic DNA. Translation: CAH72158.1 .
CH471090 Genomic DNA. Translation: EAW87503.1 .
CH471090 Genomic DNA. Translation: EAW87504.1 .
BC146762 mRNA. Translation: AAI46763.1 .
CCDSi CCDS6832.1. [Q5VWQ8-2 ]
CCDS6833.2. [Q5VWQ8-5 ]
RefSeqi NP_115941.2. NM_032552.3. [Q5VWQ8-5 ]
NP_619723.1. NM_138709.2. [Q5VWQ8-2 ]
XP_005251776.1. XM_005251719.2. [Q5VWQ8-1 ]
UniGenei Hs.522378.

3D structure databases

ProteinModelPortali Q5VWQ8.
SMRi Q5VWQ8. Positions 329-662.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127478. 20 interactions.
DIPi DIP-41721N.
IntActi Q5VWQ8. 5 interactions.
MINTi MINT-268247.
STRINGi 9606.ENSP00000259371.

PTM databases

PhosphoSitei Q5VWQ8.

Polymorphism databases

DMDMi 116247768.

Proteomic databases

MaxQBi Q5VWQ8.
PaxDbi Q5VWQ8.
PRIDEi Q5VWQ8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000259371 ; ENSP00000259371 ; ENSG00000136848 . [Q5VWQ8-5 ]
ENST00000309989 ; ENSP00000310827 ; ENSG00000136848 . [Q5VWQ8-2 ]
ENST00000408936 ; ENSP00000386183 ; ENSG00000136848 . [Q5VWQ8-1 ]
GeneIDi 153090.
KEGGi hsa:153090.
UCSCi uc004bln.3. human.
uc004blo.3. human. [Q5VWQ8-1 ]

Organism-specific databases

CTDi 153090.
GeneCardsi GC09P124329.
HGNCi HGNC:17294. DAB2IP.
HPAi HPA036977.
MIMi 609205. gene.
neXtProti NX_Q5VWQ8.
PharmGKBi PA27133.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG245428.
GeneTreei ENSGT00760000119092.
HOVERGENi HBG006492.
InParanoidi Q5VWQ8.
OMAi EKGGQPT.
OrthoDBi EOG74XS5P.
PhylomeDBi Q5VWQ8.
TreeFami TF105303.

Miscellaneous databases

ChiTaRSi DAB2IP. human.
GeneWikii DAB2IP.
GenomeRNAii 153090.
NextBioi 87071.
PROi Q5VWQ8.
SOURCEi Search...

Gene expression databases

Bgeei Q5VWQ8.
CleanExi HS_DAB2IP.
ExpressionAtlasi Q5VWQ8. baseline and differential.
Genevestigatori Q5VWQ8.

Family and domain databases

Gene3Di 1.10.506.10. 1 hit.
2.30.29.30. 1 hit.
2.60.40.150. 1 hit.
InterProi IPR000008. C2_dom.
IPR021887. DUF3498.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR001936. RasGAP.
IPR023152. RasGAP_CS.
IPR008936. Rho_GTPase_activation_prot.
[Graphical view ]
Pfami PF00168. C2. 1 hit.
PF12004. DUF3498. 1 hit.
PF00616. RasGAP. 1 hit.
[Graphical view ]
SMARTi SM00239. C2. 1 hit.
SM00233. PH. 1 hit.
SM00323. RasGAP. 1 hit.
[Graphical view ]
SUPFAMi SSF48350. SSF48350. 1 hit.
SSF49562. SSF49562. 1 hit.
PROSITEi PS50003. PH_DOMAIN. 1 hit.
PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Differential regulation of the human gene DAB2IP in normal and malignant prostatic epithelia: cloning and characterization."
    Chen H., Pong R.-C., Wang Z., Hsieh J.-T.
    Genomics 79:573-581(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
  2. "Identification of a novel RAS GTPase-activating protein (RASGAP) gene at 9q34 as an MLL fusion partner in a patient with de novo acute myeloid leukemia."
    von Bergh A.R.M., Wijers P.M., Groot A.J., van Zelderen-Bhola S., Falkenburg J.H.F., Kluin P.M., Schuuring E.
    Genes Chromosomes Cancer 39:324-334(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
  3. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Brain.
  4. "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.
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [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] (ISOFORM 4).
  8. "AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3."
    Zhang R., He X., Liu W., Lu M., Hsieh J.-T., Min W.
    J. Clin. Invest. 111:1933-1943(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAP3K5, MUTAGENESIS OF 228-LYS--LYS-230; 281-LYS--LYS-284 AND ARG-413.
  9. "AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation."
    Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.
    J. Biol. Chem. 279:44955-44965(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TNFR1; MAP3K5; TRADD; RALBP1 AND TRAF2.
  10. "Tumor necrosis factor alpha-induced desumoylation and cytoplasmic translocation of homeodomain-interacting protein kinase 1 are critical for apoptosis signal-regulating kinase 1-JNK/p38 activation."
    Li X., Zhang R., Luo D., Park S.-J., Wang Q., Kim Y., Min W.
    J. Biol. Chem. 280:15061-15070(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIPK1, SUBCELLULAR LOCATION.
  11. "RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation."
    Zhang H., Zhang H., Lin Y., Li J., Pober J.S., Min W.
    J. Biol. Chem. 282:14788-14796(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH 14-3-3 PROTEINS; MAP3K5; RIPK1 AND TRAF2, PHOSPHORYLATION AT SER-728, MUTAGENESIS OF SER-728 AND THR-935, TISSUE SPECIFICITY.
  12. "AIP1 recruits phosphatase PP2A to ASK1 in tumor necrosis factor-induced ASK1-JNK activation."
    Min W., Lin Y., Tang S., Yu L., Zhang H., Wan T., Luhn T., Fu H., Chen H.
    Circ. Res. 102:840-848(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF SER-728.
  13. "AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice."
    Zhang H., He Y., Dai S., Xu Z., Luo Y., Wan T., Luo D., Jones D., Tang S., Chen H., Sessa W.C., Min W.
    J. Clin. Invest. 118:3904-3916(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KDR AND P85 SUBUNIT OF PI3K, MUTAGENESIS OF 228-LYS--LYS-230 AND 281-LYS--LYS-284.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "DAB2IP coordinates both PI3K-Akt and ASK1 pathways for cell survival and apoptosis."
    Xie D., Gore C., Zhou J., Pong R.C., Zhang H., Yu L., Vessella R.L., Min W., Hsieh J.T.
    Proc. Natl. Acad. Sci. U.S.A. 106:19878-19883(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AKT1 AND P85 SUBUNIT OF PI3K, PHOSPHORYLATION AT SER-728, MUTAGENESIS OF ARG-413; SER-728 AND 920-PRO--PRO-929.
  16. "AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling."
    Wan T., Liu T., Zhang H., Tang S., Min W.
    J. Biol. Chem. 285:3750-3757(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHOSPHATIDYLINOSITOL, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-413.
  17. "An oncogene-tumor suppressor cascade drives metastatic prostate cancer by coordinately activating Ras and nuclear factor-kappaB."
    Min J., Zaslavsky A., Fedele G., McLaughlin S.K., Reczek E.E., De Raedt T., Guney I., Strochlic D.E., Macconaill L.E., Beroukhim R., Bronson R.T., Ryeom S., Hahn W.C., Loda M., Cichowski K.
    Nat. Med. 16:286-294(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROSTATE CANCER, INDUCTION, MUTAGENESIS OF ARG-413 AND SER-728.
  18. "Role of DAB2IP in modulating epithelial-to-mesenchymal transition and prostate cancer metastasis."
    Xie D., Gore C., Liu J., Pong R.C., Mason R., Hao G., Long M., Kabbani W., Yu L., Zhang H., Chen H., Sun X., Boothman D.A., Min W., Hsieh J.T.
    Proc. Natl. Acad. Sci. U.S.A. 107:2485-2490(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROSTATE CANCER, INTERACTION WITH GSK3B AND PPP2CA.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "AIP1 prevents graft arteriosclerosis by inhibiting interferon-gamma-dependent smooth muscle cell proliferation and intimal expansion."
    Yu L., Qin L., Zhang H., He Y., Chen H., Pober J.S., Tellides G., Min W.
    Circ. Res. 109:418-427(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH JAK2, TISSUE SPECIFICITY.
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-978, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "EZH2-regulated DAB2IP is a medulloblastoma tumor suppressor and a positive marker for survival."
    Smits M., van Rijn S., Hulleman E., Biesmans D., van Vuurden D.G., Kool M., Haberler C., Aronica E., Vandertop W.P., Noske D.P., Wurdinger T.
    Clin. Cancer Res. 18:4048-4058(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MEDULLOBLASTOMA DEVELOPMENT, INDUCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiDAB2P_HUMAN
AccessioniPrimary (citable) accession number: Q5VWQ8
Secondary accession number(s): A6H8V2
, A6NHI9, B0QZB1, G3XA90, Q8TDL2, Q96SE1, Q9C0C0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 104 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

Miscellaneous

The DAB2IP gene is found epigenetically silenced in numerous aggressive cancers, like prostate cancers and medulloblastoma tumors. Epigenetic suppression of DAB2IP by EZH2 is a major mechanism of DAB2IP inactivation in human prostate cancer and increases metastatic potential (PubMed:20154697, PubMed:22696229).2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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