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Q9Y613

- FHOD1_HUMAN

UniProt

Q9Y613 - FHOD1_HUMAN

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Protein

FH1/FH2 domain-containing protein 1

Gene

FHOD1

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

Functioni

Required for the assembly of F-actin structures, such as stress fibers. Depends on the Rho-ROCK cascade for its activity. Contributes to the coordination of microtubules with actin fibers and plays a role in cell elongation. Acts synergistically with ROCK1 to promote SRC-dependent non-apoptotic plasma membrane blebbing.3 Publications

GO - Molecular functioni

  1. identical protein binding Source: IntAct

GO - Biological processi

  1. positive regulation of stress fiber assembly Source: BHF-UCL
  2. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
FH1/FH2 domain-containing protein 1
Alternative name(s):
Formin homolog overexpressed in spleen 1
Short name:
FHOS
Formin homology 2 domain-containing protein 1
Gene namesi
Name:FHOD1
Synonyms:FHOS, FHOS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:17905. FHOD1.

Subcellular locationi

Cytoplasm. Cytoplasmcytoskeleton. Cell projectionbleb
Note: Predominantly cytoplasmic.

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. cytoplasm Source: HPA
  3. cytoskeleton Source: UniProtKB-KW
  4. membrane Source: UniProtKB
  5. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28143.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11641163FH1/FH2 domain-containing protein 1PRO_0000194905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei367 – 3671Phosphoserine2 Publications
Modified residuei486 – 4861Phosphoserine1 Publication
Modified residuei495 – 4951Phosphothreonine1 Publication
Modified residuei498 – 4981Phosphoserine2 Publications
Modified residuei523 – 5231Phosphoserine3 Publications
Modified residuei573 – 5731Phosphoserine1 Publication
Modified residuei690 – 6901Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated by ROCK1.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Y613.
PaxDbiQ9Y613.
PeptideAtlasiQ9Y613.
PRIDEiQ9Y613.

PTM databases

PhosphoSiteiQ9Y613.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in spleen.

Gene expression databases

BgeeiQ9Y613.
CleanExiHS_FHOD1.
ExpressionAtlasiQ9Y613. baseline and differential.
GenevestigatoriQ9Y613.

Organism-specific databases

HPAiHPA024468.

Interactioni

Subunit structurei

Self-associates via the FH2 domain. Binds to F-actin via its N-terminus. Binds to the cytoplasmic domain of CD21 via its C-terminus. Interacts with ROCK1 in a Src-dependent manner.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself8EBI-348433,EBI-348433

Protein-protein interaction databases

BioGridi118877. 24 interactions.
DIPiDIP-31134N.
IntActiQ9Y613. 13 interactions.
MINTiMINT-1033686.
STRINGi9606.ENSP00000258201.

Structurei

Secondary structure

1
1164
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 228Combined sources
Beta strandi36 – 394Combined sources
Beta strandi42 – 465Combined sources
Helixi51 – 533Combined sources
Helixi55 – 617Combined sources
Beta strandi68 – 758Combined sources
Turni76 – 783Combined sources
Turni88 – 936Combined sources
Helixi98 – 1003Combined sources
Helixi102 – 1043Combined sources
Beta strandi109 – 1146Combined sources
Helixi116 – 12914Combined sources
Helixi132 – 14716Combined sources
Helixi152 – 1587Combined sources
Helixi161 – 1699Combined sources
Helixi174 – 18714Combined sources
Helixi191 – 1999Combined sources
Helixi201 – 2099Combined sources
Helixi210 – 2123Combined sources
Helixi216 – 23217Combined sources
Helixi234 – 2363Combined sources
Helixi237 – 25115Combined sources
Helixi257 – 2637Combined sources
Turni264 – 2674Combined sources
Helixi271 – 28717Combined sources
Helixi291 – 30313Combined sources
Helixi306 – 3149Combined sources
Helixi321 – 33818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DADX-ray2.30A/B1-339[»]
DisProtiDP00448.
ProteinModelPortaliQ9Y613.
SMRiQ9Y613. Positions 14-339, 651-1013.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y613.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 458406GBD/FH3PROSITE-ProRule annotationAdd
BLAST
Domaini487 – 615129FH1Add
BLAST
Domaini616 – 1013398FH2PROSITE-ProRule annotationAdd
BLAST
Domaini1053 – 113381DADAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni612 – 807196Interaction with ROCK1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili884 – 92138Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi583 – 59311Poly-ProAdd
BLAST
Compositional biasi597 – 6059Poly-Pro
Compositional biasi996 – 10016Poly-Gln

Domaini

The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments.1 Publication

Sequence similaritiesi

Belongs to the formin homology family.Curated
Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG246341.
GeneTreeiENSGT00760000119258.
HOGENOMiHOG000015130.
HOVERGENiHBG051615.
InParanoidiQ9Y613.
OMAiPKLCIGD.
OrthoDBiEOG71G9T2.
PhylomeDBiQ9Y613.
TreeFamiTF316268.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
IPR015425. FH2_Formin.
IPR027647. FHDC1.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view]
PANTHERiPTHR23213:SF189. PTHR23213:SF189. 1 hit.
PfamiPF02181. FH2. 1 hit.
[Graphical view]
SMARTiSM00498. FH2. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y613-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGGEDRGDG EPVSVVTVRV QYLEDTDPFA CANFPEPRRA PTCSLDGALP
60 70 80 90 100
LGAQIPAVHR LLGAPLKLED CALQVSPSGY YLDTELSLEE QREMLEGFYE
110 120 130 140 150
EISKGRKPTL ILRTQLSVRV NAILEKLYSS SGPELRRSLF SLKQIFQEDK
160 170 180 190 200
DLVPEFVHSE GLSCLIRVGA AADHNYQSYI LRALGQLMLF VDGMLGVVAH
210 220 230 240 250
SDTIQWLYTL CASLSRLVVK TALKLLLVFV EYSENNAPLF IRAVNSVAST
260 270 280 290 300
TGAPPWANLV SILEEKNGAD PELLVYTVTL INKTLAALPD QDSFYDVTDA
310 320 330 340 350
LEQQGMEALV QRHLGTAGTD VDLRTQLVLY ENALKLEDGD IEEAPGAGGR
360 370 380 390 400
RERRKPSSEE GKRSRRSLEG GGCPARAPEP GPTGPASPVG PTSSTGPALL
410 420 430 440 450
TGPASSPVGP PSGLQASVNL FPTISVAPSA DTSSERSIYK ARFLENVAAA
460 470 480 490 500
ETEKQVALAQ GRAETLAGAM PNEAGGHPDA RQLWDSPETA PAARTPQSPA
510 520 530 540 550
PCVLLRAQRS LAPEPKEPLI PASPKAEPIW ELPTRAPRLS IGDLDFSDLG
560 570 580 590 600
EDEDQDMLNV ESVEAGKDIP APSPPLPLLS GVPPPPPLPP PPPIKGPFPP
610 620 630 640 650
PPPLPLAAPL PHSVPDSSAL PTKRKTVKLF WRELKLAGGH GVSASRFGPC
660 670 680 690 700
ATLWASLDPV SVDTARLEHL FESRAKEVLP SKKAGEGRRT MTTVLDPKRS
710 720 730 740 750
NAINIGLTTL PPVHVIKAAL LNFDEFAVSK DGIEKLLTMM PTEEERQKIE
760 770 780 790 800
EAQLANPDIP LGPAENFLMT LASIGGLAAR LQLWAFKLDY DSMEREIAEP
810 820 830 840 850
LFDLKVGMEQ LVQNATFRCI LATLLAVGNF LNGSQSSGFE LSYLEKVSEV
860 870 880 890 900
KDTVRRQSLL HHLCSLVLQT RPESSDLYSE IPALTRCAKV DFEQLTENLG
910 920 930 940 950
QLERRSRAAE ESLRSLAKHE LAPALRARLT HFLDQCARRV AMLRIVHRRV
960 970 980 990 1000
CNRFHAFLLY LGYTPQAARE VRIMQFCHTL REFALEYRTC RERVLQQQQK
1010 1020 1030 1040 1050
QATYRERNKT RGRMITETEK FSGVAGEAPS NPSVPVAVSS GPGRGDADSH
1060 1070 1080 1090 1100
ASMKSLLTSR PEDTTHNRRS RGMVQSSSPI MPTVGPSTAS PEEPPGSSLP
1110 1120 1130 1140 1150
SDTSDEIMDL LVQSVTKSSP RALAARERKR SRGNRKSLRR TLKSGLGDDL
1160
VQALGLSKGP GLEV
Length:1,164
Mass (Da):126,551
Last modified:January 23, 2007 - v3
Checksum:iE6C7AE1FB8DC3FC7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti249 – 2491S → T in AAD39906. (PubMed:10352228)Curated
Sequence conflicti249 – 2491S → T in AAO38757. (PubMed:15138285)Curated
Sequence conflicti264 – 2641E → D in AAO38757. (PubMed:15138285)Curated
Sequence conflicti277 – 2771T → M in BAD06250. (PubMed:14576350)Curated
Sequence conflicti307 – 3082EA → DT in AAD39906. (PubMed:10352228)Curated
Sequence conflicti307 – 3082EA → DT in AAO38757. (PubMed:15138285)Curated
Sequence conflicti359 – 3591E → D in AAO38757. (PubMed:15138285)Curated
Sequence conflicti387 – 3871S → T in AAO38757. (PubMed:15138285)Curated
Sequence conflicti533 – 5331P → L in BAD92821. 1 PublicationCurated
Sequence conflicti633 – 6342EL → DV in AAD39906. (PubMed:10352228)Curated
Sequence conflicti689 – 6891R → Q in AAO38757. (PubMed:15138285)Curated
Sequence conflicti700 – 7001S → T in AAD39906. (PubMed:10352228)Curated
Sequence conflicti745 – 7451E → G in AAO38757. (PubMed:15138285)Curated
Sequence conflicti751 – 7511E → G in AAD39906. (PubMed:10352228)Curated
Sequence conflicti849 – 8491E → D in AAD39906. (PubMed:10352228)Curated
Sequence conflicti1061 – 10611P → L in AAD39906. (PubMed:10352228)Curated
Sequence conflicti1061 – 10611P → L in AAO38757. (PubMed:15138285)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF113615 mRNA. Translation: AAD39906.1.
AB041046 mRNA. Translation: BAD06250.1.
AY192154 mRNA. Translation: AAO38757.1.
BC033084 mRNA. Translation: AAH33084.1.
AB209584 mRNA. Translation: BAD92821.1.
CCDSiCCDS10834.1.
RefSeqiNP_037373.2. NM_013241.2.
UniGeneiHs.95231.

Genome annotation databases

EnsembliENST00000258201; ENSP00000258201; ENSG00000135723.
GeneIDi29109.
KEGGihsa:29109.
UCSCiuc002esl.3. human.

Polymorphism databases

DMDMi62512187.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF113615 mRNA. Translation: AAD39906.1 .
AB041046 mRNA. Translation: BAD06250.1 .
AY192154 mRNA. Translation: AAO38757.1 .
BC033084 mRNA. Translation: AAH33084.1 .
AB209584 mRNA. Translation: BAD92821.1 .
CCDSi CCDS10834.1.
RefSeqi NP_037373.2. NM_013241.2.
UniGenei Hs.95231.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DAD X-ray 2.30 A/B 1-339 [» ]
DisProti DP00448.
ProteinModelPortali Q9Y613.
SMRi Q9Y613. Positions 14-339, 651-1013.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118877. 24 interactions.
DIPi DIP-31134N.
IntActi Q9Y613. 13 interactions.
MINTi MINT-1033686.
STRINGi 9606.ENSP00000258201.

PTM databases

PhosphoSitei Q9Y613.

Polymorphism databases

DMDMi 62512187.

Proteomic databases

MaxQBi Q9Y613.
PaxDbi Q9Y613.
PeptideAtlasi Q9Y613.
PRIDEi Q9Y613.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258201 ; ENSP00000258201 ; ENSG00000135723 .
GeneIDi 29109.
KEGGi hsa:29109.
UCSCi uc002esl.3. human.

Organism-specific databases

CTDi 29109.
GeneCardsi GC16M067263.
HGNCi HGNC:17905. FHOD1.
HPAi HPA024468.
MIMi 606881. gene.
neXtProti NX_Q9Y613.
PharmGKBi PA28143.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG246341.
GeneTreei ENSGT00760000119258.
HOGENOMi HOG000015130.
HOVERGENi HBG051615.
InParanoidi Q9Y613.
OMAi PKLCIGD.
OrthoDBi EOG71G9T2.
PhylomeDBi Q9Y613.
TreeFami TF316268.

Miscellaneous databases

EvolutionaryTracei Q9Y613.
GeneWikii FHOD1.
GenomeRNAii 29109.
NextBioi 52175.
PROi Q9Y613.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y613.
CleanExi HS_FHOD1.
ExpressionAtlasi Q9Y613. baseline and differential.
Genevestigatori Q9Y613.

Family and domain databases

InterProi IPR016024. ARM-type_fold.
IPR015425. FH2_Formin.
IPR027647. FHDC1.
IPR014768. GTPase-bd/formin_homology_3.
[Graphical view ]
PANTHERi PTHR23213:SF189. PTHR23213:SF189. 1 hit.
Pfami PF02181. FH2. 1 hit.
[Graphical view ]
SMARTi SM00498. FH2. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS51444. FH2. 1 hit.
PS51232. GBD_FH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a protein containing formin homology (FH1/FH2) domains."
    Westendorf J.J., Mernaugh R., Hiebert S.W.
    Gene 232:173-182(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Fhos, a mammalian formin, directly binds to F-actin via a region N-terminal to the FH1 domain and forms a homotypic complex via the FH2 domain to promote actin fiber formation."
    Takeya R., Sumimoto H.
    J. Cell Sci. 116:4567-4575(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT.
  3. "EBV attachment stimulates FHOS/FHOD1 redistribution and co-aggregation with CD21: formin interactions with the cytoplasmic domain of human CD21."
    Gill M.B., Roecklein-Canfield J., Sage D.R., Zambela-Soediono M., Longtine N., Uknis M., Fingeroth J.D.
    J. Cell Sci. 117:2709-2720(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
  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].
    Tissue: Prostate.
  5. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19.
    Tissue: Platelet.
  6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-1164.
    Tissue: Spleen.
  7. "FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation."
    Gasteier J.E., Schroeder S., Muranyi W., Madrid R., Benichou S., Fackler O.T.
    Exp. Cell Res. 306:192-202(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOINHIBITION, SUBCELLULAR LOCATION.
  8. "Biochemical characterization of the diaphanous autoregulatory interaction in the formin homology protein FHOD1."
    Schonichen A., Alexander M., Gasteier J.E., Cuesta F.E., Fackler O.T., Geyer M.
    J. Biol. Chem. 281:5084-5093(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN DAD, AUTOINHIBITION.
  9. "The diaphanous-related formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing."
    Hannemann S., Madrid R., Stastna J., Kitzing T., Gasteier J., Schoenichen A., Bouchet J., Jimenez A., Geyer M., Grosse R., Benichou S., Fackler O.T.
    J. Biol. Chem. 283:27891-27903(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ROCK1, PHOSPHORYLATION.
  10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; THR-495; SER-498 AND SER-523, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-486; SER-523 AND SER-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523 AND THR-690, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFHOD1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y613
Secondary accession number(s): Q59F76
, Q6Y1F2, Q76MS8, Q8N521
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 131 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3