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Q15027

- ACAP1_HUMAN

UniProt

Q15027 - ACAP1_HUMAN

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Protein

Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1

Gene

ACAP1

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

Functioni

GTPase-activating protein (GAP) for ADP ribosylation factor 6 (ARF6) required for clathrin-dependent export of proteins from recycling endosomes to trans-Golgi network and cell surface. Required for regulated export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration.5 Publications

Enzyme regulationi

GAP activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidic acid.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri420 – 44324C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ARF GTPase activator activity Source: InterPro
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
  2. regulation of ARF GTPase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ15027.

Names & Taxonomyi

Protein namesi
Recommended name:
Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1
Alternative name(s):
Centaurin-beta-1
Short name:
Cnt-b1
Gene namesi
Name:ACAP1
Synonyms:CENTB1, KIAA0050
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:16467. ACAP1.

Subcellular locationi

Recycling endosome membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

GO - Cellular componenti

  1. endosome Source: UniProtKB-KW
  2. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141S → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi29 – 291S → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi274 – 2741K → N: Loss of binding to PIP2 and PIP3. Loss of association with endosomal tubules when coexpressed with PIP5K1C. 1 Publication
Mutagenesisi277 – 2771S → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi289 – 2891T → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi358 – 3581S → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi389 – 3891T → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi448 – 4481R → Q: Loss of GAP activity. No effect on GULP1 binding or association with endosomal tubules when coexpressed with PIP5K1C. 2 Publications
Mutagenesisi461 – 4611T → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi554 – 5541S → A: Loss of phosphorylation by PKB, interaction with ITGB1 and ITGB1-dependent cell migration. 2 Publications
Mutagenesisi554 – 5541S → D: Enhances interaction with ITGB1. 2 Publications
Mutagenesisi568 – 5681S → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi711 – 7111T → A: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi712 – 7121Y → F: No effect on interaction with ITGB1. 1 Publication
Mutagenesisi724 – 7241S → A: Loss of phosphorylation at S-554, interaction with ITGB1 and ITGB1-dependent cell migration. 1 Publication
Mutagenesisi724 – 7241S → D: Enhances interaction with ITGB1. 1 Publication

Organism-specific databases

PharmGKBiPA26406.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 740740Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1PRO_0000074209Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei485 – 4851Nitrated tyrosine1 Publication
Modified residuei554 – 5541Phosphoserine; by PKB1 Publication

Post-translational modificationi

Phosphorylation at Ser-554 by PKB is required for interaction with ITGB1, export of ITGB1 from recycling endosomes to the cell surface and ITGB1-dependent cell migration.1 Publication

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

MaxQBiQ15027.
PaxDbiQ15027.
PRIDEiQ15027.

PTM databases

PhosphoSiteiQ15027.

Expressioni

Tissue specificityi

Highest level in lung and spleen. Low level in heart, kidney, liver and pancreas.1 Publication

Gene expression databases

BgeeiQ15027.
CleanExiHS_ACAP1.
ExpressionAtlasiQ15027. baseline and differential.
GenevestigatoriQ15027.

Organism-specific databases

HPAiHPA021127.

Interactioni

Subunit structurei

Interacts with GTP-bound ARF6. Interacts with third cytoplasmic loop of SLC2A4/GLUT4. Interacts with CLTC. Interacts with GULP1. Forms a complex with GDP-bound ARF6 and GULP1. Interacts with ITGB1; required for ITGB1 recycling.5 Publications

Protein-protein interaction databases

BioGridi115092. 3 interactions.
IntActiQ15027. 6 interactions.
MINTiMINT-1446333.
STRINGi9606.ENSP00000158762.

Structurei

Secondary structure

1
740
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi407 – 4126
Turni415 – 4184
Turni421 – 4233
Beta strandi430 – 4323
Turni433 – 4364
Beta strandi437 – 4393
Helixi441 – 45010
Turni452 – 4543
Beta strandi457 – 4593
Turni460 – 4623
Helixi467 – 4759
Helixi478 – 4858
Turni486 – 4938
Helixi503 – 51412
Helixi571 – 5788
Beta strandi580 – 5823
Helixi585 – 5939
Turni603 – 6064
Helixi610 – 6167
Helixi620 – 6289
Helixi643 – 6508
Helixi653 – 6619
Helixi676 – 6827
Helixi686 – 69611
Helixi713 – 7208

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JUEX-ray2.30A/B378-740[»]
3T9KX-ray2.30A/B378-740[»]
4F1PX-ray2.30A/B378-740[»]
ProteinModelPortaliQ15027.
SMRiQ15027. Positions 4-357, 405-723.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15027.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 226226BARAdd
BLAST
Domaini265 – 36096PHPROSITE-ProRule annotationAdd
BLAST
Domaini405 – 527123Arf-GAPPROSITE-ProRule annotationAdd
BLAST
Repeati606 – 63530ANK 1Add
BLAST
Repeati639 – 66830ANK 2Add
BLAST
Repeati672 – 70231ANK 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 382382Required for formation of endosomal tubules when overexpressed with PIP5K1CAdd
BLAST
Regioni405 – 740336Required for interaction with GULP1Add
BLAST
Regioni525 – 56642Prevents interaction with ITGB1 when S-554 is not phosphorylatedAdd
BLAST

Domaini

PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate ACAP1-binding to PIP2 or PIP3 containing membranes.

Sequence similaritiesi

Contains 3 ANK repeats.PROSITE-ProRule annotation
Contains 1 Arf-GAP domain.PROSITE-ProRule annotation
Contains 1 BAR domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri420 – 44324C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

ANK repeat, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5347.
GeneTreeiENSGT00760000118874.
HOGENOMiHOG000220815.
HOVERGENiHBG050889.
InParanoidiQ15027.
KOiK12489.
OMAiFSQAHLD.
OrthoDBiEOG7PVWNT.
PhylomeDBiQ15027.
TreeFamiTF318315.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view]
PfamiPF00023. Ank. 2 hits.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSiPR00405. REVINTRACTNG.
SMARTiSM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15027 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVKLDFEEC LKDSPRFRAS IELVEAEVSE LETRLEKLLK LGTGLLESGR
60 70 80 90 100
HYLAASRAFV VGICDLARLG PPEPMMAECL EKFTVSLNHK LDSHAELLDA
110 120 130 140 150
TQHTLQQQIQ TLVKEGLRGF REARRDFWRG AESLEAALTH NAEVPRRRAQ
160 170 180 190 200
EAEEAGAALR TARAGYRGRA LDYALQINVI EDKRKFDIME FVLRLVEAQA
210 220 230 240 250
THFQQGHEEL SRLSQYRKEL GAQLHQLVLN SAREKRDMEQ RHVLLKQKEL
260 270 280 290 300
GGEEPEPSLR EGPGGLVMEG HLFKRASNAF KTWSRRWFTI QSNQLVYQKK
310 320 330 340 350
YKDPVTVVVD DLRLCTVKLC PDSERRFCFE VVSTSKSCLL QADSERLLQL
360 370 380 390 400
WVSAVQSSIA SAFSQARLDD SPRGPGQGSG HLAIGSAATL GSGGMARGRE
410 420 430 440 450
PGGVGHVVAQ VQSVDGNAQC CDCREPAPEW ASINLGVTLC IQCSGIHRSL
460 470 480 490 500
GVHFSKVRSL TLDSWEPELV KLMCELGNVI INQIYEARVE AMAVKKPGPS
510 520 530 540 550
CSRQEKEAWI HAKYVEKKFL TKLPEIRGRR GGRGRPRGQP PVPPKPSIRP
560 570 580 590 600
RPGSLRSKPE PPSEDLGSLH PGALLFRASG HPPSLPTMAD ALAHGADVNW
610 620 630 640 650
VNGGQDNATP LIQATAANSL LACEFLLQNG ANVNQADSAG RGPLHHATIL
660 670 680 690 700
GHTGLACLFL KRGADLGARD SEGRDPLTIA METANADIVT LLRLAKMREA
710 720 730 740
EAAQGQAGDE TYLDIFRDFS LMASDDPEKL SRRSHDLHTL
Length:740
Mass (Da):81,536
Last modified:November 1, 1996 - v1
Checksum:i64891DA3CE00189C
GO

Sequence cautioni

The sequence BAA06418.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681R → C.
Corresponds to variant rs35933585 [ dbSNP | Ensembl ].
VAR_048328
Natural varianti114 – 1141K → R in a breast cancer sample; somatic mutation. 1 Publication
VAR_036178
Natural varianti129 – 1291R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036179
Natural varianti533 – 5331R → W.
Corresponds to variant rs35019942 [ dbSNP | Ensembl ].
VAR_048329

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D30758 mRNA. Translation: BAA06418.2. Different initiation.
BT009788 mRNA. Translation: AAP88790.1.
BC018543 mRNA. Translation: AAH18543.1.
CCDSiCCDS11101.1.
RefSeqiNP_055531.1. NM_014716.3.
UniGeneiHs.337242.

Genome annotation databases

EnsembliENST00000158762; ENSP00000158762; ENSG00000072818.
GeneIDi9744.
KEGGihsa:9744.
UCSCiuc002ggd.2. human.

Polymorphism databases

DMDMi3183210.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D30758 mRNA. Translation: BAA06418.2 . Different initiation.
BT009788 mRNA. Translation: AAP88790.1 .
BC018543 mRNA. Translation: AAH18543.1 .
CCDSi CCDS11101.1.
RefSeqi NP_055531.1. NM_014716.3.
UniGenei Hs.337242.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3JUE X-ray 2.30 A/B 378-740 [» ]
3T9K X-ray 2.30 A/B 378-740 [» ]
4F1P X-ray 2.30 A/B 378-740 [» ]
ProteinModelPortali Q15027.
SMRi Q15027. Positions 4-357, 405-723.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115092. 3 interactions.
IntActi Q15027. 6 interactions.
MINTi MINT-1446333.
STRINGi 9606.ENSP00000158762.

PTM databases

PhosphoSitei Q15027.

Polymorphism databases

DMDMi 3183210.

Proteomic databases

MaxQBi Q15027.
PaxDbi Q15027.
PRIDEi Q15027.

Protocols and materials databases

DNASUi 9744.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000158762 ; ENSP00000158762 ; ENSG00000072818 .
GeneIDi 9744.
KEGGi hsa:9744.
UCSCi uc002ggd.2. human.

Organism-specific databases

CTDi 9744.
GeneCardsi GC17P007239.
HGNCi HGNC:16467. ACAP1.
HPAi HPA021127.
MIMi 607763. gene.
neXtProti NX_Q15027.
PharmGKBi PA26406.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5347.
GeneTreei ENSGT00760000118874.
HOGENOMi HOG000220815.
HOVERGENi HBG050889.
InParanoidi Q15027.
KOi K12489.
OMAi FSQAHLD.
OrthoDBi EOG7PVWNT.
PhylomeDBi Q15027.
TreeFami TF318315.

Enzyme and pathway databases

SignaLinki Q15027.

Miscellaneous databases

EvolutionaryTracei Q15027.
GeneWikii CENTB1.
GenomeRNAii 9744.
NextBioi 36666.
PROi Q15027.
SOURCEi Search...

Gene expression databases

Bgeei Q15027.
CleanExi HS_ACAP1.
ExpressionAtlasi Q15027. baseline and differential.
Genevestigatori Q15027.

Family and domain databases

Gene3Di 1.20.1270.60. 1 hit.
1.25.40.20. 1 hit.
2.30.29.30. 1 hit.
InterProi IPR027267. AH/BAR-dom.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR001164. ArfGAP.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view ]
Pfami PF00023. Ank. 2 hits.
PF01412. ArfGap. 1 hit.
PF00169. PH. 1 hit.
[Graphical view ]
PRINTSi PR00405. REVINTRACTNG.
SMARTi SM00248. ANK. 3 hits.
SM00105. ArfGap. 1 hit.
SM00233. PH. 1 hit.
[Graphical view ]
SUPFAMi SSF48403. SSF48403. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50115. ARFGAP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1."
    Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.
    DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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].
    Tissue: Lymph.
  4. "ACAPs are arf6 GTPase-activating proteins that function in the cell periphery."
    Jackson T.R., Brown F.D., Nie Z., Miura K., Foroni L., Sun J., Hsu V.W., Donaldson J.G., Randazzo P.A.
    J. Cell Biol. 151:627-638(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-448.
  5. "Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin beta1 to control cell migration."
    Li J., Ballif B.A., Powelka A.M., Dai J., Gygi S.P., Hsu V.W.
    Dev. Cell 9:663-673(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-554, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ITGB1, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-14; SER-29; SER-277; THR-289; SER-358; THR-389; THR-461; SER-554; SER-568; THR-711; TYR-712 AND SER-724.
  6. "Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry."
    Zhan X., Desiderio D.M.
    Anal. Biochem. 354:279-289(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary adenoma.
  7. "Cooperation of phosphoinositides and BAR domain proteins in endosomal tubulation."
    Shinozaki-Narikawa N., Kodama T., Shibasaki Y.
    Traffic 7:1539-1550(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHOSPHOLIPIDS, MUTAGENESIS OF LYS-274.
  8. "Regulation of Arf6 and ACAP1 signaling by the PTB-domain-containing adaptor protein GULP."
    Ma Z., Nie Z., Luo R., Casanova J.E., Ravichandran K.S.
    Curr. Biol. 17:722-727(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GULP AND ARF6, MUTAGENESIS OF ARG-448.
  9. "An ACAP1-containing clathrin coat complex for endocytic recycling."
    Li J., Peters P.J., Bai M., Dai J., Bos E., Kirchhausen T., Kandror K.V., Hsu V.W.
    J. Cell Biol. 178:453-464(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CLTC.
  10. "Mechanistic insights into regulated cargo binding by ACAP1 protein."
    Bai M., Pang X., Lou J., Zhou Q., Zhang K., Ma J., Li J., Sun F., Hsu V.W.
    J. Biol. Chem. 287:28675-28685(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 378-740 WILD TYPE AND MUTANT ASP-554 IN COMPLEX WITH ITGB1 PEPTIDE AND ZINC IONS, FUNCTION, INTERACTION WITH ITGB1, MUTAGENESIS OF SER-554.
  11. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-114 AND GLN-129.

Entry informationi

Entry nameiACAP1_HUMAN
AccessioniPrimary (citable) accession number: Q15027
Secondary accession number(s): Q53XN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 141 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

Miscellaneous

Cells overexpressing ACAP1 show an accumulation of ITGB1 in recycling endosomes and inhibition of stimulation-dependent cell migration. Cells with reduced levels of ACAP1 or AKT1 and AKT2 show inhibition of stimulation-dependent cell migration. Cells overexpressing ACAP1 and PIP5K1C show formation of tubular structures derived from endosomal membranes.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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

External Data

Dasty 3