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Q9NRY4 (RHG35_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho GTPase-activating protein 35
Alternative name(s):
Glucocorticoid receptor DNA-binding factor 1
Glucocorticoid receptor repression factor 1
Short name=GRF-1
Rho GAP p190A
Short name=p190-A
Gene names
Name:ARHGAP35
Synonyms:GRF1, GRLF1, KIAA1722
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1499 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'. May participate in the regulation of retinal development and degeneration. May transduce signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP). May also act as a tumor suppressor. Ref.5 Ref.6

Subunit structure

Interacts with RASA1. Interacts with the general transcription factor GTF2I, the interaction sequesters GTF2I in the cytoplasm. Ref.18

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Post-translational modification

Phosphorylation of Tyr-1105 by PTK6 promotes the association with RASA1, inactivating RHOA while activating RAS. Phosphorylation at Tyr-308 by PDGFRA inhibits binding to GTF2I.

Sequence similarities

Contains 4 FF domains.

Contains 1 Rho-GAP domain.

Sequence caution

The sequence AAA58618.1 differs from that shown. Reason: Frameshift at positions 389, 533, 540, 607, 614, 1167, 1241, 1292, 1334 and 1446.

The sequence AAF80386.1 differs from that shown. Reason: Frameshift at positions 533, 540, 607 and 614.

The sequence AAF80386.1 differs from that shown. Reason: Unlikely isoform. Aberrant splice sites.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DiseaseTumor suppressor
   DomainRepeat
   LigandDNA-binding
   Molecular functionGTPase activation
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

camera-type eye development

Inferred from electronic annotation. Source: Ensembl

forebrain development

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.6. Source: UniProtKB

negative regulation of vascular permeability

Inferred from electronic annotation. Source: Ensembl

neural tube closure

Inferred from electronic annotation. Source: Ensembl

positive regulation of Rho GTPase activity

Traceable author statement. Source: GOC

regulation of cell shape

Inferred from electronic annotation. Source: Ensembl

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement Ref.6. Source: ProtInc

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred by curator Ref.6. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement Ref.6. Source: ProtInc

GTP binding

Inferred from electronic annotation. Source: InterPro

Rho GTPase activator activity

Traceable author statement. Source: Reactome

transcription corepressor activity

Traceable author statement Ref.6. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14991499Rho GTPase-activating protein 35
PRO_0000056730

Regions

Domain270 – 32758FF 1
Domain368 – 42255FF 2
Domain429 – 48355FF 3
Domain485 – 55066FF 4
Domain1249 – 1436188Rho-GAP
Compositional bias1440 – 149051Pro-rich

Amino acid modifications

Modified residue3081Phosphotyrosine Ref.18
Modified residue5891Phosphoserine Ref.12 Ref.14 Ref.15 Ref.17
Modified residue7731Phosphoserine Ref.14
Modified residue9701Phosphoserine Ref.10 Ref.12
Modified residue9751Phosphoserine Ref.12 Ref.14
Modified residue10721Phosphoserine Ref.14
Modified residue10871Phosphotyrosine Ref.14
Modified residue11051Phosphotyrosine; by ABL2 and PTK6 Ref.9 Ref.14
Modified residue11341Phosphoserine Ref.14 Ref.17
Modified residue11501Phosphoserine Ref.12 Ref.17
Modified residue11791Phosphoserine Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.17

Experimental info

Sequence conflict2511R → P in AAF80386. Ref.5
Sequence conflict3091V → D in AAF80386. Ref.5
Sequence conflict3621S → G in AAF80386. Ref.5
Sequence conflict4141Q → A in AAF80386. Ref.5
Sequence conflict4141Q → A in AAA58618. Ref.6
Sequence conflict4741M → T in AAF80386. Ref.5
Sequence conflict4741M → T in AAA58618. Ref.6
Sequence conflict9781C → S in AAF80386. Ref.5
Sequence conflict12921M → I in AAF80386. Ref.5
Sequence conflict1452 – 14532PS → RN in AAA58618. Ref.6

Secondary structure

............................................................................................ 1499
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NRY4 [UniParc].

Last modified October 3, 2012. Version 3.
Checksum: 8CCB493414A7E3E6

FASTA1,499170,514
        10         20         30         40         50         60 
MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF HLDHTSVLST 

        70         80         90        100        110        120 
SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI DDQTFQPHRS TALQPYIKRA 

       130        140        150        160        170        180 
AATKLASAEK LMYFCTDQLG LEQDFEQKQM PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF 

       190        200        210        220        230        240 
VSNLYNQLAK TKKPIVVVLT KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF 

       250        260        270        280        290        300 
STLVQLIDKS RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWLSVSRKMQ 

       310        320        330        340        350        360 
ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA LIPNLDEIDH 

       370        380        390        400        410        420 
LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE RIPFDLMDTV PAEQLYEAHL 

       430        440        450        460        470        480 
EKLRNERKRV EMRRAFKENL ETSPFITPGK PWEEARSFIM NEDFYQWLEE SVYMDIYGKH 

       490        500        510        520        530        540 
QKQIIDKAKE EFQELLLEYS ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER 

       550        560        570        580        590        600 
DALILKHIHF VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDPNIDRINL 

       610        620        630        640        650        660 
VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS FQTPTFQPHG 

       670        680        690        700        710        720 
CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL ILVNKRGDTS GETLHSLIQQ 

       730        740        750        760        770        780 
GQQIASKLQC VFLDPASAGI GYGRNINEKQ ISQVLKGLLD SKRNLNLVSS TASIKDLADV 

       790        800        810        820        830        840 
DLRIVMCLMC GDPFSADDIL FPVLQSQTCK SSHCGSNNSV LLELPIGLHK KRIELSVLSY 

       850        860        870        880        890        900 
HSSFSIRKSR LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAVDVLDNDL 

       910        920        930        940        950        960 
SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LEIFHPFFKD VVEKKNIIEA THMYDNAAEA 

       970        980        990       1000       1010       1020 
CSTTEEVFNS PRAGSPLCNS NLQDSEEDIE PSYSLFREDT SLPSLSKDHS KLSMELEGND 

      1030       1040       1050       1060       1070       1080 
GLSFIMSNFE SKLNNKVPPP VKPKPPVHFE ITKGDLSYLD QGHRDGQRKS VSSSPWLPQD 

      1090       1100       1110       1120       1130       1140 
GFDPSDYAEP MDAVVKPRNE EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT 

      1150       1160       1170       1180       1190       1200 
SSLERGRKVS IVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG 

      1210       1220       1230       1240       1250       1260 
DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP LTTVVTPEKP 

      1270       1280       1290       1300       1310       1320 
IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD QDHNLDLAEK DFTVNTVAGA 

      1330       1340       1350       1360       1370       1380 
MKSFFSELPD PLVPYNMQID LVEAHKINDR EQKLHALKEV LKKFPKENHE VFKYVISHLN 

      1390       1400       1410       1420       1430       1440 
KVSHNNKVNL MTSENLSICF WPTLMRPDFS TMDALTATRT YQTIIELFIQ QCPFFFYNRP 

      1450       1460       1470       1480       1490 
ITEPPGARPS SPSAVASTVP FLTSTPVTSQ PSPPQSPPPT PQSPMQPLLP SQLQAEHTL 

« Hide

References

« Hide 'large scale' references
[1]"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].
Tissue: Brain.
[2]"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.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"p190-A, a human tumor suppressor gene, maps to the chromosomal region 19q13.3 that is reportedly deleted in some gliomas."
Tikoo A., Czekay S., Viars C., White S., Heath J.K., Arden K., Maruta H.
Gene 257:23-31(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1491.
Tissue: Mammary cancer.
[6]"Molecular cloning and characterization of a factor that binds the human glucocorticoid receptor gene and represses its expression."
LeClerc S., Palaniswami R., Xie B.X., Govindan M.V.
J. Biol. Chem. 266:17333-17340(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 377-1453, FUNCTION.
Tissue: Mammary cancer.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"Breast tumor kinase phosphorylates p190RhoGAP to regulate rho and ras and promote breast carcinoma growth, migration, and invasion."
Shen C.H., Chen H.Y., Lin M.S., Li F.Y., Chang C.C., Kuo M.L., Settleman J., Chen R.H.
Cancer Res. 68:7779-7787(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-1105.
[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-970 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-970; SER-975; SER-1150 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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].
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589; SER-773; SER-975; SER-1072; TYR-1087; TYR-1105; SER-1134 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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-589; SER-1134; SER-1150 AND SER-1179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"NMR structural studies on human p190-A RhoGAPFF1 revealed that domain phosphorylation by the PDGF-receptor alpha requires its previous unfolding."
Bonet R., Ruiz L., Aragon E., Martin-Malpartida P., Macias M.J.
J. Mol. Biol. 389:230-237(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 267-331, PHOSPHORYLATION AT TYR-308, INTERACTION WITH GTF2I.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB051509 mRNA. Translation: BAB21813.2.
CH471126 Genomic DNA. Translation: EAW57450.1.
BC150257 mRNA. Translation: AAI50258.1.
AF159851 mRNA. Translation: AAF80386.1. Sequence problems.
M73077 mRNA. Translation: AAA58618.1. Frameshift.
CCDSCCDS46127.1.
RefSeqNP_004482.4. NM_004491.4.
UniGeneHs.509447.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K85NMR-A267-331[»]
3C5HX-ray1.80A13-249[»]
3FK2X-ray2.80A/B/C/D1212-1439[»]
ProteinModelPortalQ9NRY4.
SMRQ9NRY4. Positions 13-249, 267-331, 1242-1437.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109166. 9 interactions.
IntActQ9NRY4. 1 interaction.
STRING9606.ENSP00000385720.

PTM databases

PhosphoSiteQ9NRY4.

Polymorphism databases

DMDM408360250.

Proteomic databases

MaxQBQ9NRY4.
PaxDbQ9NRY4.
PRIDEQ9NRY4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000404338; ENSP00000385720; ENSG00000160007.
GeneID2909.
KEGGhsa:2909.
UCSCuc010ekv.3. human.

Organism-specific databases

CTD2909.
GeneCardsGC19P047422.
H-InvDBHIX0015264.
HGNCHGNC:4591. ARHGAP35.
HPACAB037311.
MIM605277. gene.
neXtProtNX_Q9NRY4.
PharmGKBPA28988.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG241832.
HOVERGENHBG051844.
InParanoidQ9NRY4.
KOK05732.
OMAVLYRTRC.
OrthoDBEOG779NWX.
TreeFamTF324451.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
SignaLinkQ9NRY4.

Gene expression databases

BgeeQ9NRY4.
CleanExHS_GRLF1.
GenevestigatorQ9NRY4.

Family and domain databases

Gene3D1.10.555.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR002713. FF_domain.
IPR027417. P-loop_NTPase.
IPR008936. Rho_GTPase_activation_prot.
IPR000198. RhoGAP_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamPF01846. FF. 1 hit.
PF00071. Ras. 1 hit.
PF00620. RhoGAP. 1 hit.
[Graphical view]
SMARTSM00441. FF. 4 hits.
SM00324. RhoGAP. 1 hit.
[Graphical view]
SUPFAMSSF48350. SSF48350. 1 hit.
SSF52540. SSF52540. 2 hits.
SSF81698. SSF81698. 1 hit.
PROSITEPS51676. FF. 4 hits.
PS50238. RHOGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSARHGAP35. human.
EvolutionaryTraceQ9NRY4.
GeneWikiGRLF1.
GenomeRNAi2909.
NextBio11533.
PROQ9NRY4.
SOURCESearch...

Entry information

Entry nameRHG35_HUMAN
AccessionPrimary (citable) accession number: Q9NRY4
Secondary accession number(s): A7E2A4, Q14452, Q9C0E1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2003
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM